- Characterization of Recombinant β-Glucosidase from Arthrobacter chlorophenolicus and Biotransformation of Ginsenosides Rb1, Rb2, Rc, and Rd
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Myung Keun Park , Chang-Hao Cui , Sung Chul Park , Seul-Ki Park , Jin-Kwang Kim , Mi-Sun Jung , Suk-Chae Jung , Mi-Sun Jung , Suk-Chae Jung , Sun-Chang Kim , Wan-Taek Im
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J. Microbiol. 2014;52(5):399-406. Published online May 9, 2014
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DOI: https://doi.org/10.1007/s12275-014-3601-7
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The focus of this study was the cloning, expression, and characterization of recombinant ginsenoside hydrolyzing β-glucosidase from Arthrobacter chlorophenolicus with an ultimate objective to more efficiently bio-transform ginse-nosides. The gene bglAch, consisting of 1,260 bp (419 amino acid residues) was cloned and the recombinant enzyme, over-expressed in Escherichia coli BL21 (DE3), was characterized. The GST-fused BglAch was purified using GST·Bind agarose resin and characterized. Under optimal conditions (pH 6.0 and 37°C) BglAch hydrolyzed the outer glucose and arabino-pyranose moieties of ginsenosides Rb1 and Rb2 at the C20 position of the aglycone into ginsenoside Rd. This was fol-lowed by hydrolysis into F2 of the outer glucose moiety of ginsenoside Rd at the C3 position of the aglycone. Additio-nally, BglAch more slowly transformed Rc to F2 via C-Mc1 (compared to hydrolysis of Rb1 or Rb2). These results in-dicate that the recombinant BglAch could be useful for the production of ginsenoside F2 for use in the pharmaceutical and cosmetic industries.
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Citations
Citations to this article as recorded by  - A novel GH66 family glycoside hydrolase pseudo-dextranase from Streptococcus thermophilus 17140 in catalyzing multi-step deglycosylation of ginsenoside Rb1
Xinyi Liu, Yue Li, Jinxia Liu, Wenying Cao, Ximin Fu, Dong Wang
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Wenqi Yang, Yaowu Su, Rubing Wang, Huanyu Zhang, Hongyan Jing, Jie Meng, Guoqi Zhang, Luqi Huang, Lanping Guo, Juan Wang, Wenyuan Gao
International Journal of Biological Macromolecules.2024; 256: 127915. CrossRef - Progress in the Conversion of Ginsenoside Rb1 into Minor Ginsenosides Using β-Glucosidases
Hongrong Zhu, Rui Zhang, Zunxi Huang, Junpei Zhou
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- Mucilaginibacter composti sp. nov., with Ginsenoside Converting Activity, Isolated from Compost
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Chang-Hao Cui , Tae-Eun Choi , Hongshan Yu , Fengxie Jin , Sung-Taik Lee , Sun-Chang Kim , Wan-Taek Im
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J. Microbiol. 2011;49(3):393-398. Published online June 30, 2011
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DOI: https://doi.org/10.1007/s12275-011-1176-0
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The Gram-negative, strictly aerobic, non-motile, non-spore-forming, rod shaped bacterial strain designated TR6-03T was isolated from compost, and its taxonomic position was investigated by using a polyphasic approach. Strain TR6-03T grew at 4-42°C and at pH 6.0-8.0 on R2A and nutrient agar without NaCl supplement. Strain TR6-03T had β-glucosidase activity, which was responsible for its ability to transform ginsenoside Re (one of the dominant active components of ginseng) to Rg2. On the basis of 16S rRNA gene sequence similarity, strain TR6-03T was shown to belong to the family Sphingobacteriaceae and to be related to Mucilaginibacter lappiensis ANJLI2T (96.3% sequence similarity), M. dorajii FR-f4T (96.1%), and M. rigui WPCB133T (94.1%). The G+C content of the genomic DNA was 45.6%. The predominant respiratory quinone was MK-7 and the major fatty acids were summed feature 3 (comprising C16:1 ω7c and/or iso-C15:0 2OH), iso-C15:0 and iso-C17:0 3OH. DNA and chemotaxonomic data supported the affiliation of strain TR6-03T to the genus Mucilaginibacter. Strain TR6-03T could be differentiated genotypically and phenotypically from the recognized species of the genus Mucilaginibacter. The isolate therefore represents a novel species, for which the name Mucilaginibacter composti sp. nov. is proposed, with the type strain TR6-03T (=KACC 14956T =KCTC 12642T =LMG 23497T).
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Citations
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