草鱼主要过敏原小清蛋白亚型纯化鉴定及加工对过敏原影响的研究
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摘要
鱼类是食物的主要过敏原之一,主要过敏原蛋白为小清蛋白,是一个分子量10-12KDa的酸性钙结合蛋白。目前国外有很多关于鳕鱼、鲑鱼、沙丁鱼等海水鱼过敏原的报道,国内也有一些关于淡水鱼的报道,但是没有关于草鱼的报道。草鱼是我国主要消费的淡水鱼之一。本研究分离纯化了草鱼主要过敏原小清蛋白,制备了用于ELISA检测的兔抗小清蛋白多克隆抗体,研究了热加工对小清蛋白抗原性、变应原性及消化稳定性的影响,建立了美拉德反应调控小清蛋白抗原性的回归模型,纯化、鉴定并分析了草鱼小清蛋白的三个亚型,研究了鱼糜产品的潜在致敏性,填补了国内关于草鱼过敏原研究的空白。
1.草鱼小清蛋白分离纯化及ELISA检测方法的建立。从草鱼鱼肉中分离纯化了小清蛋白,制备了兔抗草鱼小清蛋白多克隆抗体。测定了该抗体用于ELISA实验的条件和标准曲线。分析了兔抗草鱼小清蛋白多克隆抗体和鲤鱼、鲫鱼、鲢鱼及武昌鱼的交叉反应性,结果表明这5种淡水鱼中小清蛋白有高度同源性。收集了鱼过敏患者血清,根据血清收集时间制备了两批血清池用于后续小清蛋白IgE结合能力检测。
2.热加工对草鱼小清蛋白抗原性、变应原性及消化稳定性的影响。结果表明,80和100℃热处理在90min内使白肉中小清蛋白的抗原性及变应原性升高,65℃热处理使白肉的变应原性降低。在相同热处理时间,随着温度的升高红肉的抗原性和变应原性降低。蒸、煮、高压及烤四种热加工方式对草鱼鱼肉中小清蛋白有一定影响。高压(121℃,0.15MPa)处理30min对鱼肉中小清蛋白影响最大,小清蛋白更易被消化,抗原性及变应原性显著降低。反之,100℃烘烤使小清蛋白抗原性升高,且模拟胃肠消化后小清蛋白的抗原性及变应原性均高于对照组。
3.美拉德反应条件对小清蛋白抗原性和变应原性的影响。建立了草鱼小清蛋白与麦芽糖美拉德反应中抗原性与反应条件的关系的预测模型,研究了美拉德反应条件对小清蛋白抗原性的影响。在研究范围内,反应温度对小清蛋白-麦芽糖的抗原性影响最大。以小清蛋白的抗原性为响应值优化出了获得低抗原性的小清蛋白-麦芽糖的美拉德反应条件,在此条件下得到的小清蛋白-麦芽糖的抗原性的预测值为0.276μg/mL没有发生美拉德反应的小清蛋白的抗原性为26.54μg/mL说明美拉德反应显著降低了小清蛋白的抗原性。在此反应条件制备小清蛋白-麦芽糖,其IgE结合能力显著降低。
4.小清蛋白亚型分离及性质分析。采用高效液相色谱从凝胶层析得到的小清蛋白中分离出三种小清蛋白亚型,命名为PVⅠ、PVⅡ和PVⅢ,测定了分子量和氨基酸序列。采用ELISA法分析小清蛋白亚型的IgG和IgE结合能力,IgE结合能力最强的为PVⅡ,且PVⅡ在草鱼小清蛋白中含量最高,这说明PVⅡ是主要过敏原。经过胃蛋白酶和胰蛋白酶消化后,只有PVⅠ仍然具有较高的IgE结合能力。PVⅠ之所以保留部分IgE结合能力,是因为PVⅠ有一部分没有被胃蛋白酶消化。经过热处理,PVⅡ和PVⅢ分子量分布、lgG及IgE结合能力基本保持稳定。加热时间为1h,热处理温度高于70℃时,或者热处理温度99℃,加热时间大于lOmin时,PVI被分解,这导致了其IgG及IgE结合能力下降。
5.鱼糜制品潜在致敏性分析。结果表明,-20、-40、-60℃冻藏14周草鱼白肉中小清蛋白含量和抗原性没有明显变化。鱼糜漂洗过程中,第1次的漂洗水中含有大量的小清蛋白,2-5次漂洗的漂洗水中小清蛋白含量逐渐减少,第6次漂洗的漂洗水中小清蛋白基本不可见。采用兔抗小清蛋白抗体测定,十种鱼糜产品除了2-1和7-3,其余的样品中小清蛋白含量均小于0.125μg/mL,2-1和7.3两个样品中小清蛋白含量在0.125-0.25μg/mL之间：采用人血清池测定,10种鱼糜产品的ELISA检测值小于0.1785,小清蛋白含量范围为0.001-0.1μg/mL。
Fish is one of the major food allergen, and parvalbumin is the main allergen in fish. Parvalbumin is an acidic calcium-binding protein with a molecular weight of10-12KDa. Parvalbumin was reported inseveral kinds of sea fish species, such as cod, salmon and pilchard, and it was also reported in some freshwater fish in China, but there was no research about grass carp, one of the most frequently consumed freshwater fish in china. This study purified the main allergen in grass carp, and prepared the rabbit anti-parvalbumin antibody. This study also investigated the effect of processing methods on the antigenicity, allergenicity and digestibility of parvalbumin. The effect of Maillard reaction on the antigenicity of parvalbumin was studied. Parvalbumin isotypes were purified and characterized. And the pertential allergenicity of surimi products was evaluated in this study.
1. Purification of parvalbumin from grass carp and establishment of ELISA methods. Heat treatment and Gel filtration were used to purify parvalbumin from grass carp muscle. The fractions with high IgG-binding were collected. Anti-grass carp parvalbumin antibody was produced in rabbit and then used in ELISA test. The allergen coated concentration was2μg/mL and the sera was diluted160000times in ELISA. The cross reactivity between the sera and carp, crucian, silver carp and bream were investigated, and the results revealed high cross reactivity between them. Different sera from fish allergic patients were collected and used as sera pool to test the IgE-binding capactity of parvalbumin.
2. Effects of thermal processing on the antigenicity, allergenicity and digestibility of parvalbumin. Heat treatment caused higher antigenicity and allergenicity of white muscle when heated at80and100℃within90min. However, heat treatment at65℃was able to decrease the allergenicity of white muscle as the heating time increased. For the dark muscle, the antigenicity and allergenicity decreased with the increasing temperature. The effects of steam, boil, high peressure and bake on parvalbumin were different. High pressure (121℃,0.15MPa) was the most effective method to control the antigenicity of parvalbumin, and the parvalbumin in the grass carp muscle which treated by high pressure was more sensitive to digestion and the antigenicity and allergenicity of parvalbumin were decreased significantly during digestion. The water used in boil and the water obtained from steam and high pressure treated grass carp muscle contained parvalbumin, which can cause fish allergy.
3.Effect of maillard reaction condition on the antigenicity and allergenicity of parvalbumin. A model for predicting antigenicity of PV and maltose Maillard reaction products was established. On the field of conditions studied, temperature had the most important effect on the antigenicity of PV. The predicted antigenicity of PV was reduced from26.54μg mL-1to0.276μg mL-1under the optimal Maillard reaction condition. Maillard reaction lead significantly suppressed IgE binding to PV and it was an effective method to control the major allergen of grass carp. After Maillard reaction, the essential amino acid content of PV decreased14.50%and the non-essential amino acid content of PV decreased23.21%.
4. Purification andcharacterization of parvalbuminisotypes from grass carp. Three PV isotypes were purified and denoted as PⅥ, PⅦ and PⅧ. The molecular weights of PⅥ, PⅦ and PⅧ were determined to be11.968,11.430and11.512kDa, respectively. PⅥ showed74%sequence similarity with PV isotype4a from Daniorerio while PⅦ and PⅧ showed46%sequence similarities with PⅤ isotypes from Hypophthalmichthy smolitrix, respectively. PVII showed the highest IgG-binding and IgE-binding as well as the highest content among the three isotypes. Therefore, PⅦ was demonstrated to be the main allergen. However, PⅦ was liable to gastrointestinal enzymes compared with PⅥ, which was resistant to pepsin digestion. The IgE-binding capacity of pepsin digested PⅥ was significantly higher than other digested PV isotypes, and the undigested PVI in the peptic digest was responsible for its IgE-binding capacity. After thermal treatment, the structure, antigenicity and allergenicity of PⅦ and PⅧ were stable. But PVI was degraded when the heat time was1h, and the heat temperature was higher than70℃or when the heat temperature was99℃, and the heat time was longer than10min. And the degradation of PVI may be was the reason for the dereased IgG and IgE binding capacities.
5. Analysis of the potential allergic of surimi products. The content and antigenicity of parvalbumin in grass carp white muscle were stable when stored at-20,-40,-60℃in14weeks. The content of parvalbumin decreased significantly during the surimi processing procedure. Rabbit anti-parvalbumin antibody and human sera pool were used to test parvalbumin in different concentration, and the results were used as a standard to measure the parvalbumin content in ten kinds of surimi products. The parvalbumin content of the surimi products were lower than0.125μg/mL except for2-1and7-3when tested by rabbit anti-parvalbumin antibody. The parvalbumin content of the surimi products were in the range of0.001-0.1μg/mL when tested by the human sera pool.
