鲢鱼鱼肉蛋白抗氧化肽的制备及其糖基化产物功能特性的研究
详细信息    本馆镜像全文|  推荐本文 |  |   获取CNKI官网全文
摘要
鲢鱼是我国主要的淡水鱼种,其生长快,产量大,但其特有腥味,骨刺多等造成鲢鱼低价值。近来,有关如何提高鲢鱼附加值的问题已成为国内水产加工研究者们研究和开发产品的热点,但仍然处在初级阶段。因此,本研究以鲢鱼鱼肉蛋白为原料,采用酶解的方法制备抗氧化活性肽,并通过糖基化作用对酶解产物和水溶性蛋白进行功能特性和抗氧化活性改性的研究,为鲢鱼蛋白综合加工和提高其附加值提供理论基础。
     本研究选择了五种蛋白酶酶解鲢鱼鱼肉蛋白,通过测定了鲢鱼鱼肉蛋白的水解度及酶解产物的抗氧化活性,并分析了水解度与抗氧化各指标间的相关性。结果表明,胃蛋白酶酶解产物的清除DPPH自由基能力和还原力较强:另外,酶解产物的水解度与亚铁离子螯合力具有显著的相关性(p<0.05)。
     通过超滤、凝胶过滤层析与反相高效液相色谱(RP-HPLC)相结合的方法对鲢鱼鱼肉蛋白多肽进行分离,并运用清除DPPH自由基、清除羟基自由基、亚铁离子螯合力、还原力及氧活性自由基吸收能力(ORAC)等方法测定其抗氧化活性。通过液质联用的方法鉴定了10个来源于鲢鱼肌球蛋白和肌动蛋白的肽,经过合成后测定了其抗氧化活性,其中有两个肽Tyr-Thr-Ile-Gln-Tyr(YTIQY)和Asn-Trp-Asp-Asp-Met (NWDDM)抗氧化活性较高,且高于相同浓度的茶多酚的ORAC值。
     鲢鱼鱼肉蛋白多肽和葡萄糖在不同温度和质量比的条件下经过糖基化改性制备鲢鱼鱼肉蛋白多肽-糖复合物。糖基化反应产物有较好的清除DPPH自由基能力和还原力,显著高于未经过糖基化反应的多肽(p<0.05)。当鲢鱼鱼肉蛋白多肽与葡萄糖在60℃,以2:1混合反应后其产物显现出较高的褐变程度和抗氧化活性,且294nm的吸光值与抗氧化活性之间具有显著的相关性(p<0.05)。因此糖基化改性技术可以在一定程度上提高鲢鱼鱼肉蛋白多肽的抗氧化活性。
     鲢鱼水溶性蛋白在鱼糜加工过程中被作为废水处理,为了更好的利用鲢鱼水溶性蛋白资源,研究了鲢鱼水溶性蛋白经过热加工、冷冻干燥以及不同pH条件处理下的鲢鱼水溶性蛋白的溶解性、乳化性、起泡性、热稳定性等功能特性和理化特性。结果表明,鲢鱼水溶性蛋白在40℃到55℃之间经历了变性和聚集,在50℃时变化速率最大。组成鲢鱼水溶性蛋白的蛋白质分子量主要集中在30~97kDa,大部分水溶性蛋白在55℃发生沉淀。经过冷冻干燥的水溶性蛋白溶解性降低至72%左右。在等电点时,鲢鱼水溶性蛋白的功能特性较差。
     鲢鱼水溶性蛋白在加热过程中容易发生变性聚集而降低其各方面功能特性,本研究将5种糖基供体(包括木糖、葡萄糖、半乳糖、低聚异麦芽糖、葡聚糖-10)引入到鲢鱼水溶性蛋白,经过糖基化反应后测定其产物的功能特性,包括溶解性、热稳定性、乳化活性、乳化稳定性,同时将其理化特性如表面疏水性、总巯基含量及SDS-PAGE电泳进行分析。结果表明:经过糖基化改性的鲢鱼水溶性蛋白在50℃条件下的溶解性、乳化活性、热稳定性得到提高。并且随着提供的糖基供体分子量的增大,溶解性、乳化活性及热稳定性有一定程度的增加。综合得出鲢鱼水溶性蛋白与葡聚糖-10的反应产物具有较好效果。
In China, silver carp with fast growing and large production is one of the main freshwater fish species. However it is a low market-value resource because of its muddy flavor and many fish bones. Nowerday, the development of silver carp products became to be most popular research area for aquatic researchers, but the researches are still in the early stages. The research objective of this study was to utilize silver carp fish protein and to impove the additional value for this freshwater fish. Antioxidant peptides from silver carp protein by enzymes hydrolysation were prepared. And functional properties and antioxidant acitivities of glycosylated hydrolysates and water-soluble proteins from silver carp were studied.
     Five common enzymes were used for hydrolysation at the same enzyme activity. The hydrolysis degree and antioxidant activities of hydrolysates were determined. The relativity between the degree of hydrolysis and antioxidant activities were also dicussed. The results showed that the DPPH radical scavenging capacity and reducing power of pepsin hydrolysates were higher than other hydrolysates, and the values were61%and1.6, respectively. There were marked relativity between the degree of hydrolysis and metal-chelating activity (p<0.05)
     Silver carp peptides were separated by ultrafiltration, gel filtration and reverse phrase high pressure liquid chromatogram. The DPPH radical scavenging capacity, hydroxyl radical scavenging capacity, iron chelating, reducing power and oxygen radical absorbance capacity of fractions were determined. Ten peptides from silver carp myosin and actin were identified by LC-MS/MS, and their antioxidant activities were determined using synthetic peptides. Two pentapeptides (Tyr-Thr-Ile-Gln-Tyr and Asn-Trp-Asp-Asp-Met) showed higher antioxidant activity, and the ORAC values of them were higher than catechin.
     The Maillard reaction products (MRPs) were prepared at different temperatures and ratios between silver carp protein hydrolysates (SPH) and glucose by Maillard reaction in powdered state, respectively. MRPs possessed a strong2,2-diphenyl-l-picrylhydrazyl (DPPH) radical scavenging activity and reducing power (p<0.05). The hydrolysate and glucose heated with the ratio of2:1at60℃showed high browning intensity and good antioxidant properties (p<0.05). According to the correlation coefficients of variables included in the hydrolysate-glucose system, good correlations were observed among the antioxidant activities and the absorbance at294nm. The results suggested that Maillard reaction has a good potential to improve the antioxidant activity of SPH.
     Water-soluble proteins (WSP) from silver carp muscle are currently underutilized in China and are discarded into waste streams in surimi processing. In order to utilize WSP resources efficiently, this work investigated the effect of three processing conditions on the physicochemical properties and fuctional properties such as solubility, heat stability, emulsifying activity and foamability of water-soluble proteins from silver carp. The results showed that silver carp water-soluble proteins would suffer huge denaturation and aggregation from40to55℃. Most of silver carp water-soluble proteins precipitated at55℃. Lyophilization could increase surface hydrophobicity of water-soluble proteins, but decrease its solubility and sulfhydryl groups. The functional properties of WSP were greatly affected by pH value, the lowest solubility was observed at pH4.0-5.0.
     WSP denature easily during thermal processing, leading to the reduction of functional properties. Five different kinds of carbohydrates (i.e., xylose, glucose, galactose, oligoisomaltose, and dextran-10) were used to conjugate with WSP by Maillard reaction. Results suggested that the use of the Maillard reaction improved the solubility, heat stability, and emulsifying properties of WSP.With the increase of molecular weight (MW) of the sugars, the solubility, emulsifying properties, and total sulfhydryl (SH) group of WSP increased, while the surface hydrophobicity decreased. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the five Maillard reaction products (MRPs) showed that xylose reacted easily with WSP than the other four kinds of sugar did. Dextran-10conjugated to WSP could efficiently improve the functional properties of WSP during heat processing.
引文
[1]农业部渔业局,2013中国渔业统计年鉴.北京:中国农业出版社.2013,p.1-145.
