The effect of structural changes on the activity of peroxidase with different initial state under high-pressure freezing
文献类型： 外文期刊
作者： Liang, Zhanhong 1 ; Yu, Yuanshan 1 ; Zou, Bo 1 ; Fu, Manqin 1 ; Hu, Tenggen 1 ; Yin, Xiaomeng 3 ; Wang, Jin 3 ; Xu, Yujuan 1 ; Cheng, Lina 1 ;
作者机构： 1.Guangdong Acad Agr Sci, Sericultural & Argi Food Res Inst, Guangdong Key Lab Agr Prod Proc, Key Lab Funct Foods,Minist Agr & Rural Affairs, 133 Yiheng St,Dongguanzhuang Rd, Guangzhou 510610, Peoples R China
2.Guangdong Pharmaceut Univ, Sch Food Sci, Zhongshan 528400, Peoples R China
3.Guangzhou Conghua Dist Agr & Rural Bur, Guangzhou 510610, Peoples R China
关键词： High-pressure freezing; Peroxidase; Physical state; Structure; Activity; Molecular docking
期刊名称：FOOD CHEMISTRY （ 影响因子：8.5； 五年影响因子：8.2 ）
ISSN： 0308-8146
年卷期： 2024 年 459 卷
页码：
收录情况： SCI
摘要： The combined impact of initial state, pressure, and freezing on peroxidase denaturation during high-pressure freezing (HPF) processing of enzyme-containing foods remains unclear. This study investigated solid-liquid (initial low/high concentration) biphasic peroxidase using spectroscopic and computer simulation techniques to analyze structural changes affecting peroxidase (POD) activity under HPF. The results indicate that the primary factors determining POD activity during HPF treatment can be ranked as follows: concentration > physical state > pressure > freezing. Higher initial concentrations strengthen protein interactions, leading to a 1% increase in the molecular diameter and a 34% increase in molecular height of HL-POD, thereby increasing aggregation likelihood during crystallization and facilitating structural changes that activate enzymes by 6-17%. The amide I peak proves to be a reliable indicator for monitoring both POD activity and structural alterations. This study offers valuable insights for optimizing HPF technology in food processing.
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