Fei-Liang Zhong1, Wei-Wei Dong1, Songquan Wu1, Jun Jiang1, Deok-Chun Yang2, Donghao Li3, Lin-Hu Quan4. 1. Key Laboratory of Natural Resources of Changbai Mountain and Functional Molecules, Ministry of Education, Yanbian University, Park Road 977, Yanji, 133002, Jilin, People's Republic of China. 2. Department of Oriental Medicinal Material and Processing, College of Life Science, Korean Ginseng Center Most Valuable Product and Ginseng Genetic Resource Bank, Kyung-Hee University, Seocheon-dong, Giheung-gu, Yongin-Si, Gyeonggi-do, 446-701, Republic of Korea. dcyang@khu.ac.kr. 3. Key Laboratory of Natural Resources of Changbai Mountain and Functional Molecules, Ministry of Education, Yanbian University, Park Road 977, Yanji, 133002, Jilin, People's Republic of China. dhli@ybu.edu.cn. 4. Key Laboratory of Natural Resources of Changbai Mountain and Functional Molecules, Ministry of Education, Yanbian University, Park Road 977, Yanji, 133002, Jilin, People's Republic of China. lhquan@ybu.edu.cn.
Abstract
OBJECTIVE: To study the β-glucosidase gene (bgy1) from Lactobacillus brevis that was cloned and expressed in Escherichia coli BL21 (DE3) and then using it for the biotransformation of gypenoside XVII. RESULTS: The bgy1 gene consists of 2283 bp encoding 761 amino acids, with homology to the glycosyl hydrolase family-3 protein domain. The enzyme (Bgy1) hydrolyzed the glucose moieties at the C-3 position and the outer glucose moieties at the C-20 position of gypenoside XVII. Using 0.1 mg enzyme ml(-1) in 20 mM sodium phosphate buffer at 30 °C and pH 6.0, 1 mg gypenoside XVII ml(-1) was transformed into 0.58 mg compound K ml(-1) within 6 h, with a corresponding molar conversion yield of 89 %. CONCLUSION: The recombinant Bgy1 is considered potentially useful for the practical preparation of compound K.
OBJECTIVE: To study the β-glucosidase gene (bgy1) from Lactobacillus brevis that was cloned and expressed in Escherichia coli BL21 (DE3) and then using it for the biotransformation of gypenoside XVII. RESULTS: The bgy1 gene consists of 2283 bp encoding 761 amino acids, with homology to the glycosyl hydrolase family-3 protein domain. The enzyme (Bgy1) hydrolyzed the glucose moieties at the C-3 position and the outer glucose moieties at the C-20 position of gypenoside XVII. Using 0.1 mg enzyme ml(-1) in 20 mM sodium phosphate buffer at 30 °C and pH 6.0, 1 mg gypenoside XVII ml(-1) was transformed into 0.58 mg compound K ml(-1) within 6 h, with a corresponding molar conversion yield of 89 %. CONCLUSION: The recombinant Bgy1 is considered potentially useful for the practical preparation of compound K.
Authors: Gang Wang; Fei Yan; Yufei Wang; Yingping Liu; Jingnan Cui; Zhenlong Yu; Lei Feng; Tony D James; Chao Wang; Ying Kong Journal: Front Chem Date: 2022-05-27 Impact factor: 5.545