罗伊氏乳杆菌DSM20016醛酮还原酶的酶学表征
Characterisation of aldo-keto reductases from Lactobacillus reuteri DSM20016
Wenhao Qu, Yajun Bai, Tai-Ping Fan, Xiaohui Zheng, Yujie Cai
Journal:PROCESS BIOCHEMISTRY
IF:4.89
DOI:10.1016/j.procbio.2022.10.001
PMID:
Published:2022-10-04
research field:神经科学分子生物学药理学植物化学遗传学与基因组学生物化学
Abstract
Lactobacillus reuteri DSM20016 has several aldo-keto reductases (AKRs), and they were heterologously expressed in E. coli BL21 (DE3) in this study. Subsequently, these AKRs were purified, and their enzymatic properties were investigated. It was found that these enzymes used NADPH as coenzyme and did not depend on metal ions. The optimum pH of these AKRs was a slightly acidic (AKR-1 and AKR-6: 5.5; AKR-3 and AKR-8: 6; AKR-2 and AKR-4: 6.5). These enzymes had a broad substrate spectrum and could convert a variety of aldehydes to alcohols; however, they did not catalyze the reverse reactions. All results showed that Lactobacillus reuteri had the ability to produce various volatile compounds, which allowed Lactobacillus reuteri to impart complex aroma to something.
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