L-精氨酸对猪肉肌浆蛋白乳化特性的影响  

Effects of L-Arginine on Emulsifying Properties of Pork Sarcoplasmic Protein

作　　者：王昱 刘宁宁 王家乐 孟少华 陈博 李可 栗俊广 李胜杰 白艳红 WANG Yu;LIU Ningning;WANG Jiale;MENG Shaohua;CHEN Bo;LI Ke;LI Junguang;LI Shengjie;BAI Yanhong(Collaborative Innovation Center of Production and Safety,Henan Province,Key Laboratory of Cold Chain Food Processing and Safety Control,Ministry of Education,College of Food and Bioengineering,Zhengzhou University of Light Industry,Zhengzhou 450001,China;Henan Shuanghui Investment Development Co.Ltd.,Luohe 462000,China;School of Food Science and Technology,Dalian Polytechnic University,Dalian 116033,China)

机构地区：[1]郑州轻工业大学食品与生物工程学院,冷链食品加工与安全控制教育部重点实验室,食品生产与安全河南省协同创新中心,河南郑州450001 [2]河南双汇投资发展股份有限公司,河南漯河462000 [3]大连工业大学食品学院,辽宁大连116033

出　　处：《肉类研究》2025年第3期1-7,共7页Meat Research

基　　金：河南省高等学校重点科研项目(22B550022);郑州轻工业大学博士科研基金资助项目(2020BSJJ088);国家自然科学基金青年科学基金项目(32101989)。

摘　　要：以猪肉肌浆蛋白为对象,研究不同质量分数(0.0%、0.5%、1.0%、1.5%)L-精氨酸对其乳化特性的影响。研究发现,L-精氨酸(质量分数≥1%)显著提高肌浆蛋白的乳化活性和乳化稳定性(P<0.05),使肌浆蛋白乳液的粒径(D_(4,3)、D_(50)、D_(90))显著降低(P<0.05),Turbiscan稳定性指数呈下降趋势。界面流变的结果显示,L-精氨酸能够增加肌浆蛋白的油-水界面张力,而表面疏水性和紫外吸收光谱的结果表明,L-精氨酸促进了蛋白质疏水基团(色氨酸、酪氨酸残基)的暴露。拉曼光谱的结果表明,L-精氨酸有利于肌浆蛋白二级结构中的α-螺旋向β-转角转变。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳的结果显示,L-精氨酸不影响肌浆蛋白的基本组成。综上所述,L-精氨酸能通过改变乳液的理化性质、蛋白质界面性质及二、三级结构显著改善肌浆蛋白的乳化性能。The effects of different mass fractions of L-arginine(0.0%,0.5%,1.0%,and 1.5%)on the emulsifying characteristics of pork sarcoplasmic protein were studied.The findings indicated that addition of L-arginine(≥1%)significantly enhanced the emulsifying activity and emulsion stability of sarcoplasmic protein(P<0.05)and decreased the particle size(D_(4,3),D_(50)and D_(90))of sarcoplasmic protein-stabilized emulsion(P<0.05).The Turbiscan stability index(TSI)decreased after addition of L-arginine.The results of interfacial rheology showed that L-arginine increased the oil-water interfacial tension.The results of surface hydrophobicity and ultraviolet(UV)absorption spectroscopy implied that L-arginine promoted the exposure of protein hydrophobic groups(tryptophan and tyrosine residues).Raman spectroscopy showed that L-arginine was beneficial for the secondary structure transformation of sarcoplasmic protein fromα-helix toβ-turn.The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE)showed that the basic composition of sarcoplasmic protein was not affected by L-arginine.In summary,L-arginine could significantly improve the emulsifying properties of sarcoplasmic protein by changing emulsion physicochemical properties,protein interfacial characteristics,and protein secondary and tertiary structures.

关 键 词：猪肉 肌浆蛋白 乳化特性 L-精氨酸 结构修饰 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]