1.草鱼小清蛋白分离纯化及ELISA检测方法的建立。从草鱼鱼肉中分离纯化了小清蛋白,制备了兔抗草鱼小清蛋白多克隆抗体。测定了该抗体用于ELISA实验的条件和标准曲线。分析了兔抗草鱼小清蛋白多克隆抗体和鲤鱼、鲫鱼、鲢鱼及武昌鱼的交叉反应性,结果表明这5种淡水鱼中小清蛋白有高度同源性。收集了鱼过敏患者血清,根据血清收集时间制备了两批血清池用于后续小清蛋白IgE结合能力检测。
2.热加工对草鱼小清蛋白抗原性、变应原性及消化稳定性的影响。结果表明,80和100℃热处理在90min内使白肉中小清蛋白的抗原性及变应原性升高,65℃热处理使白肉的变应原性降低。在相同热处理时间,随着温度的升高红肉的抗原性和变应原性降低。蒸、煮、高压及烤四种热加工方式对草鱼鱼肉中小清蛋白有一定影响。高压(121℃,0.15MPa)处理30min对鱼肉中小清蛋白影响最大,小清蛋白更易被消化,抗原性及变应原性显著降低。反之,100℃烘烤使小清蛋白抗原性升高,且模拟胃肠消化后小清蛋白的抗原性及变应原性均高于对照组。
3.美拉德反应条件对小清蛋白抗原性和变应原性的影响。建立了草鱼小清蛋白与麦芽糖美拉德反应中抗原性与反应条件的关系的预测模型,研究了美拉德反应条件对小清蛋白抗原性的影响。在研究范围内,反应温度对小清蛋白-麦芽糖的抗原性影响最大。以小清蛋白的抗原性为响应值优化出了获得低抗原性的小清蛋白-麦芽糖的美拉德反应条件,在此条件下得到的小清蛋白-麦芽糖的抗原性的预测值为0.276μg/mL没有发生美拉德反应的小清蛋白的抗原性为26.54μg/mL说明美拉德反应显著降低了小清蛋白的抗原性。在此反应条件制备小清蛋白-麦芽糖,其IgE结合能力显著降低。
4.小清蛋白亚型分离及性质分析。采用高效液相色谱从凝胶层析得到的小清蛋白中分离出三种小清蛋白亚型,命名为PVⅠ、PVⅡ和PVⅢ,测定了分子量和氨基酸序列。采用ELISA法分析小清蛋白亚型的IgG和IgE结合能力,IgE结合能力最强的为PVⅡ,且PVⅡ在草鱼小清蛋白中含量最高,这说明PVⅡ是主要过敏原。经过胃蛋白酶和胰蛋白酶消化后,只有PVⅠ仍然具有较高的IgE结合能力。PVⅠ之所以保留部分IgE结合能力,是因为PVⅠ有一部分没有被胃蛋白酶消化。经过热处理,PVⅡ和PVⅢ分子量分布、lgG及IgE结合能力基本保持稳定。加热时间为1h,热处理温度高于70℃时,或者热处理温度99℃,加热时间大于lOmin时,PVI被分解,这导致了其IgG及IgE结合能力下降。
5.鱼糜制品潜在致敏性分析。结果表明,-20、-40、-60℃冻藏14周草鱼白肉中小清蛋白含量和抗原性没有明显变化。鱼糜漂洗过程中,第1次的漂洗水中含有大量的小清蛋白,2-5次漂洗的漂洗水中小清蛋白含量逐渐减少,第6次漂洗的漂洗水中小清蛋白基本不可见。采用兔抗小清蛋白抗体测定,十种鱼糜产品除了2-1和7-3,其余的样品中小清蛋白含量均小于0.125μg/mL,2-1和7.3两个样品中小清蛋白含量在0.125-0.25μg/mL之间：采用人血清池测定,10种鱼糜产品的ELISA检测值小于0.1785,小清蛋白含量范围为0.001-0.1μg/mL。
Fish is one of the major food allergen, and parvalbumin is the main allergen in fish. Parvalbumin is an acidic calcium-binding protein with a molecular weight of10-12KDa. Parvalbumin was reported inseveral kinds of sea fish species, such as cod, salmon and pilchard, and it was also reported in some freshwater fish in China, but there was no research about grass carp, one of the most frequently consumed freshwater fish in china. This study purified the main allergen in grass carp, and prepared the rabbit anti-parvalbumin antibody. This study also investigated the effect of processing methods on the antigenicity, allergenicity and digestibility of parvalbumin. The effect of Maillard reaction on the antigenicity of parvalbumin was studied. Parvalbumin isotypes were purified and characterized. And the pertential allergenicity of surimi products was evaluated in this study.
1. Purification of parvalbumin from grass carp and establishment of ELISA methods. Heat treatment and Gel filtration were used to purify parvalbumin from grass carp muscle. The fractions with high IgG-binding were collected. Anti-grass carp parvalbumin antibody was produced in rabbit and then used in ELISA test. The allergen coated concentration was2μg/mL and the sera was diluted160000times in ELISA. The cross reactivity between the sera and carp, crucian, silver carp and bream were investigated, and the results revealed high cross reactivity between them. Different sera from fish allergic patients were collected and used as sera pool to test the IgE-binding capactity of parvalbumin.
2. Effects of thermal processing on the antigenicity, allergenicity and digestibility of parvalbumin. Heat treatment caused higher antigenicity and allergenicity of white muscle when heated at80and100℃within90min. However, heat treatment at65℃was able to decrease the allergenicity of white muscle as the heating time increased. For the dark muscle, the antigenicity and allergenicity decreased with the increasing temperature. The effects of steam, boil, high peressure and bake on parvalbumin were different. High pressure (121℃,0.15MPa) was the most effective method to control the antigenicity of parvalbumin, and the parvalbumin in the grass carp muscle which treated by high pressure was more sensitive to digestion and the antigenicity and allergenicity of parvalbumin were decreased significantly during digestion. The water used in boil and the water obtained from steam and high pressure treated grass carp muscle contained parvalbumin, which can cause fish allergy.
3.Effect of maillard reaction condition on the antigenicity and allergenicity of parvalbumin. A model for predicting antigenicity of PV and maltose Maillard reaction products was established. On the field of conditions studied, temperature had the most important effect on the antigenicity of PV. The predicted antigenicity of PV was reduced from26.54μg mL-1to0.276μg mL-1under the optimal Maillard reaction condition. Maillard reaction lead significantly suppressed IgE binding to PV and it was an effective method to control the major allergen of grass carp. After Maillard reaction, the essential amino acid content of PV decreased14.50%and the non-essential amino acid content of PV decreased23.21%.
4. Purification andcharacterization of parvalbuminisotypes from grass carp. Three PV isotypes were purified and denoted as PⅥ, PⅦ and PⅧ. The molecular weights of PⅥ, PⅦ and PⅧ were determined to be11.968,11.430and11.512kDa, respectively. PⅥ showed74%sequence similarity with PV isotype4a from Daniorerio while PⅦ and PⅧ showed46%sequence similarities with PⅤ isotypes from Hypophthalmichthy smolitrix, respectively. PVII showed the highest IgG-binding and IgE-binding as well as the highest content among the three isotypes. Therefore, PⅦ was demonstrated to be the main allergen. However, PⅦ was liable to gastrointestinal enzymes compared with PⅥ, which was resistant to pepsin digestion. The IgE-binding capacity of pepsin digested PⅥ was significantly higher than other digested PV isotypes, and the undigested PVI in the peptic digest was responsible for its IgE-binding capacity. After thermal treatment, the structure, antigenicity and allergenicity of PⅦ and PⅧ were stable. But PVI was degraded when the heat time was1h, and the heat temperature was higher than70℃or when the heat temperature was99℃, and the heat time was longer than10min. And the degradation of PVI may be was the reason for the dereased IgG and IgE binding capacities.
5. Analysis of the potential allergic of surimi products. The content and antigenicity of parvalbumin in grass carp white muscle were stable when stored at-20,-40,-60℃in14weeks. The content of parvalbumin decreased significantly during the surimi processing procedure. Rabbit anti-parvalbumin antibody and human sera pool were used to test parvalbumin in different concentration, and the results were used as a standard to measure the parvalbumin content in ten kinds of surimi products. The parvalbumin content of the surimi products were lower than0.125μg/mL except for2-1and7-3when tested by rabbit anti-parvalbumin antibody. The parvalbumin content of the surimi products were in the range of0.001-0.1μg/mL when tested by the human sera pool.
引文
[1]Rona, R.J., Keil, T., Summers, C., et al., The prevalence of food allergy:A meta-analysis. Journal of Allergy and Clinical Immunology,2007.120(3),638-646.
[2]Savage, J.H., Matsui, E.C., Skripak, J.M., et al., The natural history of egg allergy. Journal of Allergy and Clinical Immunology,2007.120(6),1413-1417.
[3]Skripak, J.M., Matsui, E.C., Mudd, K., et al., The natural history of IgE-mediated cow's milk allergy. Journal of Allergy and Clinical Immunology,2007.120(5),1172-1177.
[4]董金和,陈恩友,袁晓初,等,2013中国渔业统计年鉴.中国农业出版社,2013.5,27-31.
[5]Cho, J.H. and I.H. Kim, Fish meal-nutritive value. Journal of Animal Physiology and Animal Nutrition,2011.95(6),685-692.
[6]Beveridge, M.C.M., Thilsted, S.H., Phillips, M.J., et al., Meeting the food and nutrition needs of the poor:The role of fish and the opportunities and challenges emerging from the rise of aquaculturea. Journal of Fish Biology,2013.83(4),1067-1084.
[7]Sharp, M. and A. Lopata, Fish Allergy:In Review. Clinical Reviews in Allergy & Immunology, 2013,1-14.