    [2]熊善柏,湖北省淡水鱼加工业现状、产业化发展思路与建议.养殖与饲料,2012(09):p.4-8.
    [3]赵永锋,胡海彦,蒋高中等,我国大宗淡水鱼的发展现状及趋势研究.中国渔业经济,2012(05):p.91-99.
    [4]潘锦锋,草鱼肌原纤维蛋白在冻藏与加热过程中理化特性的变化及蛋白变性保护剂的研究:[硕士学位论文].北京:中国农业大学,2009.
    [5]史策,韩烽烽,刘鹏等,鲢鱼肉蛋白酶解产物功能特性的研究.中国食物与营养,2013(10):p.25-28.
    [6]张洵,发酵鱼糜的风味改良研究,2013,江南大学.
    [7]戈贤平和缪凌鸿,我国大宗淡水鱼产业发展现状与体系研究进展.中国渔业质量与标准,2011(03):p.22-31.
    [8]罗永康,周新华,鲢鱼蛋白质低温变性保护剂的研究.食品科学,1996(01):p.59-62.
    [9]李兆杰,水产品化学,北京:化学工业出版社,2007,14-20.
    [10]刘召静,鲢鱼肌球蛋白重链球状结构域的cDNA克隆及结构解析:[硕士学位论文].上海:上海海洋大学,2010.
    [11]Park, J., Surimi and surimi seafood. Third edition. Section 4. U.S.:CRC Press.2013,102-104.
    [12]Luo, Y., Kuwahara, R,, Kaneniwa, M., et al., Comparison of gel properties of surimi from Alaska Pollock and three freshwater fish species:effects of thermal processing and protein concentration. Journal of Food Science,2001.66(4):p.548-554.
    [13]Zhou, F., Zhao, M., Zhao, H., et al., Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals. Meat Science,2014.96(4):p. 1432-1439.
    [14]Chanarat, S. and Benjakul, S. Impact of microbial transglutaminase on gelling properties of Indian mackerel fish protein isolates. Food Chemistry,2013.136(2):p.929-937.
    [15]Kaewudom, P., Benjakul, S. and Kijroongrojana, K. Properties of surimi gel as influenced by fish gelatin and microbial transglutaminase. Food Bioscience,2013.1:p.39-47.
    [16]Ko, W.-C, Yu, C.-C. and Hsu, K.-C. Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment. LWT-Food Science and Technology,2007.40(8):p. 1316-1320.
    [17]Sun, F., Huang, Q., Hu, T., et al., Effects and mechanism of modified starches on the gel properties of myofibrillar protein from grass carp. International Journal of Biological Macromolecules,2014.64:p.17-24.
    [18]Yang, Z., Wang, W., Wang, H., et al., Effects of a highly resistant rice starch and pre-incubation temperatures on the physicochemical properties of surimi gel from grass carp(Ctenopharyn Odon ldellus). Food Chemistry,2014.145:p.212-219.
    [19]Liu, J., Wang, X., and Ding, Y., Optimization of adding konjac glucomannan to improve gel properties of low-quality surimi. Carbohydrate Polymers,2013.92(1):p.484-489.
    [20]Dyer, W.J., Protein denaturation in frozen and stored fish. Journal of Food Science,1951.16(1-6): p.522-527.
    [21]Pan, J., Shen, H. and Luo, Y., Changes in salt extractrable protein and Ca2+ATPase activity of mince from silver carp (Hypophthalmichthys Mollitrix) during frozen storage:A kinetic study. Journal of Muscle Foods,2010.21(4):p.834-847.
    [22]Pan, J., Shen, H., You, J., et al., Changes in physiochemical properties of myofibrillar protein from silver carp (Hypophthalmichthys Mollitrix) during heat-treatment. Journal of Food Biochemistry,2011.35(3):p.939-952.
    [23]宋永令,团头鲂贮藏及热加工过程中生化特性变化及机理研究.[博士学位论文].北京:中国农业大学,2011.
    [24]Wang, H., Luo, Y. and Shen, H. Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle. International Journal of Food Science & Technology,2013.48(9):p.1962-1969.
    [25]Kulawik, P., Ozogul, F. and Glew, R.H. Quality properties, fatty acids, and biogenic amines profile of fresh Tilapia stored in ice. Journal of Food Science,2013.78(7):p.1063-1068.
    [26]刘建华和丁玉庭,糖基化反应改善鱼肉肌原纤维蛋白功能特性及其机制研究进展.食品与发酵工业,2012.38(8):p.132-136.
    [27]Villaverde, A. and Estevez, M. Carbonylation of myofibrillar proteins through the Maillard pathway:Effect of reducing sugars and reaction temperature. Journal of Agricultural and Food Chemistry,2013.61(12):p.3140-3147.
    [28]Park, J., Surimi and surimi seafood. Third edition. Section 13. U.S.:CRC Press.2013,317-320.
    [29]Stine, J.J., Pedersen, L., Smiley, S., et al., Recovery and utilization of protien derived from surimi wash-water. Journal of Food Quality,2012.35(1):p.43-50.
    [30]Kim, Y.S., Yongsawatdigul, J., Park, J.W., et al., Characteristics of sarcoplasmic proteins and their interaction with myofibrillar proteins. Journal of Food Biochemistry,2005.29(5):p. 517-532.
    [31]Tadpitchayangkoon, P., Park, J.W. and Yongsawatdigul, J. Conformational changes and dynamic rheological properties offish sarcoplasmic proteins treated at various pHs. Food Chemistry,2010. 121(4):p.1046-1052.
    [32]Samejima, K., Hashimoto, Y., Yasui, T., et al., Heat gelling properties of myosin, actin, actomyosin and myosin-subunits in a saline model system. Journal of Food Science,1969.34(3): p.242-245.
    [33]Jafarpour, A. and Gorczyca, E.M. Characteristics of sarcoplasmic proteins and their interaction with surimi and kamaboko gel. Journal of Food Science,2009.74(1):p.16-22.
    [34]Karthikeyan, M., Mathew, S., Shamasundar, B.A., et al., Fractionation and properties of sarcoplasmic proteins from oil sardine (Sardinella longiceps):Influence on the thermal gelation behavior of washed meat. Journal of Food Science,2004.69(3):p.79-84.
    [35]Piyadhammaviboon, P. and Yongsawatdigul, J. Protein cross-linking ability of sarcoplasmic proteins extracted from threadfin bream. LWT-Food Science and Technology,2009.42(1):p. 37-43.
    [36]Morioka, K. and Shimizu, Y. Contribution of sarcoplasmic proteins to gel formation offish meat. Bulletin of the Japanese Society of Scientific Fisheries (Japan),1990.
    [37]Miyaguchi, Y., Hayashi, Y. and Sakamoto, T. Physicochemical properties of the thermal gel of water-washed meat in the presence of the more soluble fraction of porcine sarcoplasmic protein. Animal Science Journal,2007.78(1):p.77-84.
    [38]Hemung, B.-O. and Chin, K.B. Effects of fish sarcoplasmic proteins on the properties of myofibrillar protein gels mediated by microbial transglutaminase. LWT-Food Science and Technology,2013.53(1):p.184-190.
    [39]Ghassem, M., Babji, AS., Said, M., et al., Angiotensin I-converting enzyme inhibitory peptides from snakehead fish sarcoplasmic protein hydrolysate. Journal of Food Biochemistry,2013. DOI: 10.1111/jfbc-12031.
    [40]Kuan, Y.-H., Bhat, R., Patras, A., et al., Radiation processing of food proteins-A review on the recent developments. Trends in Food Science & Technology,2013.30(2):p.105-120.
    [41]何轩辉,刘红芝,赵冠里,等,超高压对食品蛋白凝胶性的影响研究进展.食品科学,2013(13):p.334-337.
    [42]Li, H., Zhu, K., Zhou, H., et al., Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chemistry,2012. 132(2):p.808-814.
    [43]Qiu, C., Xia, W. and Jiang, Q. Effect of high hydrostatic pressure (HHP) on myofibril-bound serine proteinases and myofibrillar protein in silver carp(Hypophthalmichthys molitrix). Food Research International,2013.52(1):p.199-205.
