等离子体预处理对花生粕蛋白酶解特性的影响

Effect of Plasma Pretreatment on Protease Hydrolysis of Peanut Meal

本研究以花生粕为实验原料,通过高效液相色谱仪、扫描电子显微镜等手段,研究不同等离子体预处理对花生粕蛋白的分子量大小、氨基酸组成以及微观结构的影响规律。与对照相比,经过等离子体预处理的花生粕蛋白的水解度提高了10.69%;高效液相色谱仪和氨基酸分析仪结果表明,经过等离子体预处理后的花生粕蛋白的分子量主要集中在200~1000 u,其中Glu、Arg、Asp、Leu和Phe 5种氨基酸在花生粕蛋白的水解过程中起到了重要作用;通过对处理120 s的花生粕蛋白进行酶解动力学参数测定,与对照相比,等离子体预处理组的KA保持基本不变,而K_(M)下降了14.67%;在1000倍的扫描电镜下发现处理后的花生粕蛋白结构受到破坏。本文系统揭示了等离子体调控过程中底物蛋白关键结构域变化与其酶解特性之间的内在关联机制,为制备高效酶解和结构紧凑的花生粕蛋白提供了理论基础。

In this study,peanut meal was used as experimental raw material.By means of high performance liquid chromatography(HPLC)and scanning electron microscopy(SEM),the influences of different plasma pretreatment on the molecular weight,amino acid composition and micro structure of peanut meal protein were studied.Compared with the control,the degree of hydrolysis of peanut meal protease hydrolysate after plasma pretreatment was increased by 10.69%.The results of high performance liquid chromatography and amino acid analyzer showed that the molecular weight of the peanut meal protease hydrolysates after plasma pretreatment was about 200~1000 u,among which five kinds of amino acids Glu,Arg,Asp,Leu and Phe played an important role in the hydrolysis process of peanut meal protease hydrolysates.Compared with the control group,the KAof the peanut meal protein treated for 120 s remained basically unchanged,while the K_(M)decreased by 14.67%.Under 1000-fold scanning electron microscope,the structure of the treated peanut meal protease hydrolysate was damaged.This paper systematically revealed the internal mechanism of the correlation between the changes of key domains of substrate proteins and their enzymolysis properties during the plasma regulation process,which provided a theoretical basis for the preparation of peanut meal proteins with high enzymolysis efficiency and compact structure.