β-甘露糖苷酶酶解对HOVM结构与胰蛋白酶抑制活性的影响  

Effects of Enzymolysis by β-mannosidase on the Structure and Trypsin-inhibitory Activity of Hen-egg Ovomucoid

作　　者：侯惠静 吴子健[2] 石振鹏 姜宇峰 HOU Hui-jing;WU Zi-jian;SHI Zhen-peng;JIANG Yu-feng(School of Bioengineering and Food Engineering,Tianjin Tianshi College,Tianjin 301700,China;School of Biotechnology and Food Science,Tianjin University of Commerce,Tianjin Key Laboratory of Food and Biotechnology,Tianjin 300134,China)

机构地区：[1]天津天狮学院生物与食品工程学院,天津301700 [2]天津商业大学生物技术与食品科学学院天津市食品生物技术重点实验室,天津300134

出　　处：《食品研究与开发》2019年第4期32-37,共6页Food Research and Development

基　　金：天津市应用基础与前沿技术研究计划面上项目(14JCYBJC30900);天津市应用基础与前沿技术研究计划青年项目(15JCQNJC12200);天津市高等学校创新团队"农产品加工贮藏新新技术及相关机理研究"(TD13-5087)

摘　　要：通过苯酚-硫酸法、8-苯氨基-1-萘磺酸(8-Anilino-1-naphthalenesulfonic acid,ANS)荧光探针法以及圆二色谱法检测分析β-甘露糖苷酶酶解处理鸡卵类黏蛋白(hen-egg ovomucoid,HOVM)上的糖基部分后,HOVM中糖基含量变化与蛋白的表面疏水性、二级结构组成以及HOVM对胰蛋白酶抑制活力之间的关系。研究结果表明:β-甘露糖苷酶酶处理降低了HOVM中糖基部分的含量,会逐步提高HOVM对胰蛋白酶的抑制活力,同时对于二级结构组成的影响不是很显著,但是随着糖基含量的降低,HOVM中无规则卷曲的含量降低与胰蛋白酶的抑制率逐渐增高具有显著的相关性。Hen-egg ovomucoid(HOVM)was enzymolysated byβ-mannosidase,and then phenol-sulfuric acid method,8-Anilino-1-naphthalenesulfonic acid(ANS)-fluorescence-probe method and circular dichroism chromatography were used to evaluate the relationship between the variation of sugar group content and surface hydrophobicity,secondary structure component and the inhibitory activity of HOVM on trypsin.Results showed that enzymolysis byβ-mannosidase could decrease the content of sugar group in HOVM,and also gradually increased the inhibitory activity of HOVM on trypsin;at the same time,effects on the secondary structure was not significant.However,with the decreasing of sugar group content,the content of random coil in HOVM decreased and the inhibition rate on trypsin decreased too;and there was a significant correlation between their variation.

关 键 词：鸡卵类黏蛋白 胰蛋白酶抑制活性 β-甘露糖苷酶 无规则卷曲 

分 类 号：TS253.1[轻工技术与工程—农产品加工及贮藏工程]