    [44]Je, J.Y., Qian, Z.J., Lee, S.H., et al., Purification and antioxidant properties of bigeye tuna (Thunnus obesus) dark muscle peptide on free radical-mediated oxidative systems. Jounal of Medical Food,2008.11(4):p.629-37.
    [45]Pownall, T.L., Udenigwe, C.C. and Aluko, R.E. Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions. Journal of Agricultural and Food Chemistry,2010.58(8):p.4712-4718.
    [46]Batista, I., Biological activities of fish-protein hydrolysates:in marine proteins and peptides. U.K.:John Wiley & Sons, Ltd.2013, p.111-138.
    [47]Himaya, S.W.A., Ngo, D.H., Ryu, B.M., et al., An active peptide purified from gastrointestinal enzyme hydrolysate of Pacific cod skin gelatin attenuates angiotensin-1 converting enzyme (ACE) activity and cellular oxidative stress. Food Chemistry,2012.132(4):p.1872-1882.
    [48]Liu, M., Du, M., Zhang, Y, et al., Purification and identification of an ACE inhibitory peptide from walnut protein. Journal of Agricultural and Food Chemistry,2013.61(17):p.4097-4100.
    [49]Garcia-Nebot, M.J., I. Recio, and Hernandez-Ledesma, B. Antioxidant activity and protective effects of peptide lunasin against oxidative stress in intestinal Caco-2 cells. Food and Chemical Toxicology,2014.65:p.155-161.
    [50]Power, O., Jakeman, P. and FitzGerald, R.J. Antioxidative peptides:enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides. Amino Acids,2013.44(3):p.797-820.
    [51]Sun, Q., Luo, Y., Shen, H., et al., Purification and characterisation of a novel antioxidant peptide from porcine haemoglobin hydrolysate. International Journal of Food Science & Technology, 2012.47(1):p.148-154.
    [52]He, J., Krauson, A.J. and Wimley, W.C. Toward the de novo design of antimicrobial peptides: Lack of correlation between peptide permeabilization of lipid vesicles and antimicrobial, cytolytic, or cytotoxic activity in living cells. Peptide Science,2014.102(1):p.1-6.
    [53]Wu, W.-H., Di, R. and Matthews, K.R. Activity of the plant-derived peptide Ib-AMP1 and the control of enteric foodborne pathogens. Food Control,2013.33(1):p.142-147.
    [54]莫文敏,曾庆孝,蛋白质改性研究进展.食品科学,2000.21(6):p.6-10.
    [55]Treuel, L., Brandholt, S., Maffre, P., et al., Impact of protein modification on the protein corona on nanoparticles and nanoparticle-cell interactions. ACS Nano,2013.8(1):p.503-513.
    [56]Hrynets, Y., Ndagijimana, M. and Betti, M. Non-enzymatic glycation of natural actomyosin (NAM) with glucosamine in a liquid system at moderate temperatures. Food Chemistry,2013. 139(1-4):p.1062-1072.
    [57]Wu, J. and Majumder, K. Peptides that inhibit aangiotensin converting enzyme and peptides with antioxidant activity purified from ovotransferrin and methods of producing and using the same, Canada, WO Patent 2010106437,2010.
    [58]Petrick, J.S., Brower-Toland, B., Jackson, A.L., et al., Safety assessment of food and feed from biotechnology-derived crops employing RNA-mediated gene regulation to achieve desired traits: A scientific review. Regulatory Toxicology and Pharmacology,2013.66(2):p.167-176.
    [59]孙骞,猪血红蛋白抗氧化肽的制备纯化与表征及其糖基化产物活性机制的研究.[博士学位论文].北京:中国农业大学,2010.
    [60]林亲录,赵谋明,邓靖,等,毛霉产蛋白酶的特性研究.食品科学,2005(05):p.44-47.
    [61]You, L., Zhao, M., Regenstein, J.M., et al., Purification and identification of antioxidative peptides from loach(Misgurnus anguillicaudatus) protein hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry. Food Research International, 2010.43(4):p.1167-1173.
    [62]Majumder, K. and Wu, J. A new approach for identification of novel antihypertensive peptides from egg proteins by QSAR and bioinfonnatics. Food Research International,2010.43(5):p. 1371-1378.
    [63]Sagardia, I., Roa-Ureta, R.H. and Bald, C. A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides. Food Chemistry.2013.136(3~4):p.1370-1376.
    [64]Carocho, M. and Ferreira, I.C.F.R. A review on antioxidants, prooxidants and related controversy:Natural and synthetic compounds, screening and analysis methodologies and future perspectives. Food and Chemical Toxicology,2013.51:p.15-25.
    [65]Athukorala, Y., Kim, K.-N. and Jeon, Y.-J. Antiproliferative and antioxidant properties of an enzymatic hydrolysate from brown alga, Ecklonia cava. Food and Chemical Toxicology,2006. 44(7):p.1065-1074.
    [66]Butterfield, D.A., Castegna, A., Pocernich, C.B., et al., Nutritional approaches to combat oxidative stress in Alzheimer's disease. The Journal of Nutritional Biochemistry,2002.13(8):p. 444-461.
    [67]Manso, M.A., Miguel, M., Even, J., et al., Effect of the long-term intake of an egg white hydrolysate on the oxidative status and blood tipid profile of spontaneously hypertensive rats. Food Chemistry,2008.109(2):p.361-367.
    [68]Shahidi, F., Antioxidants in food and food antioxidants. Food/Nahrung,2000.44(3):p. 158-163.
    [69]Aruoma, O., Free radicals, oxidative stress, and antioxidants in human health and disease. Journal of the American Oil Chemists' Society,1998.75(2):p.199-212.
    [70]You, J., Luo, Y. and Wu, J. Conjugation of ovotransferrin with catechin shows improved antioxidant activity. Journal of Agricultural and Food Chemistry,2014.62(12):p.2581-2587.
    [71]Li, X., Luo, Y, Shen, H., et al., Antioxidant activities and functional properties of grass carp (Ctenopharyngodon idellus) protein hydrolysates. Journal of the Science of Food and Agriculture, 2012.92(2):p.292-298.
    [72]Castro, R.J.S.d. and Sato, H.H. Comparison and synergistic effects of intact proteins and their hydrolysates on the functional properties and antioxidant activities in a simultaneous process of enzymatic hydrolysis. Food and Bioproducts Processing,2014.92(1):p.80-88.
    [73]Najafian, L. and Babji, A.S. A review of fish-derived antioxidant and antimicrobial peptides: Their production, assessment, and applications. Peptides,2012.33(1):p.178-185.
    [74]Irvine, J.D., Takahashi, L., Lockhart, K., et al., MDCK (Madin-Darby canine kidney) cells:A tool for membrane permeability screening. Journal of Pharmaceutical Sciences,1999.88(1):p. 28-33.
    [75]Samaranayaka, A.G.P., Kitts, D.D. and Li-Chan, E.C.Y. Antioxidative and angiotensin-I-converting enzyme inhibitory potential of a pacific hake(Merluccius productus) fish protein hydrolysate subjected to simulated gastrointestinal digestion and Caco-2 cell permeation. Journal of Agricultural and Food Chemistry,2010.58(3):p.1535-1542.
    [76]Chen, H.-M., Muramoto, K., Yamauchi, F., et al., Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agricultural and Food Chemistry,1998.46(1):p.49-53.
    [77]Qian, Z.-J., Jung, W.-K. and Kim, S.-K. Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate of bullfrog skin, Rana catesbeiana Shaw. Bioresource Technology,2008.99(6):p.1690-1698.
    [78]Donnelly, J.L., Decker, E.A. and McClements, D.J. Iron-catalyzed oxidation of menhaden oil as affected by emulsifiers. Journal of Food Science,1998.63(6):p.997-1000.
