草鱼肌原纤维蛋白-葡萄糖糖基化产物的理化特性及乳化特性研究
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摘要
选取葡萄糖作为糖基供体对草鱼肌原纤维蛋白进行糖基化修饰,探讨糖基化产物理化性质及其乳化性能。草鱼肌原纤维蛋白与葡萄糖按质量比1∶2混合,在相对湿度为44%、50℃条件下进行糖基化反应,测定产物的糠氨酸含量、荧光强度、游离氨基含量、蛋白质二级结构以及乳化性和乳化稳定性。结果表明:随着加热时间的延长,糠氨酸含量和荧光强度呈现先增大后降低的趋势,游离氨基含量和褐变强度ΔE持续增加(p<0.05),其中在反应48 h时,糠氨酸含量达到最大值((4.09±0.07)mg/100 mg样品);二级结构分析表明,糖基化对草鱼肌原纤维蛋白的二级结构影响较小。此外,糖基化修饰显著提高了草鱼肌原纤维蛋白的乳化性能(p<0.05),且经过48 h制备的糖基化产物的乳化活性及乳化稳定性最高,分别为未反应草鱼肌原纤维蛋白的1.32倍(p<0.05)和1.53倍(p<0.05)。进一步通过相关性分析发现,草鱼肌原纤维蛋白的乳化性受糖基化反应程度的影响。
Glucose was used as a glycosyl donor to glycosylate the grass carp myofibrillar protein to investigate the physicochemical properties and emulsifying properties of glycosylation production. The reaction products of grass carp myofibrillar protein and glucose mixture( 1∶ 2,w/w) were prepared by dry-heating at 50 ℃ and 44% relative humidity,and the content of furosine,free amino group,fluorescence intensity and secondary structure,and emulsifying property and emulsifying stability of the conjugates were further analyzed.Results showed that,as dry-heating time was prolonged,the content of furosine and the fluorescence intensity firstly increased and then decreased; and the total colour difference( ΔE) increased( p < 0.05),and for 48 h of dry-heating,the content of furosine reached the maximum(( 4.09 ± 0.07) mg/100 mg). Structural analyses suggested that glycosylation had little effects on the secondary structure of myofibrillar protein. Moreover,the glycation significantly improved the emulsifying activity( EAI) and emulsifying stability( ESI) of grass carp myofibrillar protein( p <0.05),and the conjugates prepared from 48 h of dry-heating showed the highest ability of EAI and ESI,which was 1.32 and1.53 times of original grass carp myofibrillar protein,respectively.Furthermore,the extent of glycation clearly affected the ability of EAI and ESI of grass carp myofibrillar protein based on the correlation analysis.
Glucose was used as a glycosyl donor to glycosylate the grass carp myofibrillar protein to investigate the physicochemical properties and emulsifying properties of glycosylation production. The reaction products of grass carp myofibrillar protein and glucose mixture( 1∶ 2,w/w) were prepared by dry-heating at 50 ℃ and 44% relative humidity,and the content of furosine,free amino group,fluorescence intensity and secondary structure,and emulsifying property and emulsifying stability of the conjugates were further analyzed.Results showed that,as dry-heating time was prolonged,the content of furosine and the fluorescence intensity firstly increased and then decreased; and the total colour difference( ΔE) increased( p < 0.05),and for 48 h of dry-heating,the content of furosine reached the maximum(( 4.09 ± 0.07) mg/100 mg). Structural analyses suggested that glycosylation had little effects on the secondary structure of myofibrillar protein. Moreover,the glycation significantly improved the emulsifying activity( EAI) and emulsifying stability( ESI) of grass carp myofibrillar protein( p <0.05),and the conjugates prepared from 48 h of dry-heating showed the highest ability of EAI and ESI,which was 1.32 and1.53 times of original grass carp myofibrillar protein,respectively.Furthermore,the extent of glycation clearly affected the ability of EAI and ESI of grass carp myofibrillar protein based on the correlation analysis.
引文
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[7]Fujiwara K,Oosawa T,Saeki H.Improved thermal stability and emulsifying properties of carp myofibrillar proteins by conjugation with dextran.[J].Journal of Agricultural and Food Chemistry,1998,46(4):1257-1261.
[8]陈欣,周春霞,洪鹏志,等.糖基化改性对罗非鱼肉肌原纤维蛋白功能特性的影响[J].现代食品科技,2010,26(8):793-796.
