非天然磷酰化氨基酸对胰蛋白酶的荧光猝灭效应  

Study on the Fluorescence Quenching Effect between Non-Natural Phosphoryl Amino Acids and Trypsin

作　　者：符芳妮 张晖[1] 邓少平[1] 陈丽春[1,2] 

机构地区：[1]浙江工商大学食品与生物工程学院,浙江杭州310012 [2]浙江科技学院生物与化学工程学院,浙江杭州310023

出　　处：《食品与生物技术学报》2014年第2期197-203,共7页Journal of Food Science and Biotechnology

基　　金：浙江省科技计划项目(2012C22026)

摘　　要：作者利用荧光法研究了非天然L-型氨基酸磷酰化前后与胰蛋白酶的相互作用。实验结果表明,L-2-氨基戊酸、庚酸、辛酸及壬酸非天然氨基酸不能使胰蛋白酶的荧光强度减弱,非天然氨基酸磷酰化后能够对胰蛋白酶产生荧光猝灭。同时,浓度不同、侧链长度不同的同系列磷酰化氨基酸对胰蛋白酶的猝灭效应均不同。随着非天然脂肪酸链磷酰化氨基酸侧链的增长及磷酰化庚酸浓度的增大,胰蛋白酶的荧光强度均明显降低,并且其荧光可以被完全猝灭。非天然氨基酸的磷酰化能够影响非天然氨基酸与胰蛋白酶的相互作用。Trypsin has the fluorescence.Fluorescence method was used to study the interactions between N-phosphoryl non-natural amino acids and trypsin solution in detail.The results indicated that L-2-amino valeric acid,heptanoic acid,octanoic acid and nonanoc acid can＇t decrease the fluorescence intensity of trypsin solution,but N-phosphoryl amino valeric acid,heptanoic acid,octanoic acid and nonanoc acid can quench the fluorescence of trypsin solution.At the same time,N-phosphoryl amino acid of different concentration,different length have different quenching effects on trypsin.With the increasing of carbon chain length of N-phosphoryl amino acid and the increasing of N-phosphoryl heptanoic acid＇s concentration,the intensity of trypsin decreased fast.What＇s more,the fluorescence of trypsin could be quenched completely by N-phosphoryl amino heptanoic acid.It showed that N-phosphoryl amino acids could change the interactions with trypsin.

关 键 词：非天然氨基酸 磷酰化 胰蛋白酶 荧光光谱 

分 类 号：TS201.25[轻工技术与工程—食品科学]