    [79]Li, Y.-W., Li, B., He, J., et al., Structure-activity relationship study of antioxidative peptides by QSAR modeling:the amino acid next to C-terminus affects the activity. Journal of Peptide Science,2011.17(6):p.454-462.
    [80]Gu, Y., Majumder, K. and Wu, J. QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides. Food Research International,2011.44(8):p. 2465-2474.
    [81]Shen, S., Chahal, B., Majumder, K., et al., Identification of novel antioxidative peptides derived from a thermolytic hydrolysate of ovotransferrin by LC-MS/MS. Journal of Agricultural and Food Chemistry,2010.58(13):p.7664-7672.
    [82]Seo, H.-S., Kwak, S.-Y. and Lee, Y.-S. Antioxidative activities of histidine containing caffeic acid-dipeptides. Bioorganic & Medicinal Chemistry Letters,2010.20(14):p.4266-4272.
    [83]Sharp, J.S., Becker, J.M. and Hettich, R.L. Analysis of protein solvent accessible surfaces by photochemical oxidation and mass spectrometry. Analytical Chemistry,2003.76(3):p.672-683.
    [84]Davalos, A., Miguel, M., Bartolome, B., et al., Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection,2004.67(9):p.1939-1944.
    [85]Hernandez-Ledesma, B., Davalos, A., Bartolome, B., et al., Preparation of antioxidant enzymatic hydrolysates from a-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/MS. Journal of Agricultural and Food Chemistry,2005.53(3):p.588-593.
    [86]Hernandez-Ledesma, B., Quiros, A., Amigo, L., et al., Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin. International Dairy Journal,2007.17(1):p.42-49.
    [87]Saito, K., Jin, D.H., Ogawa, T., et al., Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry. Journal of Agricultural and Food Chemistry,2003.51(12):p. 3668-3674.
    [88]Chalamaiah, M., Hemalatha, R., Jyothirmayi, T., et al., Fish protein hydrolysates:Proximate composition, amino acid composition, antioxidant activities and applications:A review. Food Chemistry,2012.135(4):p.3020-3038.
    [89]Zeng, M., Dong, S., Zhao, Y., et al., Antioxidant activities of marine peptides from fish and shrimp, in marine proteins and peptides, U.K. John Wiley & Sons, Ltd.,2013, p.449-466.
    [90]Kristinsson, H.G. and Rasco, B.A. Fish protein hydrolysates:Production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition,2000.40(1):p.43-81.
    [91]Dekkers, E., Raghavan S., Kristinsson H.G, et al., Oxidative stability of mahi red muscle dipped in tilapia protein hydrolysates. Food Chemistry,2011.124(2):p.640-645.
    [92]Marzani, B., Balage, M., Venien, A., et al., Antioxidant supplementation restores defective leucine stimulation of protein synthesis in skeletal muscle from old rats. The Journal of Nutrition, 2008.138(11):p.2205-2211.
    [93]Khalil, A., Gaudreau, P., Cherki, M., et al., Antioxidant-rich food intakes and their association with blood total antioxidant status and vitamin C and E levels in community-dwelling seniors from the Quebec longitudinal study NuAge. Experimental Gerontology,2011.46(6):p.475-481.
    [94]Oliver, C.M., Melton, L.D. and Stanley, R.A. Creating proteins with novel functionality via the maillard reaction:A Review. Critical Reviews in Food Science and Nutrition,2006.46(4):p. 337-350.
    [95]Liu, J., Ru, Q. and Ding, Y. Glycation a promising method for food protein modification: Physicochemical properties and structure, a review. Food Research International,2012.49(1):p. 170-183.
    [96]Hodge, J.E., Dehydrated foods, chemistry of browning reactions in model systems. Journal of Agricultural and Food Chemistry,1953.1(15):p.928-943.
    [97]Ames, J., The Maillard Reaction, in Biochemistry of Food Proteins, B.J.F. Hudson, Editor 1992, Springer US. p.99-153.
    [98]Saeki, H., Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose:Biochemical properties and emulsifying properties. Journal of Agricultural and Food Chemistry,1997.45(3):p.680-684.
    [99]Saeki, H. and K. Inoue, Improved solubility of carp myofibrillar proteins in low ionic strength medium by glycosylation. Journal of Agricultural and Food Chemistry,1997.45(9):p. 3419-3422.
    [100]Zhang, J., Wu, N., Lan, T., et al., Improvement in emulsifying properties of soy protein isolate by conjugation with maltodextrin using high-temperature, short-time dry-heating Maillard reaction. International Journal of Food Science & Technology,2014.49(2):p.460-467.
    [101]Liu, Q., Kong, B., Han, et al., Structure and antioxidant activity of whey protein isolate conjugated with glucose via the Maillard reaction under dry-heating conditions. Food Structure, 2014.1(2):p.145-154.
    [102]Zhuo, X.-Y., Qi, J.R., Yin, S.W. et al., Formation of soy protein isolate-dextran conjugates by moderate Maillard reaction in macromolecular crowding conditions. Journal of the Science of Food and Agriculture,2013.93(2):p.316-323.
    [103]Zhu, D., Damodaran, S. and Lucey, J.A. Formation of whey protein isolate (WPI)-Dextran conjugates in aqueous solutions. Journal of Agricultural and Food Chemistry,2008.56(16):p. 7113-7118.
    [104]Kato, A., Industrial applications of Maillard-type protein-polysaccharide conjugates. Food Science and Technology Research,2002.8(3):p.193-199.
    [105]Huang, X., Tu, Z., Wang, H., et al., Increase of ovalbumin glycation by the Maillard reaction after disruption of the disulfide bridge evaluated by liquid chromatography and high resolution mass spectrometry. Journal of Agricultural and Food Chemistry,2013.61(9):p.2253-2262.
    [106]Schwarzenbolz, U., H. Klostermeyer, and T. Henle, Maillard reaction under high hydrostatic pressure:studies on the formation of protein-bound amino acid derivatives. International Congress Series,2002.1245(0):p.223-227.
    [107]Tsubokura, Y., Fukuzaki, S., Noma, S., et al., Glycation of ovalbumin in solid-state by conductive and microwave heating. Food Science and Technology Research,2009.15(4):p. 377-380.
    [108]Tu, Z., Hu, Y., Wang, H., et al., Microwave heating enhances antioxidant and emulsifying activities of ovalbumin glycated with glucose in solid-state. Journal of Food Science and Technology,2013:p.1-9.
    [109]Casal, E., Ramirez, P., Ibanez, E., et al., Effect of supercritical carbon dioxide treatment on the Maillard reaction in model food systems. Food Chemistry,2006.97(2):p.272-276.
    [110]Guan, Y.G., Zhang, B.S., Yu, S.J., et al., Effects of ultrasound on a glycin-glucose model system—A means of promoting Maillard reaction. Food and Bioprocess Technology,2011.4(8): p.1391-1398.
    [111]Mu, L., Zhao, M., Yang, B., et al., Effect of ultrasonic treatment on the graft reaction between soy protein isolate and gum acacia and on the physicochemical properties of conjugates. Journal of Agricultural and Food Chemistry,2010.58(7):p.4494-4499.
    [112]Li, C., Liu, F., Gong, Y., et al., Investigation into the Maillard reaction between ε-polylysine and dextran in subcritical water and evaluation of the functional properties of the conjugates. LWT-Food Science and Technology,2014.57(2):p.612-617.
    [113]Yajima, K., Onodera, S., Takeda, Y., et al., Improved radical scavenging activity of β-lactoglobulin-xylobiose modified by the Maillard reaction.2007.
    [114]Yadav, M.P., Strahan, G.D., Mukhopadhyay, S., et al., Formation of corn fiber gum-milk protein conjugates and their molecular characterization. Food Hydrocolloids,2012.26(2):p.326-333.
    [115]Du, Y., Shi, S., Jiang, Y., et al., Physicochemical properties and emulsion stabilization of rice dreg giutelin conjugated with κ-carrageenan through Maillard reaction. Journal of the Science of Food and Agriculture,2013.93(1):p.125-133.
