机构地区: 广东省水产品加工与安全重点实验室广东湛江524088
出 处: 《食品与机械》 2013年第4期4-7,34,共5页
摘 要: 探讨两种从中国毛虾蛋白酶解产物中分离鉴定的血管紧张素转化酶(ACE)抑制肽Leu-His-Pro和Val-Trp对ACE的抑制类型及其机制,为其进一步的开发利用提供基础数据。根据Leu-His-Pro和Val-Trp对ACE催化合成底物Hippuryl-Histidyl-Leucine(HHL)生成马尿酸的抑制动力学和Linweaver-Burk曲线判断其抑制类型。结果表明,Leu-His-Pro和Val-Trp对ACE的抑制动力学曲线均通过原点,属可逆性抑制;Leu-His-Pro的Linweaver-Burk曲线符合竞争性抑制剂特征,抑制常数Ki=0.078 9g/mL;Val-Trp的Linweaver-Burk曲线符合非竞争性抑制剂特征,Ki=0.147mg/mL。 Investigated the inhibition type and mechanism of two angiontensin I-converting enzyme(ACE) inhibitory inhibitory peptides,Leu-His-Pro and Val-Trp,which was isolated and characterized from the enzymatic hydrolysate of Acetes chinensis.The purpose is to gain the basic data for further developing and utilizing the two active peptides.The inhibition kinetics were studied of Leu-His-Pro and Val-Trp on the catalysis of ACE on Hippuryl-Histidyl-Leucine(HHL) to hippuric acid,and the Linweaver-Burk plots were drew to judge their inhibition type on ACE.The kinetic curves of Leu-His-Pro and Val-Trp cut the origin of the coordinate plane,they were reversible inhibition.The Linweaver-Burk plot of Leu-His-Pro was suited to competitive inhibition character,the inhibition constant Ki was 0.078 9 g/mL.The Linweaver-Burk plot of Val-Trp was suited to noncompetitive inhibition character,the inhibition constant Ki was 0.147 g/mL.