摘要
氨基酸脱羧酶(AAD)是生物胺合成的关键酶。微生物AAD一般为胞内酶,但性质稳定,在脱离细胞体系中仍可保持催化活性。文章以具有产生物胺能力的3种微生物细胞超声破碎后的粗酶液为对象,探究了前体氨基酸浓度、pH和盐浓度对离体AAD催化活性的影响。结果显示,多数情况下前体氨基酸未充分转化为生物胺,但低浓度前体氨基酸显著降低了离体AAD的催化活性;Lactobacillusplantarum 1-8和Escherichia coli BA-1的AAD在pH为6时催化活性最强,Debaryomyces hansenii MB-1Y的AAD在pH为5时催化活性最强;盐浓度提升导致AAD的催化活性降低。该研究可为探讨食品发酵中AAD的催化特性及其控制提供参考。
Amino acid decarboxylase(AAD)is a key enzyme in biogenic amine synthesis.Microbial AAD is generally an intracellular enzyme,but its properties are stable and it can still maintain catalytic activity in extracellular systems.In this paper,with crude enzyme solution obtained from three microbial cells with the ability to produce biogenic amines after ultrasonic disruption as the object,the effects of precursor amino acid concentration,pH and salt concentration on the catalytic activity of in vitro AAD are investigated.The results show that in most cases,the precursor amino acids are not fully converted into biogenic amines,but low concentrations of precursor amino acids significantly reduce the catalytic activity of in vitro AAD.The catalytic activity of AAD of Lactobacillus plantarum 1-8 and Escherichia coli BA-1 is the strongest when pH is 6,while the catalytic activity of AAD of Debaryomyces hansenii MB-1Y is the strongest when pH is 5.The increase of salt concentration leads to the decrease of the catalytic activity of AAD.This study can provide references for exploring the catalytic characteristics and controlling of AAD in food fermentation.
作者
李书婷
林泽
尹礼国
张文学
吴正云
LI Shu-ting;LIN Ze;YIN Li-guo;ZHANG Wen-xue;WU Zheng-yun(Key Laboratory of Solid-state Fermentation Resource Utilization in Sichuan Province,Yibin University,Yibin 644005,China;College of Biomass Science and Engineering,Sichuan University,Chengdu 610065,China)
出处
《中国调味品》
CAS
北大核心
2024年第10期65-69,100,共6页
China Condiment
基金
固态发酵资源利用四川省重点实验室开放基金项目(2022GTYY09)。
关键词
生物胺
氨基酸脱羧酶
离体酶
催化活性
环境因素
biogenic amine
amino acid decarboxylase
in vitro enzyme
catalytic activity
environmental factors