    [116]Wong, B.T., Day, L. and Augustin, M.A. Deamidated wheat protein-dextran Maillard conjugates:Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocolloids,2011.25(6):p.1424-1432.
    [117]Lertittikul, W., Benjakul, S. and Tanaka, M. Characteristics and antioxidative activity of Maillard reaction products from a porcine plasma protein-glucose model system as influenced by pH. Food Chemistry,2007.100(2):p.669-677.
    [118]Wooster, T.J. and Augustin, M.A. p-Lactoglobulin-dextran Maillard conjugates:Their effect on interfacial thickness and emulsion stability. Journal of colloid and interface science,2006.303(2): p.564-572.
    [119]Wooster, T.J. and Augustin, M.A. Rheology of whey protein-dextran conjugate films at the air/water interface. Food Hydrocolloids,2007.21(7):p.1072-1080.
    [120]Wooster, T.J. and Augustin, M.A. The emulsion flocculation stability of protein-carbohydrate diblock copolymers. Journal of colloid and interface science,2007.313(2):p.665-675.
    [121]Hellwig, M. and Henle, T. Release of pyrraline in absorbable peptides during simulated digestion of casein glycated by 3-deoxyglucosone. European Food Research and Technology, 2013.237(1):p.47-55.
    [122]Hong, P.K., Gottardi, D., Ndagijimana, M., et al., Glycation and transglutaminase mediated glycosylation of fish gelatin peptides with glucosamine enhance bioactivity. Food Chemistry, 2014.142(0):p.285-293.
    [123]ter Haar, R., Schols, H.A. and Gruppen, H. Effect of saccharide structure and size on the degree of substitution and product dispersity of a-lactalbumin glycated via the Maillard reaction. Journal of Agricultural and Food Chemistry,2011.59(17):p.9378-9385.
    [124]Cardoso, J., Albuquerque Jr, R.L.C., Padilha, F.F., et al., Effect of the Maillard reaction on properties of casein and casein films. Journal of Thermal Analysis and Calorimetry,2011.104(1): p.249-254.
    [125]Cerny, C. and Guntz-Dubini, R. Formation of cysteine-S-conjugates in the Maillard reaction of cysteine and xylose. Food Chemistry,2013.141(2):p.1078-1086.
    [126]You, J., Luo, Y., Shen, H., et al., Effect of substrate ratios and temperatures on development of Maillard reaction and antioxidant activity of silver carp (Hypophthalmichthys molitrix) protein hydrolysate-glucose system. International Journal of Food Science & Technology,2011.46(12): p.2467-2474.
    [127]Sun, Y., Hayakawa, S. and Izumori, K. Modification of ovalbumin with a rare ketohexose through the Maillard reaction:effect on protein structure and gel properties. Journal of Agricultural and Food Chemistry,2004.52(5):p.1293-1299.
    [128]Liu, Y, Zhao, G, Zhao, M., et al., Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction. Food Chemistry,2012.131(3):p. 901-906.
    [129]Lesmes, U. and McClements, D.J. Controlling lipid digestibility:Response of lipid droplets coated by β-lactoglobulin-dextran Maillard conjugates to simulated gastrointestinal conditions. Food Hydrocolloids,2012.26(1):p.221-230.
    [130]Wu, S., Hu, J., Wei, L., et al., Antioxidant and antimicrobial activity of Maillard reaction products from xylan with chitosan/chitooligomer/glucosamine hydrochloride/taurine model systems. Food Chemistry,2014.148:p.196-203.
    [131]Benjakul, S., Lertittikul, W. and Bauer, F. Antioxidant activity of Maillard reaction products from a porcine plasma protein-sugar model system. Food Chemistry,2005.93(2):p.189-196.
    [132]Jing, H., Yap, M., Wong, P.YY, et al., Comparison of physicochemical and antioxidant properties of egg-white proteins and fructose and inulin Maillard reaction products. Food and Bioprocess Technology,2011.4(8):p.1489-1496.
    [133]Joubran, Y, Mackie, A. and Lesmes, U. Impact of the Maillard reaction on the antioxidant capacity of bovine lactoferrin. Food Chemistry,2013.141(4):p.3796-3802.
    [134]Yamabe, N., Kim, Y.J., Lee, S., et al., Increase in antioxidant and anticancer effects of ginsenoside Re-lysine mixture by Maillard reaction. Food Chemistry,2013.138(2-3):p. 876-883.
    [135]Manzocco, L., Calligaris, S., Mastrocola, D., et al., Review of non-enzymatic browning and antioxidant capacity in processed foods. Trends in Food Science & Technology,2000.11(9):p. 340-346.
    [136]Moon, J.-K. and Shibamoto, T. Formation of carcinogenic 4 (5)-methylimidazole in Maillard reaction systems. Journal of Agricultural and Food Chemistry,2010.59(2):p.615-618.
    [137]Markman, G. and Livney, YD. Maillard-conjugate based core-shell co-assemblies for nanoencapsulation of hydrophobic nutraceuticals in clear beverages. Food & Function,2012. 3(3):p.262-270.
    [138]Jiang, Z., Rai, D.K., O'Connor, P.M., et al., Heat-induced Maillard reaction of the tripeptide IPP and ribose:Structural characterization and implication on bioactivity. Food Research International,2013.50(1):p.266-274.
    [139]Ames, J.M., Evidence against dietary advanced glycation endproducts being a risk to human health. Molecular Nutrition & Food Research,2007.51(9):p.1085-1090.
    [140]Somoza, V., Five years of research on health risks and benefits of Maillard reaction products: An update. Molecular Nutrition & Food Research,2005.49(7):p.663-672.
    [141]Zhang, J., Wu, N., Lan, T., et al., Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis. Food Hydrocolloids,2012.28(2):p.301-312.
    [142]Oliver, C.M., Insight into the glycation of milk proteins:an ESI-and MALDI-MS perspective (review). Critical Reviews in Food Science and Nutrition,2011.51(5):p.410-431.
    [143]Yamaguchi, K., Homma, T., Nomi, Y., et al., Characterisation of Maillard reaction products derived from LEKFD-A pentapeptide found in β-lactoglobulin sequence, glycated with glucose-By tandem mass spectrometry, molecular orbital calculations and gel filtration chromatography coupled with continuous photodiode array. Food Chemistry,2014.145(0):p.892-902.
    [144]Gu, F.-L., Kim, J., Abbas, S., et al., Structure and antioxidant activity of high molecular weight Maillard reaction products from casein-glucose. Food Chemistry,2010.120(2):p.505-511.
    [145]Khan, T.A., S. Amani, and A. Naeem, Glycation promotes the formation of genotoxic aggregates in glucose oxidase. Amino Acids,2012.43(3):p.1311-1322.
    [146]Niu, L.Y., Jiang, S.T., Pan, L.J., et al., Characteristics and functional properties of wheat germ protein glycated with saccharides through Maillard reaction. International Journal of Food Science & Technology,2011.46(10):p.2197-2203.
    [147]Turner, J.A., Sivasundaram, L.R., Ottenhof, M.A.., et al., Monitoring chemical and physical changes during thermal flavor generation. Journal of Agricultural and Food Chemistry,2002. 50(19):p.5406-5411.
    [148]Stanic-Vucinic, D., Prodic, I., Apostolovic, D., et al., Structure and antioxidant activity of β-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. Food Chemistry,2013.138(1):p.590-599.
    [149]Medrano, A., Abirached, C., Panizzolo, L., et al., The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chemistry,2009.113(1):p.127-133.
    [150]Tang, C.-H., Sun, X. and Foegeding, E.A. Modulation of physicochemical and conformational properties of kidney bean vicilin (Phaseolin) by glycation with glucose:implications for structure-function relationships of legume vicilins. Journal of Agricultural and Food Chemistry, 2011.59(18):p.10114-10123.
    [151]Quaglia, G.B. and Orban, E. Influence of enzymatic hydrolysis on structure and emulsifying properties of sardine(Sardina pilchardus) protein hydrolysates. Journal of Food Science,1990. 55(6):p.1571-1573.