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[13]丛艳君,苘钰婷,易红.草鱼内脏蛋白酶解产物美拉德反应制备调味基料[J].食品科学,2014,35(22):6-10.
[14]郭晶晶.草鱼肉酶解液美拉德反应制备鱼味香精及其电子舌感官评定方法[D].镇江:江苏大学,2014.
[15]Cong Y J,Yu-Ting Q,Hong Y I.Preparation of flavoring base from enzymatic hydrolysate of visceral waste proteins of grass carp through maillard reaction[J].Food Science,2014.
[16]赵谋明,刘洋,张佳男,等.木糖-草鱼肽美拉德反应产物的抗氧化性[J].农业工程学报,2014,30(9):279-286.
[17]Li Z,Jiang M,You J,et al.Impact of Maillard reaction conditions on the antigenicity of parvalbumin,the major allergen in grass carp[J].Food and Agricultural Immunology,2014,25(4):486-497.
[18]Liu Q,Chen Q,Kong B,et al.The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp(Cyprinus carpio)surimi[J].LWT-Food Science and Technology,2014,57(2):603-611.
[19]Han K,Yao Y,Dong S,et al.Chemical characterization of the glycated myofibrillar proteins from grass carp(Ctenopharyngodon idella)and their impacts on the human gut microbiota in vitro fermentation.[J].Food and Function,2017,8(3).
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[21]Jvande L,Manuel S J,Javier M F,et al.In vitro glycation and antigenicity of soy proteins[J].Food Research International,2007,40(1):153-160.
[22]Morale F J.Optimised Procedure to Analyse Maillard Reaction Associated Fluorescence in Cereal-Based Products[J].Czech Journal of Food Sciences,2008,26(5):339-346.
[23]李向红,王发祥,张付兰,等.冷藏过程中草鱼肌原纤维蛋白结构的变化[J].食品与发酵工业,2015,41(10):177-181.
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[25]Yamaguchi K,Nomi Y,Homma T,et al.Determination of furosine and fluorescence as markers of the Maillard reaction for the evaluation of meat products during actual cooking conditions[J].Food Science and Technology Research,2012,18(1):67-76.
[26]Pirestani S,Nasirpour A,Keramat J,et al.Preparation of chemically modified canola protein isolate with gum Arabic by means of Maillard reaction under wet-heating conditions[J].Carbohydrate Polymers,2017,155:201.
[27]Jing H,Kitts D D.Chemical and biochemical properties of casein-sugar Maillard reaction products[J].Food and Chemical Toxicology An International Journal Published for the British Industrial Biological Research Association,2002,40(7):1007.
[28]Boekel M A J S V.Kinetic aspects of the Maillard reaction:A critical review[J].Molecular Nutrition and Food Research,2001,45(3):150-9.
[29]Sun W W,Yu S J,Zeng X A,et al.Properties of whey protein isolate-dextran conjugate prepared using pulsed electric field[J].Food Research International,2011,44(4):1052-1058.
[30]Guo X,Xiong Y L.Characteristics and functional properties of buckwheat protein-sugar Schiff base complexes[J].LWT-Food Science and Technology,2013,51(2):397-404.
[31]Matiacevich S B,Buera M P.A critical evaluation of fluorescence as a potential marker for the Maillard reaction[J].Food Chemistry,2006,95(3):423-430.
[32]Tarassuk N P,Simonson H D.Browning and the fluorescence of evaporated milk.[J].Food Technology Champaign,1950,4(3):88-92.
[33]Jiang Z,Brodkorbb A.Structure and antioxidant activity of Maillard reaction products fromα-lactalbumin andβ-lactoglobulin with ribose in an aqueous model system[J].Food Chemistry,2012,133(3):960-968.
[34]程恒,陈尚武,景浩.3种乳蛋白与乳糖在不同湿度条件下美拉德反应进程的研究[J].食品科技,2013(6):58-66.
[35]Geng X,Cui B,Li Y,et al.Preparation and characterization of ovalbumin and carboxymethyl cellulose conjugates via glycosylation[J].Food Hydrocolloids,2014,37(37):86-92.
[36]Huang Y T,Liao H F,Wang S L,et al.Glycation and secondary conformational changes of human serum albumin:study of the FTIR spectroscopic curve-fitting technique[J].Aims Biophysics,2016,3(2):247-260.