[8]Douglas, J.D., McSharry, C., Blaikie, L., et al., Occupational asthma caused by automated salmon processing. The Lancet,1995.346(8977),737-740.
[9]Lopata, A. and M. Jeebhay, Airborne Seafood Allergens as a Cause of Occupational Allergy and Asthma. Current Allergy and Asthma Reports,2013.13(3),288-297.
[10]Dahlman-Hoglund, A., Renstrom, A., Larsson, Per H., et al., Salmon allergen exposure, occupational asthma, and respiratory symptoms among salmon processing workers. American Journal of Industrial Medicine,2012.55(7),624-630.
[11]Van Do, T., Hordvik, I. Endresen, C., et al., Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M. Molecular Immunology,2005. 42(3),345-353.
[12]Elsayed, S.M. and K. Aas, Characterization of a Major Allergen (Cod). Chemical Composition and Immunological Properties. International Archives of Allergy and Immunology,1970.38(5), 536-548.
[13]Perez-Gordo, M., Lin, J., Bardina, L., et al., Epitope mapping of the major allergen from Atlantic cod in Spanish population reveals different IgE-binding patterns. Molecular Nutrition & Food Research,2013.57(7),1283-1290.
[14]Hildebrandt, S. and E.A.E. Garber, Effects of processing on detection and quantification of the parvalbumin gene in Atlantic salmon (Salmo salar). Food Chemistry,2010.119(1),75-80.
[15]Beale, J.E., M.F. Jeebhay, and A.L. Lopata, Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax. Molecular Immunology,2009.46(15),2985-2993.
[16]Griesmeier, U., Vazquez-Cortes, S., Bublin, M., et al., Expression levels of parvalbumins determine allergenicity of fish species. Allergy,2010.65(2),191-198.
[17]肖有明,鲤鱼小清蛋白的抗原性研究,2008,南昌大学.
[18]张强,赵郭存,邹菊,等,鳙鱼变应原小清蛋白单克隆抗体制备及鉴定.中国公共卫生,2012.28(4),548-550.
[19]汪宁,王锡昌,蔡秋凤,等,鱼类肌肉中过敏蛋白的检测与分析.厦门大学学报(自然科学版),2008.47(z2),141-145.
[20]李欣,陈红兵,牛奶过敏原表位研究进展.食品科学,2006.27(11),592-598.
[21]佟平,高金燕,陈红兵,鸡蛋清中主要过敏原的研究进展.食品科学,2007.28(8),565-568.
[22]吴海明,胡志和,海虾过敏原的研究进展.食品研究与开发,2010.31(7),167-173.
[23]Sampson, H.A., Update on food allergy. Journal of Allergy and Clinical Immunology,2004. 113(5),805-819.
[24]Viquez, O.M., K.N. Konan, and H.W. Dodo, Structure and organization of the genomic clone of a major peanut allergen gene, Ara h 1. Molecular Immunology,2003.40(9),565-571.
[25]田荣欢,刘迪秋,陈朝银,等,核桃分子生物学研究进展.生物技术通报,2010(11),19-24.
[26]朱倩倩,吴序栎,肖杰,等,腰果过敏原Ana o2结构及抗原表位预测.食品与生物技术学报,2012.31(2),141-145.
[27]赵郭存,张强,杨波,等,榛子主要过敏原Cor h 1单克隆抗体识别抗原表位区域的确定.食品安全质量检测学报,2012.3(4),264-269.
[28]周细平,李宏,蒿属花粉症合并板栗过敏性休克1例.中华临床免疫和变态反应杂志,2011.05(2),148-150,Ⅲ.
[29]毛炜翔,高金燕,陈红兵,小麦过敏研究进展.食品科学,2007.28(8),559-562.
[30]BaagOE, K.H., First northern congress of allergy. Allergy,1948.1(2),123-126.
[31]Eggesb(?), M., Halvorsen, R., Tambs, K., et al., Prevalence of parentally perceived adverse reactions to food in young children. Pediatric Allergy and Immunology,1999.10(2),122-132.
[32]Kajosaari, M., Food allergy in finnish children aged 1 to 6 years. Acta Paediatrica,1982.71(5), 815-819.
[33]Crespo, J.F., Pascual, C., Dominguez, C., et al., Allergic reactions associated with airborne fish particles in IgE-mediated fish hypersensitive patients. Allergy,1995.50(3),257-261.
[34]Sicherer, S.H., A. Munoz-Furlong, and H.A. Sampson, Prevalence of seafood allergy in the United States determined by a random telephone survey. Journal of Allergy and Clinical Immunology,2004.114(1),159-165.
[35]Kandyil, R.M. and C.M. Davis, Shellfish allergy in children. Pediatric Allergy and Immunology, 2009.20(5),408-414.
[36]Connett, GJ., Gerez, I., Cabrera-Morales, E.A., et al., A Population-Based Study of Fish Allergy in the Philippines, Singapore and Thailand. International Archives of Allergy and Immunology,2012.159(4),384-390.
[37]Vierk, K.A., Koehler, K.M., Fein, S.B., et al., Prevalence of self-reported food allergy in American adults and use of food labels. Journal of Allergy and Clinical Immunology,2007. 119(6),1504-1510.
[38]Ben-Shoshan, M., Harrington, D.W., Soller, L., et al., A population-based study on peanut, tree nut, fish, shellfish, and sesame allergy prevalence in Canada. Journal of Allergy and Clinical Immunology,2010.125(6),1327-1335.
[39]Thong, B.Y., Cheng, Y.K., Leong, K.P., et al., Immediate food hypersensitivity among adults attending a clinical immunology/allergy centre in Singapore. Singapore medical journal,2007. 48(3),236-240.
[40]Zinn, C., Lopata, A., Visser, M., et al., The spectrum of allergy to South African bony fish (Teleosti). Evaluation by double-blind, placebo-controlled challenge. South African Medical Journal,1997.87(2),146-152.
[41]Bang, K.M., E. Hnizdo, and B. Doney, Prevalence of asthma by industry in the US population: A study of 2001 NHIS data. American Journal of Industrial Medicine,2005.47(6),500-508.
[42]Jeebhay, M.F., Robins, T.G., Lehrer, S.B., et al., Occupational seafood allergy:a review. Occupational and Environmental Medicine,2001.58(9),553-562.
[43]Jeebhay, M.F., and Quirce, S., Occupational allergy and asthma among salt water fish processing workers. American Journal of Industrial Medicine,2008.51(12),899-910.
[44]Untersmayr, E., Poulsen, L.K., Platzer, M.H., et al., The effects of gastric digestion on codfish allergenicity. Journal of Allergy and Clinical Immunology,2005.115(2),377-382.
[45]James, J. and Crespo J., Allergic reactions to foods by inhalation. Current Allergy and Asthma Reports,2007.7(3),167-174.
[46]Jeebhay, M.F. and Cartier A., Seafood workers and respiratory disease:an update. Current Opinion in Allergy and Clinical Immunology,2010.10(2),104-113 10.1097/ACI.0b013e3283373bd0.
[47]Bardana Jr, E.J., and Emil J., Occupational asthma. Journal of Allergy and Clinical Immunology,2008.121(2, Supplement 2), S408-S411.
[48]Jeebhay, M.F. and Quirce S., Occupational asthma in the developing and industrialised world:a review [State of the Art Series. Occupational lung disease in high-and low-income countries, Edited by M. Chan-Yeung. Number 1 in the series] The International Journal of Tuberculosis and Lung Disease,2007.11(2),122-133.
[49]Taylor, A.V., Swanson, M.C., Jones, R.T., et al., Detection and quantitation of raw fish aeroallergens from an open-air fish market. Journal of Allergy and Clinical Immunology,2000. 105(1, Part1),166-169.
[50]Chehade, M., Nowak-Wegrzyn, A., Kaufman, S.S., et al., De Novo Food Allergy After Intestinal Transplantation:A Report of Three Cases. Journal of Pediatric Gastroenterology and Nutrition,2004.38(5),545-547.
[51]Asero, R. and Antonicelli L., Does Sensitization to Foods in Adults Occur Always in the Gut? International Archives of Allergy and Immunology,2011.154(1),6-14.
[52]van der Ventel, M.L., Nieuwenhuizen, N.E., Kirstein, F., et al., Differential responses to natural and recombinant allergens in a murine model of fish allergy. Molecular Immunology,2011. 48(4),637-646.
[53]Lopata, A.L. and Lehrer S.B., New insights into seafood allergy. Current Opinion in Allergy and Clinical Immunology,2009.9(3),270-277 10.1097/ACI.0b013e32832b3e6f.
[54]Nieuwenhuizen, N., Lopata, A.L., Jeebhay, M.F., et al., Exposure to the fish parasite Anisakis causes allergic airway hyperreactivity and dermatitis. Journal of Allergy and Clinical Immunology,2006.117(5),1098-1105.
[55]Bernardini, R., Mistrelio, G., Novembre, E., et al., Cross-reactivity between IgE-binding proteins from Anisakis simplex and Dermatophagoides pteronyssinus. International journal of immunopathology and pharmacology,2005.18(4),671-675.
[56]Yong Jeong, K., Hong, C.S. and Yong T.S., Allergenic Tropomyosins and Their Cross-Reactivities. Protein and Peptide Letters,2006.13(8),835-845.
[57]Aas, K. and Elsayed S.M., Characterization of a major allergen (cod):Effect of enzymic hydrolysis on the allergenic activity. Journal of Allergy,1969.44(6),333-343.
[58]Aas, K. and Lundkvist U., The radioallergosorbent test with a purified allergen from codfish. Clinical & Experimental Allergy,1973.3(3),255-261.