    [152]Bougatef, A., Nedjar-Arroume, N., Manni, L., et al., Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins. Food Chemistry,2010.118(3):p.559-565.
    [153]Gibbs, B.F., Zougman, A., Masse, R., et al., Production and characterization of bioactive peptides from soy hydrolysate and soy-fermented food. Food Research International,2004.37(2): p.123-131.
    [154]Chai, H.-J., Chan, Y.-L., Tsung-Lin, S., et al., Evaluation of lanternfish(Benthosema pterotum) hydrolysates as antioxidants against hydrogen peroxide induced oxidative injury. Food Research International,2013.54(2):p.1409-1418.
    [155]Samaranayaka, A.G.P. and Li-Chan, E.C.Y. Autolysis-assisted production of fish protein hydrolysates with antioxidant properties from Pacific hake(Merluccius productus). Food Chemistry,2008.107(2):p.768-776.
    [156]Samaranayaka, A.GP. and Li-Chan, E.C.Y. Food-derived peptidic antioxidants:A review of their production, assessment, and potential applications. Journal of Functional Foods,2011.3(4): p.229-254.
    [157]Adler-Nissen, J., Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry,1979.27(6):p. 1256-1262.
    [158]Bersuder, P., Hole, M. and Smith, G Antioxidants from a heated histidine-glucose model system. I:Investigation of the antioxidant role of histidine and isolation of antioxidants by high-performance liquid chromatography. Journal of the American Oil Chemists'Society,1998. 75(2):p.181-187.
    [159]Decker, E.A. and Welch, B. Role of ferritin as a lipid oxidation catalyst in muscle food. Journal of Agricultural and Food Chemistry,1990.38(3):p.674-677.
    [160]Yildinm, A., Mavi, A. and Kara, A.A. Determination of antioxidant and antimicrobial activities of rumex crispus L. extracts. Journal of Agricultural and Food Chemistry,2001.49(8):p. 4083-4089.
    [161]Klompong, V., Benjakul, S., Kantachote, D., et al., Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry,2007.102(4):p.1317-1327.
    [162]Dong, S., Zeng, M., Wang, D., et al., Antioxidant and biochemical properties of protein hydrolysates prepared from Silver carp (Hypophthalmichthys molitrix). Food Chemistry,2008. 107(4):p.1485-1493.
    [163]Chang, C.-Y., Wu, K.-C. and Chiang, S.-H. Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates. Food Chemistry,2007.100(4):p.1537-1543.
    [164]彭新颜,孔保华,熊幼翎,由碱性蛋白酶制备的乳清蛋白水解物抗氧化活性的研究.中国乳品工业,2008(04):p.8-12+47.
    [165]Juntachote, T. and Berghofer, E. Antioxidative properties and stability of ethanolic extracts of Holy basil and Galangal. Food Chemistry,2005.92(2):p.193-202.
    [166]张强,周正义,王松华,从米糠中制备抗氧化肽的研究.食品工业科技,2007(07):p.145-147.
    [167]Prior, R.L., Wu, X. and Schaich, K. Standardized methods for the determination of antioxidant capacity and phenolics in foods and dietary supplements. Journal of Agricultural and Food Chemistry,2005.53(10):p.4290-4302.
    [168]陈力宏,董英,孙艳辉,酶法制备蚕茧层抗氧化多肽水解液的研究.蚕业科学,2006(03):p.442-445.
    [169]孙骞,胡鑫,罗永康等,猪血红蛋白抗氧化肽的酶法制备及其体外抗氧化活力观察.中国农业大学学报,2008(04):p.77-81.
    [170]Bougatef, A., Balti, R., Zaied, S.B., et al., Pepsinogen and pepsin from the stomach of smooth hound(Mustelus mustelus):Purification, characterization and amino acid terminal sequences. Food Chemistry,2008.107(2):p.777-784.
    [171]李琳,赵谋明,鳙鱼蛋白酶解液清除自由基的研究.水产科学,2005(10):p.15-18.
    [172]毛学英,李明,李敏,等,不同因素对酪蛋白酶解产物螯合亚铁盐能力的影响.食品科学,2008(05):p.145-148.
    [173]许庆陵,曾庆祝,朱莉娜,等,鲢酶解物对羟自由基的清除作用.水产学报,2004(01):p.93-99.
    [174]李华,李佩洪,王晓宇,等,抗氧化检测方法的相关性研究.食品与生物技术学报,2008(04):p.6-11.
    [175]Elias, R.J., Kellerby, S.S. and Decker, E.A. Antioxidant activity of proteins and peptides. Critical Reviews in Food Science and Nutrition,2008.48(5):p.430-441.
    [176]Wang, W., Mejia, D. and Gonzalez, E. A new frontier in soy bioactive peptides that may Prevent age-related chronic diseases. Comprehensive Reviews in Food Science and Food Safety,2005. 4(4):p.63-78.
    [177]Hsu, K.-C., Purification of antioxidative peptides prepared from enzymatic hydrolysates of tuna dark muscle by-product. Food Chemistry,2010.122(1):p.42-48.
    [178]Wang, B., Li, L., Chi, C.F., et al., Purification and characterisation of a novel antioxidant peptide derived from blue mussel (My til us edulis) protein hydrolysate. Food Chemistry,2013. 138(2-3):p.1713-1719.
    [179]陈志军,鲢鱼蛋白酶法改性及其产物的结构和功能研究,[硕士学位论文]湖南:长沙理工大学,2013.
    [180]冯光,超滤和反渗透分离技术的原理及应用.中国食品工业,2013(3):p.42-44.
    [181]汪家政,范明,蛋白质技术手册.北京:科学出版社.2000.
    [182]Gu, Y. and Wu, J. LC-MS/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins. Food Chemistry,2013.141(3):p. 2682-2690.
    [183]He, R., Girgih, A., Malomo, S., et al., Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions. Journal of Functional Foods,2013.5(1): p.219-227.
    [184]Sabeena Farvin, K.H., Andersen, L.L., Nielsen, H.H., et al., Antioxidant activity of Cod (Gadus morhua) protein hydrolysates:In vitro assays and evaluation in 5% fish oil-in-water emulsion. Food Chemistry,2014.149:p.326-334.
    [185]Holder, A., Birke, A., Eisele, T., et al., Selective isolation of angiotensin-I-converting enzyme-inhibitory peptides from micellar casein and β-casein hydrolysates via ultrafiltration. International Dairy Journal,2013.31(1):p.34-40.
    [186]Doyen, A., Udenigwe, C.C., Mitchell, P.L., et al., Anti-diabetic and antihypertensive activities of two flaxseed protein hydrolysate fractions revealed following their simultaneous separation by electrodialysis with ultrafiltration membranes. Food Chemistry,2014.145:p.66-76.
    [187]Pyrzynska, K. and Pekal, A. Application of free radical diphenylpicrylhydrazyl (DPPH) to estimate the antioxidant capacity of food samples. Analytical Methods,2013.5(17):p. 4288-4295.
    [188]Pan, D., Cao, J., Guo, H., et al., Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate. Food Chemistry,2012.130(1):p. 121-126.
    [189]Yu, X., Zhao, M., Liu, F., et al., Identification of 2,3-dihydro-3,5-dihydroxy-6-methyl-4H-pyran-4-one as a strong antioxidant in glucose-histidine Maillard reaction products. Food Research International,2013.51(1):p.397-403.
    [190]Ajibola, C.F., Fashakin, J.B., Fagbemi, T.N., et al., Effect of peptide size on antioxidant properties of African yam beanseed (Sphenostylis stenocarpa) protein hydrolysate fractions. International Journal of Molecular Sciences,2011.12(10):p.6685-6702.
    [191]Tang, C.-H., Wang, X.-S. and Yang, X.-Q. Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates. Food Chemistry,2009.114(4):p.1484-1490.
    [192]Lapsongphon, N. and Yongsawatdigul, J. Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp. SK.37 proteinase. Food Chemistry,2013. 141(2):p.992-999.
