高斯软件模拟转谷氨酰胺酶交联大豆分离蛋白机理的研究  

Study on Mechanism of Transglutaminase Cross-linking Soybean Protein Isolate Simulated by Gauss Software

作　　者：臧学丽[1] 黄志远[1] 叶春民 ZANG Xue-li;HUANG Zhi-yuan;YE Chun-min(Changchun Medical College,Changchun 130031,China)

机构地区：[1]长春医学高等专科学校药品食品学院,长春130031

出　　处：《高分子通报》2022年第10期108-119,共12页Polymer Bulletin

基　　金：吉林省教育厅项目(JJKH20221350KJ)。

摘　　要：为了进一步验证转谷氨酰胺酶(TGase)交联大豆分离蛋白(SPI)作用机制,本研究通过计算化学方法模拟催化过程,利用在多相催化和生物催化领域来预算物质结构中经常使用的高斯软件(Gaussian)对TGase交联SPI作用机制进行模拟,经计算确定了转谷氨酰胺酶活性中心5个氨基酸连接的最佳结构。对酶催化SPI赖氨酸和谷氨酰胺脱氨反应过程进行了模拟。通过计算发现,在8种可能脱氨的方式中,只有2种方式的反应能顺利进行,每种方式各占一定比例,即谷氨酰胺脱γ位酰胺的氨基与赖氨酸ε位氨基氢、谷氨酰胺脱α位氨基与赖氨酸ε位氨基氢发生脱氨反应,反应过程的能垒分别为49.50和44.35kcal/mol。SPI发生随机交联可生成高分子聚合物,改变SPI的功能特性,提高大豆分离蛋白的凝胶强度。The purpose of this study is to further verify the mechanism of transglutaminase(TGase)cross-linking soybean protein isolate(SPI).The mechanism of SPI cross-linked with transglutaminase is simulated by Gaussian software,which is usually used in the field of the heterogeneous catalysis and biocatalysts.And the catalytic process is simulated by the chemical method.The results show that the center of transglutaminase activity comnected with 5amino acids is the optimal structure by calculation.The enzymatic catalysis of the lysine and glutamine dehydrogenation reactions is simulated.The calculating results indicate that there are 8possible deamination reactions.However,only 2reactions can be carried out smoothly.Each method has a certain proportion,that is,glutamine amideγ-amide and lysineε-amino hydrogen.Deamination reaction occurred between amino group and lysine toxic amino hydrogen,and the energy barriers of the reaction process were 49.50and 44.35kcal/mol,respectively.SPI can be cross-linked randomly to produce high molecular weight polymers.As a result,the functional characteristics of SPI is changed,and the gel strength of isolated soybean protein is improved.

关 键 词：高斯软件 转谷氨酰胺酶 交联 大豆分离蛋白 机理 

分 类 号：TS214.2[轻工技术与工程—粮食、油脂及植物蛋白工程]