[59]Lehky, P., Blum, H.E., Stein, E.A., et al., Isolation and Characterization of Parvalbumins from the Skeletal Muscle of Higher Vertebrates. Journal of Biological Chemistry,1974.249(13), 4332-4334.
[60]Perez-Gordo, M., Lin, J., Bardina, L., et al., Epitope Mapping of Atlantic Salmon Major Allergen by Peptide Microarray Immunoassay. International Archives of Allergy and Immunology,2012.157(1),31-40.
[61]Cai, Q.F., Liu, G.M., Li T., et al., Purification and Characterization of Parvalbumins, the Major Allergens in Red Stingray (Dasyatis akajei). Journal of Agricultural and Food Chemistry,2010. 58(24),12964-12969.
[62]Guo, F.F., Kubota H., and Shiomi K., Purification, immunological properties and molecular cloning of two allergenic parvalbumins from the crimson sea bream, Evynnis japonica. Food Chemistry,2012.132(2),835-840.
[63]Hamada, Y., Tanaka, H., Sato, A., et al., Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin. Allergology International,2004.53(3),271-278.
[64]Liu, G.M., Wang N., Cai Q.F, et al., Purification and characterization of parvalbumins from silver carp (Hypophthalmichthymolitrix). Journal of the Science of Food and Agriculture,2010. 90:1034-1040
[65]Van Do, T., Hordvik, I., Endresen, C, et al., The major allergen (parvalbumin) of codfish is encoded by at least two isotypic genes:cDNA cloning, expression and antibody binding of the recombinant allergens. Molecular Immunology,2003.39(10),595-602.
[66]Ma, Y., Griesmeier, U., Susani, M., et al., Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp. Molecular Nutrition & Food Research, 2008.52(S2), S196-S207.
[67]Kuehn, A., Scheuermann, T., Hilger, C., et al., Important Variations in Parvalbumin Content in Common Fish Species:A Factor Possibly Contributing to Variable Allergenicity. International Archives of Allergy and Immunology,2010.153(4),359-366.
[68]Makinen-Kiljunen, Kiistala, S.R. and Varjonen E., Severe reactions from roe without concomitant fish allergy. Annals of Allergy, Asthma & Immunology,2003.91(4),413-416.
[69]Gajewski, K.G and Hsieh Y.H.P., Monoclonal Antibody Specific to a Major Fish Allergen: Parvalbumin. Journal of Food Protection,2009.72(4),818-825.
[70]Elsayed, S. and Apold J., Immunochemical Analysis of Cod Fish Allergen M:Locations of the Immunoglobulin Binding Sites as Demonstrated by the Native and Synthetic Peptides. Allergy, 1983.38(7),449-459.
[71]Untersmayr, E., Szalai, K., Riemer, A.B., et al., Mimotopes identify conformational epitopes on parvalbumin, the major fish allergen. Molecular Immunology,2006.43(9),1454-1461.
[72]Yoshida, S., Ichimura, A. and Shiomi K., Elucidation of a major IgE epitope of Pacific mackerel parvalbumin. Food Chemistry,2008.111(4),857-861.
[73]Sicherer, S.H. and Sampson H.A., Food allergy. Journal of Allergy and Clinical Immunology, 2010.125(2, Supplement 2), S116-S125.
[74]Lopata, A.L., O'Hehir R.E., and Lehrer S.B., Shellfish allergy. Clinical & Experimental Allergy, 2010.40(6),850-858.
[75]Escudero, R., Gamboa, P.M., Anton, J., et al., Food allergy due to trout roe. Journal of investigational allergology & clinical immunology,2007.17(5),346-347.
[76]Perez-Gordo, M., Sanchez-Garcia, S., Cases, B., et al., Identification of vitellogenin as an allergen in Beluga caviar allergy. Allergy,2008.63(4),479-480.
[77]Hamada, Y, Y. Nagashima, and Shiomi K., Identification of Collagen as a New Fish Allergen. Bioscience, Biotechnology, and Biochemistry,2001.65(2),285-291.
[78]Sakaguchi, M., Toda, M., Ebihara, T., et al., IgE antibody to fish gelatin (type I collagen) in patients with fish allergy. Journal of Allergy and Clinical Immunology,2000.106(3),579-584.
[79]Taylor, S.L., Kabourek, J.L. and Hefle S.L., Fish Allergy:Fish and Products Thereof. Journal of Food Science,2004.69(8), R175-R180.
[80]Weber, P., Steinhart, H. and Paschke A., Competitive Indirect ELISA for the Determination of Parvalbumins from Various Fish Species in Food Grade Fish Gelatins and Isinglass with PARV-19 Anti-parvalbumin Antibodies. Journal of Agricultural and Food Chemistry,2009. 57(23),11328-11334.
[81]Audicana, M.T. and Kennedy, M.W., Anisakis simplex:from Obscure Infectious Worm to Inducer of Immune Hypersensitivity. Clinical Microbiology Reviews,2008.21(2),360-379.
[82]Kirstein, F., Horsnell, W.G.C., Nieuwenhuizen, N., et al., Anisakis pegreffii-Induced Airway Hyperresponsiveness Is Mediated by Gamma Interferon in the Absence of Interleukin-4 Receptor Alpha Responsiveness. Infection and Immunity,2010.78(9),4077-4086.
[83]Koppelman, S.J., Nordlee, J.A., Lee, P.W., et al., Parvalbumin in fish skin-derived gelatin:is there a risk for fish allergic consumers? Food Additives & Contaminants:Part A,2012.29(9), 1347-1355.
[84]Shibahara, Y., Uesaka, Y., Wang J. et al., A sensitive enzyme-linked immunosorbent assay for the determination offish protein in processed foods. Food Chemistry,2013.136(2),675-681.
[85]Lee, P.W., Nordlee, J.A., Koppelman, S.J., et al., Evaluation and Comparison of the Species-Specificity of 3 Antiparvalbumin IgG Antibodies. Journal of Agricultural and Food Chemistry,2011.59(23),12309-12316.
[86]董金和,陈恩友,袁晓初,等,2013中国渔业统计年鉴.中国农业出版社,2013.5,23.
[87]董金和,陈恩友,袁晓初,等,2013中国渔业统计年鉴.中国农业出版社,2013.5,96.
[88]Houska, M., Setinova, I. and Kucera P., Food Allergens and Processing:A Review of Recent Results, in Advances in Food Process Engineering Research and Applications, S. Yanniotis, et al., Editors.2013, Springer US. p.291-337.
[89]刘一璇,林洪,吴丽莎,等,加工方式对刀额新对虾主要过敏原免疫原性的影响.水产学报,2011.35(6),948-953.
[90]郑礼娜,林洪,刘一璇,等,不同热加工方式对刀额新对虾过敏原活性的影响.水产学报,2011.35(3),466-471.
[91]刘光明,余惠琳,黄秀秀,等,加工处理方式对蟹类原肌球蛋白的消化稳定性和过敏原性的影响.中国食品学报,2011.11(4),14-22.
[92]Sletten, G, Van Do, T., Lindvik, H., et al., Effects of industrial processing on the immunogenicity of commonly ingested fish species. Int Arch Allergy Immunol,2010.151(3), 223-36.
[93]Bernhisel-Broadbent, J., D. Strause, and Sampson, H.A., Fish hypersensitivity. Ⅱ:Clinical relevance of altered fish allergenicity caused by various preparation methods. J Allergy Clin Immunol,1992.90(4 Pt 1),622-9.
[94]Bernhisel-Broadbent, J., S.M. Scanlon, and Sampson, H.A., Fish hypersensitivity:Ⅰ. In vitro and oral challenge results in fish-allergic patients. Journal of Allergy and Clinical Immunology, 1992.89(3),730-737.
[95]蔡秋风,王锡昌,郭城,等,加工处理对鲢小清蛋白免疫活性的影响.水产学报,2013.37(2),297-302.
[96]李振兴,黄榕芳,吴玟静,等,热蒸加工对大菱鲆过敏原免疫原性的影响.食品安全质量检测学报,2012.3(4),279-284.
[97]Moreno, F.J., Gastrointestinal digestion of food allergens:Effect on their allergenicity. Biomedicine & Pharmacotherapy,2007.61(1),50-60.
[98]Bannon, G., What makes a food protein an allergen? Current Allergy and Asthma Reports,2004. 4(1),43-46.
[99]Dupont, D., Mandalari, G. Molle, D., et al, Comparative resistance of food proteins to adult and infant in vitro digestion models. Molecular Nutrition and Food Research,2010.54(6), 767-780.
[100]Foster, E.S., Kimber, I. and Dearman R.J., Relationship between protein digestibility and allergenicity:Comparisons of pepsin and cathepsin. Toxicology,2013.309(0),30-38.
[101]Zeece, M., Huppertz, T. and Kelly, A., Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. Innovative Food Science & Emerging Technologies,2008.9(1),62-69.
[102]Yu, H.L., Cao, M.J., Cai, Q.F., et al., Effects of different processing methods on digestibility of Scylla paramamosain allergen (tropomyosin). Food and Chemical Toxicology,2011.49(4), 791-798.
[103]Perez-Gordo, M., Cuesta-Harranz, J., Maroto, A.S., et al., Identification of sole parvalbumin as a major allergen:study of cross-reactivity between parvalbumins in a Spanish fish-allergic population. Clinical & Experimental Allergy,2011.41(5),750-758.
[104]Koppelman, S.J., Romijn, R.A., De Jongh, H.H.J., et al., Purification of Parvalbumin from Carp: A Protocol that Avoids Heat-Treatment. Journal of Food Science,2010.75(3), T49-T56.