    [193]Toldra, L.M.L.N.F., Food Analysis by HPLC, U.S.:CRC Press,2012
    [194]Ren, J., Zhao, M., Shi, J., et al., Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chemistry,2008.108(2):p.727-736.
    [195]Luo, H.-Y., Wang, B., Li, Z.-R., et al., Preparation and evaluation of antioxidant peptide from papain hydrolysate of Sphyrna lewini muscle protein. LWT-Food Science and Technology, 2013.51(1):p.281-288.
    [196]Megfas, C., Pedroche, J., Yust, M.M., et al., Affinity purification of copper-chelating peptides from sunflower protein hydrolysates. Journal of Agricultural and Food Chemistry,2007.55(16): p.6509-6514.
    [197]Hernandez-Ledesma, B., Amigo, L., Recio, I., et al., ACE-Inhibitory and radical-scavenging activity of peptides derived from (J-Lactoglobulin f(19-25). Interactions with Ascorbic Acid. Journal of Agricultural and Food Chemistry,2007.55(9):p.3392-3397.
    [198]Zhu, L., Chen, J., Tang, X., et al., Reducing, radical scavenging, and chelation properties of in vitro digests of alcalase-treated zein hydrolysate. J Agric Food Chem,2008.56(8):p.2714-21.
    [199]Tagliazucchi, D., Verzelloni, E. and Conte, A. Effect of dietary melanoidins on lipid peroxidation during simulated gastric digestion:Their possiblerole in the prevention of oxidative damage. Journal of Agricultural and Food Chemistry,2010.58(4):p.2513-2519.
    [200]Mesa, M.D., Silvan, J.M., Olza, J., et al., Antioxidant properties of soy protein fructooligosaccharide glycation systems and its hydrolyzates. Food Research International,2008. 41(6):p.606-615.
    [201]Morales, F., Martin, S., Acar,O., et al., Antioxidant activity of cookies and its relationship with heat-processing contaminants:a risk/benefit approach. European Food Research and Technology, 2009.228(3):p.345-354.
    [202]Maillard, M.N., Billaud, C., Chow, Y.N., et al., Free radical scavenging, inhibition of polyphenoloxidase activity and copper chelating properties of model Maillard systems. LWT Food Science and Technology,2007.40(8):p.1434-1444.
    [203]Kuda, T. and Yano, T. Changes of radical-scavenging capacity and ferrous reducing power in chub mackerel Scomber japonicus and Pacific saury Cololabis saira during 4 ℃ storage and retorting. LWT-Food Science and Technology,2009.42(6):p.1070-1075.
    [204]Silvan, J.M., van de Lagemaat, J., Olano, A., et al., Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods. Journal of Pharmaceutical and Biomedical Analysis,2006.41(5):p.1543-1551.
    [205]Giroux, H.J., Houde, J. and Britten, M. Use of heated milk protein-sugar blends as antioxidant in dairy beverages enriched with linseed oil. LWT-Food Science and Technology,2010.43(9): p.1373-1378.
    [206]Hwang, I.G., Kim, H.Y., Woo, K.S., et al., Biological activities of Maillard reaction products (MRPs) in a sugar-amino acid model system. Food Chemistry,2011.126(1):p.221-227.
    [207]Rufian-Henares, J.A. and Delgado-Andrade, C. Effect of digestive process on Maillard reaction indexes and antioxidant properties of breakfast cereals. Food Research International,2009.42(3): p.394-400.
    [208]Chen, S.-L., Jin, S.-Y. and Chen, C.-S. Relative reactivities of glucose and galactose in browning and pyruvaldehyde formation in sugar/glycine model systems. Food Chemistry,2005. 92(4):p.597-605.
    [209]Liu, S.-C, Yang, D.-J., Jin, S.-Y., et al., Kinetics of color development, pH decreasing, and anti-oxidative activity reduction of Maillard reaction in galactose/glycine model systems. Food Chemistry,2008.108(2):p.533-541.
    [210]Lan, X., Liu, P., Xia, S., et al., Temperature effect on the non-volatile compounds of Maillard reaction products derived from xylose-soybean peptide system:Further insights into thermal degradation and cross-linking. Food Chemistry,2010.120(4):p.967-972.
    [211]Reyes, F.G.R., Poocharoen, B. and Wrolstad, R.E. Maillard browning reaction of sugar-glycine model systems:Changes in sugar concentration, color and appearance. Journal of Food Science, 1982.47(4):p.1376-1377.
    [212]Delgado-Andrade, C., Seiquer, I., Haro, A., et al., Development of the Maillard reaction in foods cooked by different techniques. Intake of Maillard-derived compounds. Food Chemistry, 2010.122(1):p.145-153.
    [213]Morales, F. and Jimenez-Perez, S. Peroxyl radical scavenging activity of melanoidins in aqueous systems. European Food Research and Technology,2004.218(6):p.515-520.
    [214]Sun, W., Zhao, M., Cui, C., et al., Effect of Maillard reaction products derived from the hydrolysate of mechanically deboned chicken residue on the antioxidant, texrural and sensory properties of Cantonese sausages. Meat Science,2010.86(2):p.276-282.
    [215]Rufian-Henares, J.A. and Morales, F.J. A new application of a commercial microtiter plate-based assay for assessing the antimicrobial activity of Maillard reaction products. Food Research International,2006.39(1):p.33-39.
    [216]Yilmaz, Y. and Toledo, R. Antioxidant activity of water-soluble Maillard reaction products. Food Chemistry,2005.93(2):p.273-278.
    [217]Matmaroh, K., Benjakul, S. and Tanaka, M. Effect of reactant concentrations on the Maillard reaction in a fructose-glycine model system and the inhibition of black tiger shrimp polyphenoloxidase. Food Chemistry,2006.98(1):p.1-8.
    [218]Matthaus, B., Antioxidant activity of extracts obtained from residues of different oilseeds. Journal of Agricultural and Food Chemistry,2002.50(12):p.3444-3452.
    [219]Sumaya-Martinez, M.T., Thomas, S., Linard B., et al., Effect of Maillard reaction conditions on browning and antiradical activity of sugar-tuna stomach hydrolysate model system. Food Research International,2005.38(8-9):p.1045-1050.
    [220]Huang, D., Ou, B. and Prior, R.L. The chemistry behind antioxidant capacity assays. Journal of Agricultural and Food Chemistry,2005.53(6):p.1841-1856.
    [221]Zhang, L., Li, J. and Zhou, K. Chelating and radical scavenging activities of soy protein hydrolysates prepared from microbial proteases and their effect on meat lipid peroxidation. Bioresource Technology,2010.101(7):p.2084-2089.
    [222]Toshihaaru Gomyo, M.H., On the interaction of melanoidin with metallic ions. Agricultural and Biological Chemistry,1976.40:p.33-40.
    [223]Hofmann, T., Studies on the relationship between molecular weight and the color potency of fractions obtained by thermal treatment of glucose/amino acid and glucose/protein solutions by using ultracentrifugation and color dilution techniques. Journal of Agricultural and Food Chemistry,1998.46(10):p.3891-3895.
    [224]Yanagimoto, K., Lee, K.-G., Ochi, H., et al., Antioxidative activity of heterocyclic compounds formed in Maillard reaction products. International Congress Series,2002.1245(0):p.335-340.
    [225]Cho, M., Lee, H.-S., Kang, I.-J., et al., Antioxidant properties of extract and fractions from Enteromorpha prolifera, a type of green seaweed. Food Chemistry,2011.127(3):p.999-1006.
    [226]Balange, A.K. and Benjakul, S. Cross-linking activity of oxidised tannic acid towards mackerel muscle proteins as affected by protein types and setting temperatures. Food Chemistry,2010. 120(1):p.268-277.
    [227]Chaijan, M., Jongjareonrak, A., Phatcharat, S., et al., Chemical compositions and characteristics of farm raised giant catfish (Pangasianodon gigas) muscle. LWT-Food Science and Technology, 2010.43(3):p.452-457.