[37]Sun Y,Hayakawa S,Izumori K.Modification of ovalbumin with a rare ketohexose through the Maillard reaction:effect on protein structure and gel properties[J].Journal of Agricultural and Food Chemistry,2004,52(5):1293-1299.
[38]Enomoto H,Li C P,Morizane K,et al.Glycation and phosphorylation of beta-lactoglobulin by dry-heating:Effect on protein structure and some properties[J].Journal of Agricultural and Food Chemistry,2007,55(6):2392.
[39]闫冰,房子舒,高彦祥,等.ε-聚赖氨酸与葡聚糖糖基化反应初级阶段产物的乳化性研究[J].食品工业科技,2012,33(9):53-57.
[40]陆钫.糖基化反应改进大米蛋白功能性质的研究[D].无锡:江南大学,2008.
[41]高守义,刘廷福.一元线性回归相关系数显著性检验[J].林业勘察设计,1981(1):36.
[2]高威.干法美拉德反应修饰酪蛋白凝胶性质的研究[D].大连:大连工业大学,2014.
[3]张雅婷.酪蛋白美拉德反应产物理化性质与包埋释放性能研究[D].无锡:江南大学,2013.
[4]赵海贤,于国萍.干法糖基化改性提高大豆分离蛋白的乳化性[J].食品研究与开发,2012,33(9):7-11.
[5]Saeki H.Preparation of Neoglycoprotein from Carp Myofibrillar Protein by Maillard Reaction with Glucose:Biochemical Properties and Emulsifying Properties[J].Journal of Agricultural and Food Chemistry,1997,45(3):680-684.
[6]Sato R,Katayama S,Sawabe T,et al.Stability and emulsionforming ability of water-soluble fish myofibrillar protein prepared by conjugation with alginate oligosaccharide.[J].Journal of Agricultural and Food Chemistry,2003,51(15):4376.
[7]Fujiwara K,Oosawa T,Saeki H.Improved thermal stability and emulsifying properties of carp myofibrillar proteins by conjugation with dextran.[J].Journal of Agricultural and Food Chemistry,1998,46(4):1257-1261.
[8]陈欣,周春霞,洪鹏志,等.糖基化改性对罗非鱼肉肌原纤维蛋白功能特性的影响[J].现代食品科技,2010,26(8):793-796.
[9]张爱荣,沈慧星,罗永康,等.鲢鱼肉肌原纤维乳糖蛋白的制备及其溶解性[J].中国农业大学学报,2005,10(3):95-98.
[10]尤娟,张佳,罗永康,等.鲢鱼肌原纤维蛋白-低聚异麦芽糖的制备及功能特性评价[J].肉类研究,2009(9):14-18.
[11]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[J].International Journal of Food Science and Technology,2011,46(12):2467-2474.
[12]Liu S,Zhao P,Zhang J,et al.Physicochemical and functional properties of silver carp(Hypophthalmichthys molitrix)myofibrillar protein glycated with konjac oligo-glucomannan[J].Food Hydrocolloids,2017,67:216-223.
[13]丛艳君,苘钰婷,易红.草鱼内脏蛋白酶解产物美拉德反应制备调味基料[J].食品科学,2014,35(22):6-10.
[14]郭晶晶.草鱼肉酶解液美拉德反应制备鱼味香精及其电子舌感官评定方法[D].镇江:江苏大学,2014.
[15]Cong Y J,Yu-Ting Q,Hong Y I.Preparation of flavoring base from enzymatic hydrolysate of visceral waste proteins of grass carp through maillard reaction[J].Food Science,2014.
[16]赵谋明,刘洋,张佳男,等.木糖-草鱼肽美拉德反应产物的抗氧化性[J].农业工程学报,2014,30(9):279-286.
[17]Li Z,Jiang M,You J,et al.Impact of Maillard reaction conditions on the antigenicity of parvalbumin,the major allergen in grass carp[J].Food and Agricultural Immunology,2014,25(4):486-497.
[18]Liu Q,Chen Q,Kong B,et al.The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp(Cyprinus carpio)surimi[J].LWT-Food Science and Technology,2014,57(2):603-611.
[19]Han K,Yao Y,Dong S,et al.Chemical characterization of the glycated myofibrillar proteins from grass carp(Ctenopharyngodon idella)and their impacts on the human gut microbiota in vitro fermentation.[J].Food and Function,2017,8(3).