[105]刘楚怡,薛文通,李阳,青鱼致敏蛋白的识别、热稳定性及模拟肠液消化的研究,in 2011年中国农业工程学会农产品加工及贮藏工程分会学术年会暨全国食品科学与工程博士生学术论坛、管产学研助推食品安全重庆高峰论坛论文集2011：重庆.p.394-397.
[106]Kim, K.B.W.R., Lee, S.Y., Song, E.J., et al., Effect of heat and autoclave on allergenicity of porcine serum albumin. Food Science and Biotechnology,2011.20(2),455-459.
[107]Tong, P., Gao, J.Y, Chen, H.B., et al., Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chemistry,2012.131(2), 603-610.
[108]Takahashi, K., Terada, C., Tashiro, M., et al., Effects of heat treatment and pepsin digestion on trypsin inhibitory activity and ovomucoid antigenicity of japanese quail egg white. Journal of Food Biochemistry,2003.27(5),423-434.
[109]Starkl, P., Krishnamurthy, D., Szalai, K., et al., Heating Affects Structure, Enterocyte Adsorption and Signalling, As Well as Immunogenicity of the Peanut Allergen Ara h 2. Open Allergy J,2011.4,24-34.
[110]Chatterjee, U., Mondal. G., Chakraborti, P., et al., Changes in the Allergenicity during Different Preparations of Pomfret, Hilsa, Bhetki and Mackerel Fish as Illustrated by Enzyme-Linked Immunosorbent Assay and Immunoblotting. International Archives of Allergy and Immunology, 2006.141(1),1-10.
[111]Sletten, G., Van Do, T., Lindvik, H., et al., Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species. International Archives of Allergy and Immunology,2010.151(3),223-236.
[112]Bugajska-Schretter, A., Grote, M., Vangelista, L., et al., Purification, biochemical, and immunological characterisation of a major food allergen:different immunoglobulin E recognition of the apo-and calcium-bound forms of carp parvalbumin. Gut,2000.46(5), 661-669.
[113]Gornall, A.G., Bardawill, C.J. and David M.M., Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry,1949.177(2),751-766.
[114]Arif, S.H., Jabeen, M. and Hasnain A.U., Biochemical characterization and thermostable capacity of parvalbumins:the major fish-food allergens. Journal of Food Biochemistry,2007. 31(1),121-137.
[115]Bugajska-Schretter, A., Elfman, L., Fuchs, T., et al., Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion. Journal of Allergy and Clinical Immunology,1998.101(1),67-74.
[116]Besler, M., Steinhart, H. and Paschke, A., Stability of food allergens and allergenicity of processed foods. Journal of Chromatography B:Biomedical Sciences and Applications,2001. 756(1-2),207-228.
[117]Griesmeier, U., Bublin, M., Radauer, C., et al., Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff. Molecular Nutrition & Food Research,2010.54(6), 861-869.
[118]Martos, G., Lopez-Exposito, I., Bencharitiwong, R., et al., Mechanisms underlying differential food allergy response to heated egg. Journal of Allergy and Clinical Immunology,2011.127(4), 990-997.e2.
[119]Thomas, K., Herouet-Guicheney, C., Ladics, G., et al., Evaluating the effect of food processing on the potential human allergenicity of novel proteins:International workshop report. Food and Chemical Toxicology,2007.45(7),1116-1122.
[120]黄园园,水产过敏原的模拟胃肠液消化,2009,集美大学.
[121]Shen, J.D., Cai, Q.F., Liu, G.M., et al., A comparison study of the impact of boiling and high pressure steaming on the stability of soybean trypsin inhibitor. International Journal of Food Science and Technology,2013.48(9),1877-1883.
[122]De Jongh, H.H.J., Robles, C.L., Timmerman, E., et al., Digestibility and IgE-binding of glycosylated codfish parvalbumin. BioMed Research International,2013.2013.
[123]程伟,多酚氧化酶交联牛乳a-乳白蛋白的结构变化及其消化性与过敏原性的评估,2012,南昌大学.
[124]van de Lagemaat, J., Manuel Silvan, J., Javier, M.F., et al., In vitro glycation and antigenicity of soy proteins. Food Research International,2007.40(1),153-160.
[125]Nakamura, S., Suzuki, Y., Ishikawa, E., et al., Reduction of in vitro allergenicity of buckwheat Fag e 1 through the Maillard-type glycosylation with polysaccharides. Food Chemistry,2008. 109(3),538-545.
[126]Iwan, M., Vissers, Y.M., Fiedorowicz, E., et al., Impact of Maillard Reaction on Immunoreactivity and Allergenicity of the Hazelnut Allergen Cor a 11. Journal of Agricultural and Food Chemistry,2011.59(13),7163-7171.
[127]Bu, G., Lu J., Zheng Z., et al., Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology. Journal of the Science of Food and Agriculture,2009.89(14),2428-2434.
[128]Bu G.H., Luo, Y.L., Lu, J., et al. Reduced antigenicity of β-lactoglobulin by conjugation with glucose through controlled Maillard reaction conditions. Food and Agricultural Immunology, 2010.21(2),143-156.
[129]Li, Z., Luo, Y.K., and Feng, L.G., Effects of Maillard reaction conditions on the antigenicity of a-lactalbumin and P-lactoglobulin in whey protein conjugated with maltose. European Food Research and Technology,2011.233(3),387-394.
[130]Jimenez-Saiz, R., Belloque, J., Molina, E., et al., Human Immunoglobulin E (IgE) Binding to Heated and Glycated Ovalbumin and Ovomucoid before and after in Vitro Digestion. Journal of Agricultural and Food Chemistry,2011.59(18),10044-10051.
[131]Oldfield, D.J., Singh, H., Taylor, M.W., et al., Kinetics of Denaturation and Aggregation of Whey Proteins in Skim Milk Heated in an Ultra-high Temperature (UHT) Pilot Plant. International Dairy Journal,1998,8(4),311-318.
[132]Elsayed, S. and Aas, K., Isolation of purified allergens (cod) by isoelectric focusing. Int Arch Allergy Appl Immunol,1971.40(3),428-38.
[133]Laemmli, U.K., Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature,1970.227(5259),680-685.
[134]Li, S., Offengenden M., Fentabil, M., et al., Effect of egg white fermentation with lactobacilli on IgE binding ability of egg white proteins. Food Research International,2013.52(1), 359-366.
[135]Offengenden, M., Fentabil, M. and Wu, J., N-glycosylation of ovomucin from hen egg white. Glycoconjugate Journal,2011.28(3-4),113-123.
[136]Majumder, K., Panahi, S., Kaufman, S., et al., Fried egg digest decreases blood pressure in spontaneous hypertensive rats. Journal of Functional Foods,2013.5(1),187-194.
[137]Schulten, V, Lauer,1., Scheurer, S., et al., A food matrix reduces digestion and absorption of food allergens in vivo. Molecular Nutrition & Food Research,2011.55(10),1484-1491.
[138]Chicon, R., Belloque, J., Alonso, E., et al., Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure. Food Hydrocolloids,2009.23(3),593-599.
[139]Fujita, S., Shimizu, Y., Kishimura, H., et al., In vitro digestion of major allergen in salmon roe and its peptide portion with proteolytic resistance. Food Chemistry,2012.130(3),644-650.
[140]任宏伟,胡柳,我国鱼糜制品现状及发展态势.中国水产,2010(8),25-26.
[141]张俊杰,曾庆孝,我国淡水鱼鱼糜的研究情况.食品与发酵工业,2002.28(9),57-63.
[142]Sikorski, Z. and Kolakowska, A., Changes in Proteins in Frozen Stored Fish, in Seafood Proteins, Z. Sikorski, B. Pan, and F. Shahidi, Editors.1995, Springer US. p.99-112.
[143]del Mazo, M.L., Torrejon, P., Careche, M., et al., Characteristics of the Salt-Soluble Fraction of Hake (Merluccius merluccius) Fillets Stored at -20 and -30℃. Journal of Agricultural and Food Chemistry,1999.47(4),1372-1377.
[144]Matsumoto Juichiro, J., Denaturation of Fish Muscle Proteins During Frozen Storage, in Proteins at Low Temperatures 1979, American Chemical Society, p.205-224.
[145]Jiang, S.T. and Lee, T.C., Changes in free amino acids and protein denaturation of fish muscle during frozen storage. Journal of Agricultural and Food Chemistry,1985.33(5),839-844.
[146]Lee, P.W., Nordlee, J.A., Koppelman, S.J., et al., Measuring parvalbumin levels in fish muscle tissue:Relevance of muscle locations and storage conditions. Food Chemistry,2012.135(2), 502-507.
[147]汪宁,鱼类过敏蛋白的检测分析、分离纯化和分子克隆,2008,上海海洋大学.
[148]Cai, Q.F., Wang X.C., Liu, G.M., et al., Development of a monoclonal antibody-based competitive enzyme linked-immunosorbent assay (c-ELISA) for quantification of silver carp parvalbumin. Food Control,2013.29(1),241-247.
[2]Savage, J.H., Matsui, E.C., Skripak, J.M., et al., The natural history of egg allergy. Journal of Allergy and Clinical Immunology,2007.120(6),1413-1417.
[3]Skripak, J.M., Matsui, E.C., Mudd, K., et al., The natural history of IgE-mediated cow's milk allergy. Journal of Allergy and Clinical Immunology,2007.120(5),1172-1177.
[4]董金和,陈恩友,袁晓初,等,2013中国渔业统计年鉴.中国农业出版社,2013.5,27-31.