    [228]Sathivel, S., Bechtel, P., Babbitt, J.K., et al., Functional, nutritional, and rheological properties of protein powders from arrowtooth flounder and their application in mayonnaise. Journal of Food Science,2005.70(2):p. E57-E63.
    [229]Krasaechol, N., Sanguandeekul, R., Duangmal, K., et al., Structure and functional properties of modified threadfin bream sarcoplasmic protein. Food Chemistry,2008.107(1):p.1-10.
    [230]Liu, H., Yin, L., Zhang, N., et al., Isolation of cathepsin B from the muscle of silver carp (Hypophthalmichthys molitrix) and comparison of cathepsins B and L actions on surimi gel softening. Food Chemistry,2008.110(2):p.310-318.
    [231]Bourtoom, T., Chinnan, M.S., Jantawat, P., et al., Recovery and characterization of proteins precipitated from surimi wash-water. LWT-Food Science and Technology,2009.42(2):p. 599-605.
    [232]Yongsawatdigul, J. and Hemung, B.-O. Structural changes and functional properties of threadfin bream sarcoplasmic proteins subjected to pH-shifting treatments and lyophilization. Journal of Food Science,2010.75(3):p. C251-C257.
    [233]Van der Plancken, I., Van Loey, A. and Hendrickx, M.E. Effect of heat-treatment on the physico-chemical properties of egg white proteins:A kinetic study. Journal of food engineering, 2006.75(3):p.316-326.
    [234]Johnson, R., Lewis, L., Freeze-drying protein formulations above their collapse temperatures: Possible issues and concerns. American Pharmaceutical Review,2011.14:p.50-54.
    [235]Hu, X.-Z., Cheng, Y.-Q., Fan, J.-F., et at., Effects of drying method on physicochemical and functional properties of soy protein isolates. Journal of Food Processing and Preservation,2010. 34(3):p.520-540.
    [236]Pearce, K.N. and Kinsella, J.E. Emulsifying properties of proteins:evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry,1978.26(3):p.716-723.
    [237]Benjakul, S., Visessanguan, W., Thongkaew, C., et al., Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage. Food Research International,2003.36(8):p.787-795.
    [238]Leelapongwattana, K., Benjakul, S., Visessanguan, W., et al., Physicochemical and biochemical changes during frozen storage of minced flesh of lizardfish(Saurida micropectoralis). Food Chemistry,2005.90(1-2):p.141-150.
    [239]Chan, J.K., Gill, T.A. and Paulson, A.T. The dynamics of thermal denaturation offish myosins. Food Research International,1992.25(2):p.117-123.
    [240]Sankar, T.V. and Ramachandran, A. Thermal stability of myofibrillar protein from Indian major carps. Journal of the Science of Food and Agriculture,2005.85(4):p.563-568.
    [241]Yongsawatdigul, J. and Park, J.W. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry,2003.83(3):p.409-416.
    [242]Omana, D.A., Xu, Y., Moayedi, V, et al., Alkali-aided protein extraction from chicken dark meat:Chemical and functional properties of recovered proteins. Process Biochemistry,2010. 45(3):p.375-381.
    [243]Sun, W., Zhou, F., Zhao, M, et al., Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility. Food Chemistry,2011.129(2):p.472-478.
    [244]Yongsawatdigul, J. and Piyadhammaviboon, P. Gel-enhancing effect and protein cross-linking ability of tilapia sarcoplasmic proteins. Journal of the Science of Food and Agriculture,2007. 87(15):p.2810-2816.
    [245]Gratacos-Cubarsi, M. and Lametsch, R. Determination of changes in protein conformation caused by pH and temperature. Meat Science,2008.80(2):p.545-549.
    [246]Ramachandran, D., Mohan, M. and Sankar, T.V. Physicochemical characteristics of muscle proteins from barracuda (Sphyraena jello) of different weight groups. LWT-Food Science and Technology,2007.40(8):p.1418-1426.
    [247]Tadpitchayangkoon, P., Park, J.W., Mayer, S.G., et al., Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method. Journal of Agricultural and Food Chemistry,2010.58(7):p.4241-4249.
    [248]Altinelataman, C., Kundiger, R., Cakli, S., et al., Comparison of IEF patterns of sarcoplasmic proteins offish from North Atlantic and Aegean Sea. Food Control,2009.20(11):p.980-985.
    [249]Chen, T.-Y., Shiau, C.-Y., Noguchi, T., et al., Identification of puffer fish species by native isoelectric focusing technique. Food Chemistry,2003.83(3):p.475-479.
    [250]Nicolai, T., Britten, M. and Schmitt, C.β-Lactoglobulin and WP1 aggregates:Formation, structure and applications. Food Hydrocolloids,2011.25(8):p.1945-1962.
    [251]Deng, Q., Wang, L., Wei, F, et al., Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds. Food Chemistry,2011.124(4):p.1458-1465.
    [252]Tang, C.-H. and Sun, X. A comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes:Implications for the structure-function relationship. Food Hydrocolloids,2011.25(3):p.315-324.
    [253]Rocha-Estrada, J.G., Cordova-Murueta, J.H. and Garcia-Carreno, F.L. Functional properties of protein from frozen mantle and fin of jumbo squid dosidicus gigas in function of pH and ionic strength. Food Science and Technology International,2010.16(5):p.451-458.
    [254]Chan, J.T.Y., Omana, D.A. and Betti, M. Effect of ultimate pH and freezing on the biochemical properties of proteins in turkey breast meat. Food Chemistry,2011.127(1):p.109-117.
    [255]Thawornchinsombut, S. and Park, J.W. Role of pH in solubility and conformational changes of pacific whiting muscle proteins. Journal of Food Biochemistry,2004.28(2):p.135-154.
    [256]Sanmartin, E., Arboleya, J.C., Villamiel, M, et al., Recent advances in the recovery and improvement of functional proteins from fish processing by-products:Use of protein glycation as an alternative method. Comprehensive Reviews in Food Science and Food Safety,2009.8(4):p. 332-344.
    [257]Thongraung, C. and Kangsanan, S. Influence of pH, NaCl and pre-incubation on utilisation of surimi wash water in generation of antioxidative material by using the Maillard reaction. International Journal of Food Science & Technology,2010.45(8):p.1696-1702.
    [258]Bae, J., Yoon, S. and Lim, S. Heavy metal contents and chemical compositions of atlantic (Scomber scombrus), blue(Scomber australasicus), and chub(Scomber japonicus) mackerel muscles. Food Science and Biotechnology,2011.20(3):p.709-714.
    [259]Sun, Q. and Luo, Y. Effect of Maillard reaction conditions on radical scavenging activity of porcine haemoglobin hydrolysate-sugar model system. International Journal of Food Science & Technology,2011.46(2):p.358-364.
    [260]Qi, J.-R., Yang, X.-Q. and Liao, J.-S. Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction. International Journal of Food Science & Technology,2009.44(11):p.2296-2302.
    [261]Takeda, H., Iida, T., Okada, A., et al., Feasibility study on water solubilization of spawned out salmon meat by conjugation with alginate oligosaccharide. Fisheries Science,2007.73(4):p. 924-930.
    [262]Gu, X., Campbell, L.J. and Euston, S.R. Influence of sugars on the characteristics of glucono-δ-lactone-induced soy protein isolate gels. Food Hydrocolloids,2009.23(2):p.314-326.
    [263]Sun, Y., Hayakawa, S., Chuamanochan, M., et al., Antioxidant effects of Maillard reaction products obtained from ovalbumin and different D-aldohexoses. Bioscience, biotechnology, and biochemistry,2006.70(3):p.598-605.
    [264]Enomoto, H., Li, C.-P., Morizane, K., et al., Glycation and phosphorylation of P-lactoglobulin by dry-heating:Effect on protein structure and some properties. Journal of Agricultural and Food Chemistry,2007.55(6):p.2392-2398.
    [265]Achouri, A., Boye, J., Yaylayan, V.A. et al., Functional properties of glycated soy 11S glycinin. Journal of Food Science,2005.70(4):p.269-274.