Enzymatic transformation of vina-ginsenoside R7 to rare notoginsenoside ST-4 using a new recombinant glycoside hydrolase from Herpetosiphon aurantiacus

Verfasser / Beitragende:
[Ru-Feng Wang, Ming-Min Zheng, Yue-De Cao, Hao Li, Chun-Xiu Li, Jian-He Xu, Zheng-Tao Wang]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/8(2015-04-01), 3433-3442
Format:
Artikel (online)
ID: 605504172
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024 7 0 |a 10.1007/s00253-015-6446-z  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-015-6446-z 
245 0 0 |a Enzymatic transformation of vina-ginsenoside R7 to rare notoginsenoside ST-4 using a new recombinant glycoside hydrolase from Herpetosiphon aurantiacus  |h [Elektronische Daten]  |c [Ru-Feng Wang, Ming-Min Zheng, Yue-De Cao, Hao Li, Chun-Xiu Li, Jian-He Xu, Zheng-Tao Wang] 
520 3 |a An eco-friendly and convenient preparation method for notoginsenoside ST-4 has been established by completely transforming vina-ginsenoside R7 using a recombinant glycosidase hydrolyzing enzyme (HaGH03) from Herpetosiphon aurantiacus. This enzyme specifically hydrolyzed the glucose at the C-20 position but not the external xylose or two inner glucoses at position C-3. Protein sequence BLAST revealed that HaGH03, composed of 749 amino acids and presumptively listed as a member of the family 3 glycoside hydrolases, has highest identity (48%) identity with a thermostable β-glucosidase B, which was not known of any functions for ginsenoside transformation. The steady state kinetic parameters for purified HaGH03 measured against p-nitrophenyl β-D-glucopyranoside and vina-ginsenoside R7 were K M = 5.67 ± 0.24μM and 0.59 ± 0.23mM, and k cat = 69.2 ± 0.31/s and 2.15 ± 0.46/min, respectively. HaGH03 converted 2.5mg/mL of vina-ginsenoside R7 to ST-4 with a molar yield of 100% and a space-time yield of 104mg/L/h in optimized conditions. These results underscore that HaGH03 has much potential for the effective preparation of target ginsenosides possessing valuable pharmacological activities. This is the first report identifying an enzyme that has the ability to transform vina-ginsenoside R7 and provides an approach to preparing rare notoginsenoside ST-4. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Biotransformation  |2 nationallicence 
690 7 |a Notoginsenoside ST-4  |2 nationallicence 
690 7 |a Vina -ginsenoside R7  |2 nationallicence 
690 7 |a Family 3 glycoside hydrolase  |2 nationallicence 
690 7 |a Herpetosiphon aurantiacus  |2 nationallicence 
690 7 |a Heterologous expression  |2 nationallicence 
700 1 |a Wang  |D Ru-Feng  |u Department of Pharmacognosy, China Pharmaceutical University, 210038, Nanjing, People's Republic of China  |4 aut 
700 1 |a Zheng  |D Ming-Min  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
700 1 |a Cao  |D Yue-De  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
700 1 |a Li  |D Hao  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
700 1 |a Li  |D Chun-Xiu  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
700 1 |a Xu  |D Jian-He  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
700 1 |a Wang  |D Zheng-Tao  |u Department of Pharmacognosy, China Pharmaceutical University, 210038, Nanjing, People's Republic of China  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/8(2015-04-01), 3433-3442  |x 0175-7598  |q 99:8<3433  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6446-z  |q text/html  |z Onlinezugriff via DOI 
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900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
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950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wang  |D Ru-Feng  |u Department of Pharmacognosy, China Pharmaceutical University, 210038, Nanjing, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zheng  |D Ming-Min  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Cao  |D Yue-De  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Li  |D Hao  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Li  |D Chun-Xiu  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Xu  |D Jian-He  |u State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wang  |D Zheng-Tao  |u Department of Pharmacognosy, China Pharmaceutical University, 210038, Nanjing, People's Republic of China  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/8(2015-04-01), 3433-3442  |x 0175-7598  |q 99:8<3433  |1 2015  |2 99  |o 253