[5]Cho, J.H. and I.H. Kim, Fish meal-nutritive value. Journal of Animal Physiology and Animal Nutrition,2011.95(6),685-692.
[6]Beveridge, M.C.M., Thilsted, S.H., Phillips, M.J., et al., Meeting the food and nutrition needs of the poor:The role of fish and the opportunities and challenges emerging from the rise of aquaculturea. Journal of Fish Biology,2013.83(4),1067-1084.
[7]Sharp, M. and A. Lopata, Fish Allergy:In Review. Clinical Reviews in Allergy & Immunology, 2013,1-14.
[8]Douglas, J.D., McSharry, C., Blaikie, L., et al., Occupational asthma caused by automated salmon processing. The Lancet,1995.346(8977),737-740.
[9]Lopata, A. and M. Jeebhay, Airborne Seafood Allergens as a Cause of Occupational Allergy and Asthma. Current Allergy and Asthma Reports,2013.13(3),288-297.
[10]Dahlman-Hoglund, A., Renstrom, A., Larsson, Per H., et al., Salmon allergen exposure, occupational asthma, and respiratory symptoms among salmon processing workers. American Journal of Industrial Medicine,2012.55(7),624-630.
[11]Van Do, T., Hordvik, I. Endresen, C., et al., Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M. Molecular Immunology,2005. 42(3),345-353.
[12]Elsayed, S.M. and K. Aas, Characterization of a Major Allergen (Cod). Chemical Composition and Immunological Properties. International Archives of Allergy and Immunology,1970.38(5), 536-548.
[13]Perez-Gordo, M., Lin, J., Bardina, L., et al., Epitope mapping of the major allergen from Atlantic cod in Spanish population reveals different IgE-binding patterns. Molecular Nutrition & Food Research,2013.57(7),1283-1290.
[14]Hildebrandt, S. and E.A.E. Garber, Effects of processing on detection and quantification of the parvalbumin gene in Atlantic salmon (Salmo salar). Food Chemistry,2010.119(1),75-80.
[15]Beale, J.E., M.F. Jeebhay, and A.L. Lopata, Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax. Molecular Immunology,2009.46(15),2985-2993.
[16]Griesmeier, U., Vazquez-Cortes, S., Bublin, M., et al., Expression levels of parvalbumins determine allergenicity of fish species. Allergy,2010.65(2),191-198.
[17]肖有明,鲤鱼小清蛋白的抗原性研究,2008,南昌大学.
[18]张强,赵郭存,邹菊,等,鳙鱼变应原小清蛋白单克隆抗体制备及鉴定.中国公共卫生,2012.28(4),548-550.
[19]汪宁,王锡昌,蔡秋凤,等,鱼类肌肉中过敏蛋白的检测与分析.厦门大学学报(自然科学版),2008.47(z2),141-145.
[20]李欣,陈红兵,牛奶过敏原表位研究进展.食品科学,2006.27(11),592-598.
[21]佟平,高金燕,陈红兵,鸡蛋清中主要过敏原的研究进展.食品科学,2007.28(8),565-568.
[22]吴海明,胡志和,海虾过敏原的研究进展.食品研究与开发,2010.31(7),167-173.
[23]Sampson, H.A., Update on food allergy. Journal of Allergy and Clinical Immunology,2004. 113(5),805-819.
[24]Viquez, O.M., K.N. Konan, and H.W. Dodo, Structure and organization of the genomic clone of a major peanut allergen gene, Ara h 1. Molecular Immunology,2003.40(9),565-571.
[25]田荣欢,刘迪秋,陈朝银,等,核桃分子生物学研究进展.生物技术通报,2010(11),19-24.
[26]朱倩倩,吴序栎,肖杰,等,腰果过敏原Ana o2结构及抗原表位预测.食品与生物技术学报,2012.31(2),141-145.
[27]赵郭存,张强,杨波,等,榛子主要过敏原Cor h 1单克隆抗体识别抗原表位区域的确定.食品安全质量检测学报,2012.3(4),264-269.
[28]周细平,李宏,蒿属花粉症合并板栗过敏性休克1例.中华临床免疫和变态反应杂志,2011.05(2),148-150,Ⅲ.
[29]毛炜翔,高金燕,陈红兵,小麦过敏研究进展.食品科学,2007.28(8),559-562.
[30]BaagOE, K.H., First northern congress of allergy. Allergy,1948.1(2),123-126.
[31]Eggesb(?), M., Halvorsen, R., Tambs, K., et al., Prevalence of parentally perceived adverse reactions to food in young children. Pediatric Allergy and Immunology,1999.10(2),122-132.
[32]Kajosaari, M., Food allergy in finnish children aged 1 to 6 years. Acta Paediatrica,1982.71(5), 815-819.
[33]Crespo, J.F., Pascual, C., Dominguez, C., et al., Allergic reactions associated with airborne fish particles in IgE-mediated fish hypersensitive patients. Allergy,1995.50(3),257-261.
[34]Sicherer, S.H., A. Munoz-Furlong, and H.A. Sampson, Prevalence of seafood allergy in the United States determined by a random telephone survey. Journal of Allergy and Clinical Immunology,2004.114(1),159-165.
[35]Kandyil, R.M. and C.M. Davis, Shellfish allergy in children. Pediatric Allergy and Immunology, 2009.20(5),408-414.
[36]Connett, GJ., Gerez, I., Cabrera-Morales, E.A., et al., A Population-Based Study of Fish Allergy in the Philippines, Singapore and Thailand. International Archives of Allergy and Immunology,2012.159(4),384-390.
[37]Vierk, K.A., Koehler, K.M., Fein, S.B., et al., Prevalence of self-reported food allergy in American adults and use of food labels. Journal of Allergy and Clinical Immunology,2007. 119(6),1504-1510.
[38]Ben-Shoshan, M., Harrington, D.W., Soller, L., et al., A population-based study on peanut, tree nut, fish, shellfish, and sesame allergy prevalence in Canada. Journal of Allergy and Clinical Immunology,2010.125(6),1327-1335.
[39]Thong, B.Y., Cheng, Y.K., Leong, K.P., et al., Immediate food hypersensitivity among adults attending a clinical immunology/allergy centre in Singapore. Singapore medical journal,2007. 48(3),236-240.
[40]Zinn, C., Lopata, A., Visser, M., et al., The spectrum of allergy to South African bony fish (Teleosti). Evaluation by double-blind, placebo-controlled challenge. South African Medical Journal,1997.87(2),146-152.
[41]Bang, K.M., E. Hnizdo, and B. Doney, Prevalence of asthma by industry in the US population: A study of 2001 NHIS data. American Journal of Industrial Medicine,2005.47(6),500-508.
[42]Jeebhay, M.F., Robins, T.G., Lehrer, S.B., et al., Occupational seafood allergy:a review. Occupational and Environmental Medicine,2001.58(9),553-562.
[43]Jeebhay, M.F., and Quirce, S., Occupational allergy and asthma among salt water fish processing workers. American Journal of Industrial Medicine,2008.51(12),899-910.
[44]Untersmayr, E., Poulsen, L.K., Platzer, M.H., et al., The effects of gastric digestion on codfish allergenicity. Journal of Allergy and Clinical Immunology,2005.115(2),377-382.
[45]James, J. and Crespo J., Allergic reactions to foods by inhalation. Current Allergy and Asthma Reports,2007.7(3),167-174.
[46]Jeebhay, M.F. and Cartier A., Seafood workers and respiratory disease:an update. Current Opinion in Allergy and Clinical Immunology,2010.10(2),104-113 10.1097/ACI.0b013e3283373bd0.
[47]Bardana Jr, E.J., and Emil J., Occupational asthma. Journal of Allergy and Clinical Immunology,2008.121(2, Supplement 2), S408-S411.
[48]Jeebhay, M.F. and Quirce S., Occupational asthma in the developing and industrialised world:a review [State of the Art Series. Occupational lung disease in high-and low-income countries, Edited by M. Chan-Yeung. Number 1 in the series] The International Journal of Tuberculosis and Lung Disease,2007.11(2),122-133.
[49]Taylor, A.V., Swanson, M.C., Jones, R.T., et al., Detection and quantitation of raw fish aeroallergens from an open-air fish market. Journal of Allergy and Clinical Immunology,2000. 105(1, Part1),166-169.
[50]Chehade, M., Nowak-Wegrzyn, A., Kaufman, S.S., et al., De Novo Food Allergy After Intestinal Transplantation:A Report of Three Cases. Journal of Pediatric Gastroenterology and Nutrition,2004.38(5),545-547.
[51]Asero, R. and Antonicelli L., Does Sensitization to Foods in Adults Occur Always in the Gut? International Archives of Allergy and Immunology,2011.154(1),6-14.
[52]van der Ventel, M.L., Nieuwenhuizen, N.E., Kirstein, F., et al., Differential responses to natural and recombinant allergens in a murine model of fish allergy. Molecular Immunology,2011. 48(4),637-646.
[53]Lopata, A.L. and Lehrer S.B., New insights into seafood allergy. Current Opinion in Allergy and Clinical Immunology,2009.9(3),270-277 10.1097/ACI.0b013e32832b3e6f.
[54]Nieuwenhuizen, N., Lopata, A.L., Jeebhay, M.F., et al., Exposure to the fish parasite Anisakis causes allergic airway hyperreactivity and dermatitis. Journal of Allergy and Clinical Immunology,2006.117(5),1098-1105.
[55]Bernardini, R., Mistrelio, G., Novembre, E., et al., Cross-reactivity between IgE-binding proteins from Anisakis simplex and Dermatophagoides pteronyssinus. International journal of immunopathology and pharmacology,2005.18(4),671-675.