[20]Amigobenavent M,Villamiel M,del Castillo M D.Chromatographic and electrophoretic approaches for the analysis of protein quality of soy beverages[J].Journal of Separation Science,2007,30(4):502-7.
[21]Jvande L,Manuel S J,Javier M F,et al.In vitro glycation and antigenicity of soy proteins[J].Food Research International,2007,40(1):153-160.
[22]Morale F J.Optimised Procedure to Analyse Maillard Reaction Associated Fluorescence in Cereal-Based Products[J].Czech Journal of Food Sciences,2008,26(5):339-346.
[23]李向红,王发祥,张付兰,等.冷藏过程中草鱼肌原纤维蛋白结构的变化[J].食品与发酵工业,2015,41(10):177-181.
[24]Pearce K N,Kinsella J E.Emulsifying properties of proteins:Evaluation of a turbidimetric technique[J].Journal of Agricultural and Food Chemistry,1978,26(3):716-723.
[25]Yamaguchi K,Nomi Y,Homma T,et al.Determination of furosine and fluorescence as markers of the Maillard reaction for the evaluation of meat products during actual cooking conditions[J].Food Science and Technology Research,2012,18(1):67-76.
[26]Pirestani S,Nasirpour A,Keramat J,et al.Preparation of chemically modified canola protein isolate with gum Arabic by means of Maillard reaction under wet-heating conditions[J].Carbohydrate Polymers,2017,155:201.
[27]Jing H,Kitts D D.Chemical and biochemical properties of casein-sugar Maillard reaction products[J].Food and Chemical Toxicology An International Journal Published for the British Industrial Biological Research Association,2002,40(7):1007.
[28]Boekel M A J S V.Kinetic aspects of the Maillard reaction:A critical review[J].Molecular Nutrition and Food Research,2001,45(3):150-9.
[29]Sun W W,Yu S J,Zeng X A,et al.Properties of whey protein isolate-dextran conjugate prepared using pulsed electric field[J].Food Research International,2011,44(4):1052-1058.
[30]Guo X,Xiong Y L.Characteristics and functional properties of buckwheat protein-sugar Schiff base complexes[J].LWT-Food Science and Technology,2013,51(2):397-404.
[31]Matiacevich S B,Buera M P.A critical evaluation of fluorescence as a potential marker for the Maillard reaction[J].Food Chemistry,2006,95(3):423-430.
[32]Tarassuk N P,Simonson H D.Browning and the fluorescence of evaporated milk.[J].Food Technology Champaign,1950,4(3):88-92.
[33]Jiang Z,Brodkorbb A.Structure and antioxidant activity of Maillard reaction products fromα-lactalbumin andβ-lactoglobulin with ribose in an aqueous model system[J].Food Chemistry,2012,133(3):960-968.
[34]程恒,陈尚武,景浩.3种乳蛋白与乳糖在不同湿度条件下美拉德反应进程的研究[J].食品科技,2013(6):58-66.
[35]Geng X,Cui B,Li Y,et al.Preparation and characterization of ovalbumin and carboxymethyl cellulose conjugates via glycosylation[J].Food Hydrocolloids,2014,37(37):86-92.
[36]Huang Y T,Liao H F,Wang S L,et al.Glycation and secondary conformational changes of human serum albumin:study of the FTIR spectroscopic curve-fitting technique[J].Aims Biophysics,2016,3(2):247-260.
[37]Sun Y,Hayakawa S,Izumori K.Modification of ovalbumin with a rare ketohexose through the Maillard reaction:effect on protein structure and gel properties[J].Journal of Agricultural and Food Chemistry,2004,52(5):1293-1299.
[38]Enomoto H,Li C P,Morizane K,et al.Glycation and phosphorylation of beta-lactoglobulin by dry-heating:Effect on protein structure and some properties[J].Journal of Agricultural and Food Chemistry,2007,55(6):2392.
[39]闫冰,房子舒,高彦祥,等.ε-聚赖氨酸与葡聚糖糖基化反应初级阶段产物的乳化性研究[J].食品工业科技,2012,33(9):53-57.
[40]陆钫.糖基化反应改进大米蛋白功能性质的研究[D].无锡:江南大学,2008.
[41]高守义,刘廷福.一元线性回归相关系数显著性检验[J].林业勘察设计,1981(1):36.