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A study on the catalytic domain of pork phospholipase A2: Enzymatic properties and hydrolysis characteristics of phosphatidylcholine and its hydroperoxide

文献类型： 外文期刊

作者： Liu, Yu 1 ; Ma, Jingjing 1 ; Xu, Jiamei 1 ; Li, Pengpeng 1 ; Wang, Daoying 1 ; Zhang, Muhan 1 ; Geng, Zhiming 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Agriprod Proc, Nanjing 210014, Peoples R China

2.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China

关键词： Phospholipase A 2; Hydrolysis characteristic; Phospholipids; Peroxidized phosphatidylcholine; Pork

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：7.7； 五年影响因子：7.7 ）

ISSN： 0141-8130

年卷期： 2024 年 270 卷

页码：

收录情况： SCI

摘要： Endogenous phospholipase A2 (PLA2) plays an important role in phospholipids degradation during cured meat products manufacturing. The present study was undertaken to reveal more information about the endogenous PLA2 in muscles and its role in degradation of intramuscular phospholipids. With the catalytic domain of pork calcium-independent PLA2 (iPLA2cd), impacts of physic-chemical factors on the activity were investigated and substrate specificity of the enzyme were tested respectively. The optimum temperature and pH of pork iPLA2cd were 40 degrees C and 7.5, respectively. The iPLA2cd could be stimulated by adequate contents of NaCl and ATP, and inhibited by CaCl2 and NaNO2. For native phospholipids, the iPLA2cd was of a little higher affinity towards phosphatidylcholine (PC) than phosphatidylethanolamine (PE), phosphoserine (PS) and phosphatidylinositol (PI). The iPLA2cd could preferentially hydrolyze peroxidized PC over the native PC. The results would help better understand the degradation of phospholipids and the role played by endogenous enzymes during meat products manufacturing.

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