[56]Yong Jeong, K., Hong, C.S. and Yong T.S., Allergenic Tropomyosins and Their Cross-Reactivities. Protein and Peptide Letters,2006.13(8),835-845.
[57]Aas, K. and Elsayed S.M., Characterization of a major allergen (cod):Effect of enzymic hydrolysis on the allergenic activity. Journal of Allergy,1969.44(6),333-343.
[58]Aas, K. and Lundkvist U., The radioallergosorbent test with a purified allergen from codfish. Clinical & Experimental Allergy,1973.3(3),255-261.
[59]Lehky, P., Blum, H.E., Stein, E.A., et al., Isolation and Characterization of Parvalbumins from the Skeletal Muscle of Higher Vertebrates. Journal of Biological Chemistry,1974.249(13), 4332-4334.
[60]Perez-Gordo, M., Lin, J., Bardina, L., et al., Epitope Mapping of Atlantic Salmon Major Allergen by Peptide Microarray Immunoassay. International Archives of Allergy and Immunology,2012.157(1),31-40.
[61]Cai, Q.F., Liu, G.M., Li T., et al., Purification and Characterization of Parvalbumins, the Major Allergens in Red Stingray (Dasyatis akajei). Journal of Agricultural and Food Chemistry,2010. 58(24),12964-12969.
[62]Guo, F.F., Kubota H., and Shiomi K., Purification, immunological properties and molecular cloning of two allergenic parvalbumins from the crimson sea bream, Evynnis japonica. Food Chemistry,2012.132(2),835-840.
[63]Hamada, Y., Tanaka, H., Sato, A., et al., Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin. Allergology International,2004.53(3),271-278.
[64]Liu, G.M., Wang N., Cai Q.F, et al., Purification and characterization of parvalbumins from silver carp (Hypophthalmichthymolitrix). Journal of the Science of Food and Agriculture,2010. 90:1034-1040
[65]Van Do, T., Hordvik, I., Endresen, C, et al., The major allergen (parvalbumin) of codfish is encoded by at least two isotypic genes:cDNA cloning, expression and antibody binding of the recombinant allergens. Molecular Immunology,2003.39(10),595-602.
[66]Ma, Y., Griesmeier, U., Susani, M., et al., Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp. Molecular Nutrition & Food Research, 2008.52(S2), S196-S207.
[67]Kuehn, A., Scheuermann, T., Hilger, C., et al., Important Variations in Parvalbumin Content in Common Fish Species:A Factor Possibly Contributing to Variable Allergenicity. International Archives of Allergy and Immunology,2010.153(4),359-366.
[68]Makinen-Kiljunen, Kiistala, S.R. and Varjonen E., Severe reactions from roe without concomitant fish allergy. Annals of Allergy, Asthma & Immunology,2003.91(4),413-416.
[69]Gajewski, K.G and Hsieh Y.H.P., Monoclonal Antibody Specific to a Major Fish Allergen: Parvalbumin. Journal of Food Protection,2009.72(4),818-825.
[70]Elsayed, S. and Apold J., Immunochemical Analysis of Cod Fish Allergen M:Locations of the Immunoglobulin Binding Sites as Demonstrated by the Native and Synthetic Peptides. Allergy, 1983.38(7),449-459.
[71]Untersmayr, E., Szalai, K., Riemer, A.B., et al., Mimotopes identify conformational epitopes on parvalbumin, the major fish allergen. Molecular Immunology,2006.43(9),1454-1461.
[72]Yoshida, S., Ichimura, A. and Shiomi K., Elucidation of a major IgE epitope of Pacific mackerel parvalbumin. Food Chemistry,2008.111(4),857-861.
[73]Sicherer, S.H. and Sampson H.A., Food allergy. Journal of Allergy and Clinical Immunology, 2010.125(2, Supplement 2), S116-S125.
[74]Lopata, A.L., O'Hehir R.E., and Lehrer S.B., Shellfish allergy. Clinical & Experimental Allergy, 2010.40(6),850-858.
[75]Escudero, R., Gamboa, P.M., Anton, J., et al., Food allergy due to trout roe. Journal of investigational allergology & clinical immunology,2007.17(5),346-347.
[76]Perez-Gordo, M., Sanchez-Garcia, S., Cases, B., et al., Identification of vitellogenin as an allergen in Beluga caviar allergy. Allergy,2008.63(4),479-480.
[77]Hamada, Y, Y. Nagashima, and Shiomi K., Identification of Collagen as a New Fish Allergen. Bioscience, Biotechnology, and Biochemistry,2001.65(2),285-291.
[78]Sakaguchi, M., Toda, M., Ebihara, T., et al., IgE antibody to fish gelatin (type I collagen) in patients with fish allergy. Journal of Allergy and Clinical Immunology,2000.106(3),579-584.
[79]Taylor, S.L., Kabourek, J.L. and Hefle S.L., Fish Allergy:Fish and Products Thereof. Journal of Food Science,2004.69(8), R175-R180.
[80]Weber, P., Steinhart, H. and Paschke A., Competitive Indirect ELISA for the Determination of Parvalbumins from Various Fish Species in Food Grade Fish Gelatins and Isinglass with PARV-19 Anti-parvalbumin Antibodies. Journal of Agricultural and Food Chemistry,2009. 57(23),11328-11334.
[81]Audicana, M.T. and Kennedy, M.W., Anisakis simplex:from Obscure Infectious Worm to Inducer of Immune Hypersensitivity. Clinical Microbiology Reviews,2008.21(2),360-379.
[82]Kirstein, F., Horsnell, W.G.C., Nieuwenhuizen, N., et al., Anisakis pegreffii-Induced Airway Hyperresponsiveness Is Mediated by Gamma Interferon in the Absence of Interleukin-4 Receptor Alpha Responsiveness. Infection and Immunity,2010.78(9),4077-4086.
[83]Koppelman, S.J., Nordlee, J.A., Lee, P.W., et al., Parvalbumin in fish skin-derived gelatin:is there a risk for fish allergic consumers? Food Additives & Contaminants:Part A,2012.29(9), 1347-1355.
[84]Shibahara, Y., Uesaka, Y., Wang J. et al., A sensitive enzyme-linked immunosorbent assay for the determination offish protein in processed foods. Food Chemistry,2013.136(2),675-681.
[85]Lee, P.W., Nordlee, J.A., Koppelman, S.J., et al., Evaluation and Comparison of the Species-Specificity of 3 Antiparvalbumin IgG Antibodies. Journal of Agricultural and Food Chemistry,2011.59(23),12309-12316.
[86]董金和,陈恩友,袁晓初,等,2013中国渔业统计年鉴.中国农业出版社,2013.5,23.
[87]董金和,陈恩友,袁晓初,等,2013中国渔业统计年鉴.中国农业出版社,2013.5,96.
[88]Houska, M., Setinova, I. and Kucera P., Food Allergens and Processing:A Review of Recent Results, in Advances in Food Process Engineering Research and Applications, S. Yanniotis, et al., Editors.2013, Springer US. p.291-337.
[89]刘一璇,林洪,吴丽莎,等,加工方式对刀额新对虾主要过敏原免疫原性的影响.水产学报,2011.35(6),948-953.
[90]郑礼娜,林洪,刘一璇,等,不同热加工方式对刀额新对虾过敏原活性的影响.水产学报,2011.35(3),466-471.
[91]刘光明,余惠琳,黄秀秀,等,加工处理方式对蟹类原肌球蛋白的消化稳定性和过敏原性的影响.中国食品学报,2011.11(4),14-22.
[92]Sletten, G, Van Do, T., Lindvik, H., et al., Effects of industrial processing on the immunogenicity of commonly ingested fish species. Int Arch Allergy Immunol,2010.151(3), 223-36.
[93]Bernhisel-Broadbent, J., D. Strause, and Sampson, H.A., Fish hypersensitivity. Ⅱ:Clinical relevance of altered fish allergenicity caused by various preparation methods. J Allergy Clin Immunol,1992.90(4 Pt 1),622-9.
[94]Bernhisel-Broadbent, J., S.M. Scanlon, and Sampson, H.A., Fish hypersensitivity:Ⅰ. In vitro and oral challenge results in fish-allergic patients. Journal of Allergy and Clinical Immunology, 1992.89(3),730-737.
[95]蔡秋风,王锡昌,郭城,等,加工处理对鲢小清蛋白免疫活性的影响.水产学报,2013.37(2),297-302.
[96]李振兴,黄榕芳,吴玟静,等,热蒸加工对大菱鲆过敏原免疫原性的影响.食品安全质量检测学报,2012.3(4),279-284.
[97]Moreno, F.J., Gastrointestinal digestion of food allergens:Effect on their allergenicity. Biomedicine & Pharmacotherapy,2007.61(1),50-60.
[98]Bannon, G., What makes a food protein an allergen? Current Allergy and Asthma Reports,2004. 4(1),43-46.
[99]Dupont, D., Mandalari, G. Molle, D., et al, Comparative resistance of food proteins to adult and infant in vitro digestion models. Molecular Nutrition and Food Research,2010.54(6), 767-780.
[100]Foster, E.S., Kimber, I. and Dearman R.J., Relationship between protein digestibility and allergenicity:Comparisons of pepsin and cathepsin. Toxicology,2013.309(0),30-38.
[101]Zeece, M., Huppertz, T. and Kelly, A., Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. Innovative Food Science & Emerging Technologies,2008.9(1),62-69.
[102]Yu, H.L., Cao, M.J., Cai, Q.F., et al., Effects of different processing methods on digestibility of Scylla paramamosain allergen (tropomyosin). Food and Chemical Toxicology,2011.49(4), 791-798.
