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ε-聚赖氨酸-乳清蛋白复合物的结构、稳定性、流变学和质地特性

Structure, stability, rheology, and texture properties of ε-polylysine-whey protein complexes.

作者信息

Meng Yuecheng, Xue Qi, Chen Jie, Li Yanhua, Shao Zhipeng

机构信息

College of Food Science and Biotechnology Engineering, Zhejiang Gongshang University, Hangzhou 310018, Zhejiang, China.

College of Food Science and Biotechnology Engineering, Zhejiang Gongshang University, Hangzhou 310018, Zhejiang, China.

出版信息

J Dairy Sci. 2022 May;105(5):3746-3757. doi: 10.3168/jds.2021-21219. Epub 2022 Mar 10.

DOI:10.3168/jds.2021-21219
PMID:35282919
Abstract

ε-Polylysine (ε-PL) is a natural preservative of antimicrobial peptides with broad spectrum and high antibacterial properties. The electrostatic complex delivery system formed by ε-PL and whey protein can be used to maintain the stability of ε-PL and solve the problem of limited application of protein-based food. This work aimed to study the interaction between ε-PL and whey protein by multiple characterization methods. The spectroscopy results showed static quenching type and new stretching of C=O for ε-PL-whey protein complexes. Microstructure studies showed that the combination of ε-PL and whey protein made the structure of the complexes become rough and dense. The interaction between ε-PL and whey protein could improve the stability of the complexes system during storage. Additionally, the interaction affected critical gel temperatures and gel texture properties of complexes with change of whey protein concentration, mass ratio of ε-PL to whey protein, pH value in alkaline solutions, and ion concentration. Overall, this study confirmed the interaction between ε-PL and whey protein, and it will provide a reference for the application of ε-PL in protein food matrix.

摘要

ε-聚赖氨酸(ε-PL)是一种具有广谱抗菌特性的天然抗菌肽防腐剂。由ε-PL和乳清蛋白形成的静电复合递送系统可用于维持ε-PL的稳定性,并解决基于蛋白质的食品应用受限的问题。这项工作旨在通过多种表征方法研究ε-PL与乳清蛋白之间的相互作用。光谱学结果表明,ε-PL-乳清蛋白复合物存在静态猝灭类型和C=O的新伸缩振动。微观结构研究表明,ε-PL与乳清蛋白的结合使复合物的结构变得粗糙且致密。ε-PL与乳清蛋白之间的相互作用可提高复合物体系在储存期间的稳定性。此外,随着乳清蛋白浓度、ε-PL与乳清蛋白的质量比、碱性溶液中的pH值以及离子浓度的变化,这种相互作用会影响复合物的临界凝胶温度和凝胶质地特性。总体而言,本研究证实了ε-PL与乳清蛋白之间的相互作用,这将为ε-PL在蛋白质食品基质中的应用提供参考。

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