研究报告

L-精氨酸/L-赖氨酸对乳清蛋白凝胶质构和持水性的影响

  • 王耀松 ,
  • 马天怡 ,
  • 张唯唯 ,
  • 黄梅桂 ,
  • 应瑞峰 ,
  • 胡荣蓉 ,
  • 唐长波
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  • 1(南京林业大学 轻工与食品学院,江苏 南京,210037)
    2(肉品加工与质量控制教育部重点实验室,南京农业大学 食品科学技术学院,江苏 南京,210095)
博士,副教授(唐长波副教授为通讯作者,E-mail:tangcb@njau.edu.cn)

收稿日期: 2020-05-12

  修回日期: 2020-06-04

  网络出版日期: 2020-10-14

基金资助

国家自然科学基金青年基金项目(31401530;31501509);江苏省优势学科建设项目青年创新基金项目(80900604)

L-Arginine/L-lysine improved textural properties and water holding capacity of whey protein gels formed at various pH values

  • WANG Yaosong ,
  • MA Tianyi ,
  • ZHANG Weiwei ,
  • HUANG Meigui ,
  • YING Ruifeng ,
  • HU Rongrong ,
  • TANG Changbo
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  • 1(College of Light Industry and Food Engineering, Nanjing Forestry University, Nanjing 210037, China)
    2(Key Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China)

Received date: 2020-05-12

  Revised date: 2020-06-04

  Online published: 2020-10-14

摘要

为考察L-精氨酸/L-赖氨酸及pH对乳清蛋白结构和凝胶性质的影响,研究2种碱性氨基酸对乳清蛋白热诱导凝胶质构及持水性的影响。研究表明,L-精氨酸/L-赖氨酸对蛋白聚集体大小及ζ-电位(pH 2.0下L-精氨酸处理除外)有降低的趋势;紫外、荧光光谱显示在酸性条件下,碱性氨基酸促进蛋白分子结构展开,而在碱性条件下则使蛋白结构倾向折叠。不同pH(2.0、5.2、7.59、9.74和10.76)的蛋白溶液,每个pH的样品分别含有质量浓度1、3 g/L L-精氨酸或L-赖氨酸,90 ℃加热30 min后能够形成颜色随pH变化而变化的凝胶。化学作用力分析则显示2种氨基酸通过改变蛋白分子间作用而显著改变质构特性和持水性。总之,在pH对蛋白结构和凝胶功能性影响的基础上,L-精氨酸/L-赖氨酸能够进一步提高凝胶质构特性与持水性。

本文引用格式

王耀松 , 马天怡 , 张唯唯 , 黄梅桂 , 应瑞峰 , 胡荣蓉 , 唐长波 . L-精氨酸/L-赖氨酸对乳清蛋白凝胶质构和持水性的影响[J]. 食品与发酵工业, 2020 , 46(17) : 46 -53 . DOI: 10.13995/j.cnki.11-1802/ts.024430

Abstract

To explore the effects of L-arginine (L-Arg)/L-lysine (L-Lys) and pH on enhancing the structure and gelling properties of the whey protein, their influences on the textural characteristics and water holding capacity of the heat-induced gels were tested. The results showed that the addition of the two amino acids were capable of decreasing the protein aggregate size and ζ-potential (except L-Arg treatment at pH 2.0). UV and fluorescence spectra indicated that L-Arg/L-Lys promoted the unfolding of protein molecular structures at acidic conditions, while opposite effect was observed at alkaline conditions. Protein solutions with different pH (2.0, 5.2, 7.59, 9.74 and 10.76), each contained 1 and 3 g/L L-Arg or L-Lys, respectively, could form gels after heating at 90 °C for 30 min. The colors of these gels varied with pH. The analysis of the chemical force illustrated that L-Arg/L-Lys significantly modified the textural characteristics and water holding capacity via varying the interaction between protein molecules. In brief, on the basis of the pH effect, L-Arg/L-Lys could further enhancing the textural structure and functional properties of the resulting protein gels.

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