[103]Perez-Gordo, M., Cuesta-Harranz, J., Maroto, A.S., et al., Identification of sole parvalbumin as a major allergen:study of cross-reactivity between parvalbumins in a Spanish fish-allergic population. Clinical & Experimental Allergy,2011.41(5),750-758.
[104]Koppelman, S.J., Romijn, R.A., De Jongh, H.H.J., et al., Purification of Parvalbumin from Carp: A Protocol that Avoids Heat-Treatment. Journal of Food Science,2010.75(3), T49-T56.
[105]刘楚怡,薛文通,李阳,青鱼致敏蛋白的识别、热稳定性及模拟肠液消化的研究,in 2011年中国农业工程学会农产品加工及贮藏工程分会学术年会暨全国食品科学与工程博士生学术论坛、管产学研助推食品安全重庆高峰论坛论文集2011：重庆.p.394-397.
[106]Kim, K.B.W.R., Lee, S.Y., Song, E.J., et al., Effect of heat and autoclave on allergenicity of porcine serum albumin. Food Science and Biotechnology,2011.20(2),455-459.
[107]Tong, P., Gao, J.Y, Chen, H.B., et al., Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chemistry,2012.131(2), 603-610.
[108]Takahashi, K., Terada, C., Tashiro, M., et al., Effects of heat treatment and pepsin digestion on trypsin inhibitory activity and ovomucoid antigenicity of japanese quail egg white. Journal of Food Biochemistry,2003.27(5),423-434.
[109]Starkl, P., Krishnamurthy, D., Szalai, K., et al., Heating Affects Structure, Enterocyte Adsorption and Signalling, As Well as Immunogenicity of the Peanut Allergen Ara h 2. Open Allergy J,2011.4,24-34.
[110]Chatterjee, U., Mondal. G., Chakraborti, P., et al., Changes in the Allergenicity during Different Preparations of Pomfret, Hilsa, Bhetki and Mackerel Fish as Illustrated by Enzyme-Linked Immunosorbent Assay and Immunoblotting. International Archives of Allergy and Immunology, 2006.141(1),1-10.
[111]Sletten, G., Van Do, T., Lindvik, H., et al., Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species. International Archives of Allergy and Immunology,2010.151(3),223-236.
[112]Bugajska-Schretter, A., Grote, M., Vangelista, L., et al., Purification, biochemical, and immunological characterisation of a major food allergen:different immunoglobulin E recognition of the apo-and calcium-bound forms of carp parvalbumin. Gut,2000.46(5), 661-669.
[113]Gornall, A.G., Bardawill, C.J. and David M.M., Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry,1949.177(2),751-766.
[114]Arif, S.H., Jabeen, M. and Hasnain A.U., Biochemical characterization and thermostable capacity of parvalbumins:the major fish-food allergens. Journal of Food Biochemistry,2007. 31(1),121-137.
[115]Bugajska-Schretter, A., Elfman, L., Fuchs, T., et al., Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion. Journal of Allergy and Clinical Immunology,1998.101(1),67-74.
[116]Besler, M., Steinhart, H. and Paschke, A., Stability of food allergens and allergenicity of processed foods. Journal of Chromatography B:Biomedical Sciences and Applications,2001. 756(1-2),207-228.
[117]Griesmeier, U., Bublin, M., Radauer, C., et al., Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff. Molecular Nutrition & Food Research,2010.54(6), 861-869.
[118]Martos, G., Lopez-Exposito, I., Bencharitiwong, R., et al., Mechanisms underlying differential food allergy response to heated egg. Journal of Allergy and Clinical Immunology,2011.127(4), 990-997.e2.
[119]Thomas, K., Herouet-Guicheney, C., Ladics, G., et al., Evaluating the effect of food processing on the potential human allergenicity of novel proteins:International workshop report. Food and Chemical Toxicology,2007.45(7),1116-1122.
[120]黄园园,水产过敏原的模拟胃肠液消化,2009,集美大学.
[121]Shen, J.D., Cai, Q.F., Liu, G.M., et al., A comparison study of the impact of boiling and high pressure steaming on the stability of soybean trypsin inhibitor. International Journal of Food Science and Technology,2013.48(9),1877-1883.
[122]De Jongh, H.H.J., Robles, C.L., Timmerman, E., et al., Digestibility and IgE-binding of glycosylated codfish parvalbumin. BioMed Research International,2013.2013.
[123]程伟,多酚氧化酶交联牛乳a-乳白蛋白的结构变化及其消化性与过敏原性的评估,2012,南昌大学.
[124]van de Lagemaat, J., Manuel Silvan, J., Javier, M.F., et al., In vitro glycation and antigenicity of soy proteins. Food Research International,2007.40(1),153-160.
[125]Nakamura, S., Suzuki, Y., Ishikawa, E., et al., Reduction of in vitro allergenicity of buckwheat Fag e 1 through the Maillard-type glycosylation with polysaccharides. Food Chemistry,2008. 109(3),538-545.
[126]Iwan, M., Vissers, Y.M., Fiedorowicz, E., et al., Impact of Maillard Reaction on Immunoreactivity and Allergenicity of the Hazelnut Allergen Cor a 11. Journal of Agricultural and Food Chemistry,2011.59(13),7163-7171.
[127]Bu, G., Lu J., Zheng Z., et al., Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology. Journal of the Science of Food and Agriculture,2009.89(14),2428-2434.
[128]Bu G.H., Luo, Y.L., Lu, J., et al. Reduced antigenicity of β-lactoglobulin by conjugation with glucose through controlled Maillard reaction conditions. Food and Agricultural Immunology, 2010.21(2),143-156.
[129]Li, Z., Luo, Y.K., and Feng, L.G., Effects of Maillard reaction conditions on the antigenicity of a-lactalbumin and P-lactoglobulin in whey protein conjugated with maltose. European Food Research and Technology,2011.233(3),387-394.
[130]Jimenez-Saiz, R., Belloque, J., Molina, E., et al., Human Immunoglobulin E (IgE) Binding to Heated and Glycated Ovalbumin and Ovomucoid before and after in Vitro Digestion. Journal of Agricultural and Food Chemistry,2011.59(18),10044-10051.
[131]Oldfield, D.J., Singh, H., Taylor, M.W., et al., Kinetics of Denaturation and Aggregation of Whey Proteins in Skim Milk Heated in an Ultra-high Temperature (UHT) Pilot Plant. International Dairy Journal,1998,8(4),311-318.
[132]Elsayed, S. and Aas, K., Isolation of purified allergens (cod) by isoelectric focusing. Int Arch Allergy Appl Immunol,1971.40(3),428-38.
[133]Laemmli, U.K., Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature,1970.227(5259),680-685.
[134]Li, S., Offengenden M., Fentabil, M., et al., Effect of egg white fermentation with lactobacilli on IgE binding ability of egg white proteins. Food Research International,2013.52(1), 359-366.
[135]Offengenden, M., Fentabil, M. and Wu, J., N-glycosylation of ovomucin from hen egg white. Glycoconjugate Journal,2011.28(3-4),113-123.
[136]Majumder, K., Panahi, S., Kaufman, S., et al., Fried egg digest decreases blood pressure in spontaneous hypertensive rats. Journal of Functional Foods,2013.5(1),187-194.
[137]Schulten, V, Lauer,1., Scheurer, S., et al., A food matrix reduces digestion and absorption of food allergens in vivo. Molecular Nutrition & Food Research,2011.55(10),1484-1491.
[138]Chicon, R., Belloque, J., Alonso, E., et al., Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure. Food Hydrocolloids,2009.23(3),593-599.
[139]Fujita, S., Shimizu, Y., Kishimura, H., et al., In vitro digestion of major allergen in salmon roe and its peptide portion with proteolytic resistance. Food Chemistry,2012.130(3),644-650.
[140]任宏伟,胡柳,我国鱼糜制品现状及发展态势.中国水产,2010(8),25-26.
[141]张俊杰,曾庆孝,我国淡水鱼鱼糜的研究情况.食品与发酵工业,2002.28(9),57-63.
[142]Sikorski, Z. and Kolakowska, A., Changes in Proteins in Frozen Stored Fish, in Seafood Proteins, Z. Sikorski, B. Pan, and F. Shahidi, Editors.1995, Springer US. p.99-112.
[143]del Mazo, M.L., Torrejon, P., Careche, M., et al., Characteristics of the Salt-Soluble Fraction of Hake (Merluccius merluccius) Fillets Stored at -20 and -30℃. Journal of Agricultural and Food Chemistry,1999.47(4),1372-1377.
[144]Matsumoto Juichiro, J., Denaturation of Fish Muscle Proteins During Frozen Storage, in Proteins at Low Temperatures 1979, American Chemical Society, p.205-224.
[145]Jiang, S.T. and Lee, T.C., Changes in free amino acids and protein denaturation of fish muscle during frozen storage. Journal of Agricultural and Food Chemistry,1985.33(5),839-844.
[146]Lee, P.W., Nordlee, J.A., Koppelman, S.J., et al., Measuring parvalbumin levels in fish muscle tissue:Relevance of muscle locations and storage conditions. Food Chemistry,2012.135(2), 502-507.
[147]汪宁,鱼类过敏蛋白的检测分析、分离纯化和分子克隆,2008,上海海洋大学.
[148]Cai, Q.F., Wang X.C., Liu, G.M., et al., Development of a monoclonal antibody-based competitive enzyme linked-immunosorbent assay (c-ELISA) for quantification of silver carp parvalbumin. Food Control,2013.29(1),241-247.