Physicochemical properties and action mechanism of chicken lung protein hydrolysate modified by plastein reaction

IF 4.8 1区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

Food Bioscience Pub Date : 2025-03-26 DOI:10.1016/j.fbio.2025.106456

Siyu Cheng , Jiahua Gao , Lixin Yu , Yiyao Chen , Zeyuan Zhao , Xin Zhou , Peng Wang , Yun Bai , Xianming Zeng , Xinglian Xu , Minyi Han

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Abstract

Plastein reaction is the process of colloid formed from concentrated hydrolysate by protease under suitable conditions, but the underlying mechanism has not been clarified. This study examined the functional and mechanistic changes in chicken lung protein hydrolysate (CLPH) caused by the plastein reaction. The results revealed that the plastein reaction products stretched, the hydrophobic groups were exposed, and the reaggregation occurred. In terms of function, solubility declined after modification, but foaming properties and emulsification properties increased. Moreover, the elevated Fe²⁺ chelation (from 18.20 % to 48.32 %), DPPH (30.04 %–71.74 %), ABTS (41.66 %–62.44 %) and hydroxyl radical (34.85 %–63.22 %) scavenging power suggested that the plastein strengthened the CLPH in a broader sense. Meanwhile, hydrogen bonds and hydrophobic interactions were crucial in creating the structure of the plastein modification products. In summary, the plastein reaction is a viable method for influencing structural changes to enhance protein function.

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来源期刊

Food Bioscience Biochemistry, Genetics and Molecular Biology-Biochemistry

CiteScore

6.40

自引率

5.80%

发文量

671

审稿时长

27 days

期刊介绍： Food Bioscience is a peer-reviewed journal that aims to provide a forum for recent developments in the field of bio-related food research. The journal focuses on both fundamental and applied research worldwide, with special attention to ethnic and cultural aspects of food bioresearch.