Transcriptome profiling, cloning, and characterization of AnGlu04478, a Ginsenoside Hydrolyzing β-glucosidase from Aspergillus niger NG1306 DOI Creative Commons
Ming-Xing Jiang, Ling Zhu,

Shuhan Xie

и другие.

Research Square (Research Square), Год журнала: 2023, Номер unknown

Опубликована: Ноя. 21, 2023

Abstract Minor ginsenosides exhibit superior pharmacological activity compared to major ginsenosides, yet their presence in plants is limited. Therefore, it crucial efficiently obtain minor ginsenosides. Specific glycoside hydrolases offer the advantage of converting into specific counterparts under mild reaction conditions while minimizing structural damage. In this study, we utilized total extracted from Panax notoginseng leaves as substrates stimulate growth Aspergillus niger NG1306. Transcriptome analysis revealed that Anglu 04478 potentially participates biotransformation process Subsequently, was cloned and expressed Transetta (DE3). The An Glu04478 protein purified by Ni 2+ column its enzymatic properties were characterized. results show optimum pH 4.5 temperature 40°C, Cu had a certain inhibitory effect on Glu04478, other metal ions little it. tolerance ethanol, not significantly affected product (glucose) feedback inhibition. Using p NPG substrate, kinetic parameter K m 1.55 mmol/L, V max 0.014 mmol/min. test with substrate showed could selectively hydrolyze glucose ginsenoside Rb1, Rb2, Rb3 Rc at C3, putative metabolic pathway Rb1 → GypXVII, Rb2 C-O, C-Mx1 C-Mx, →C-Mc1.These findings indicate exhibits promiscuity β-glucosidase, thereby expanding options for biotransformation.

Язык: Английский

Strategic enrichment of ocotillol-type ginsenosides F11, RT5 and ocotillol from Panax quinquefolium DOI

Wenyu Dou,

Zongzhan Wu,

C.W. Huang

и другие.

Industrial Crops and Products, Год журнала: 2024, Номер 218, С. 118953 - 118953

Опубликована: Июнь 14, 2024

Язык: Английский

Процитировано

1
Immobilization of Bgps-Expressing Escherichia coli cells coated with ZIF-67 for the production of rare ginsenoside F1 DOI
Anni Zheng, Hao Liang

Biochemical Engineering Journal, Год журнала: 2024, Номер 210, С. 109432 - 109432

Опубликована: Июль 14, 2024

Язык: Английский

Процитировано

1
A GH1 β-glucosidase from the Fervidobacterium pennivorans DSM9078 showed extraordinary thermostability and distinctive ability in the efficient transformation of ginsenosides DOI

Kailu Zhou,

Yangyang Zhang, Minghao Xu

и другие.

Bioorganic Chemistry, Год журнала: 2024, Номер 154, С. 108049 - 108049

Опубликована: Дек. 9, 2024

Язык: Английский

Процитировано

1
Transcriptome Profiling, Cloning, and Characterization of AnGlu04478, a Ginsenoside Hydrolyzing β-Glucosidase from Aspergillus niger NG1306 DOI Creative Commons
Ming-Xing Jiang, Ling Zhu,

Shuhan Xie

и другие.

Current Microbiology, Год журнала: 2024, Номер 82(1)

Опубликована: Дек. 24, 2024

β-Glucosidase plays a pivotal role in transforming ginsenosides into specific minor ginsenosides. In this study, total from Panax notoginseng leaves were used as substrates to stimulate the growth of Aspergillus niger NG1306. Transcriptome analysis identified β-glucosidase gene, Anglu04478 (1455 bp, 484 amino acids, 54.5 kDa, pI = 5.1), participant biotransformation process. This gene was cloned and expressed Escherichia coli BL21 Transetta (DE3). The AnGlu04478 protein purified using Ni2+ column, its enzymatic properties characterized. Purified exhibited activity 32.97 U/mg when assayed against pNPG. Under optimal conditions (pH 4.5, temperature 40 °C), kinetic parameters, Km Vmax, for pNPG 1.55 mmol/L 0.014 mmol/min, respectively. Cu2+ displayed an inhibitory effect on AnGlu04478, whereas Ca2+, Co2+, ions had minimal impact. enzyme showed tolerance ethanol largely unaffected by glucose feedback inhibition. Testing with revealed selective hydrolysis at C3 position Rb1, Rb2, Rb3, Rc, metabolic pathway delineated Rb1 → GypXVII, Rb2 C–O, Rb3 C-Mx1 C-Mx, Rc C-Mc1. conversion rates varied 2.58 20.63%. With 0.5 U mg ginsenosides, incubated °C 12 h, 42.6% 10.4% 6.27% C-Mx1, 26.96% 90% Rc. These results suggest that displays substrate promiscuity β-glucosidase, thus broadening potential ginsenoside biotransformation.

Язык: Английский

Процитировано

0
Transcriptome profiling, cloning, and characterization of AnGlu04478, a Ginsenoside Hydrolyzing β-glucosidase from Aspergillus niger NG1306 DOI Creative Commons
Ming-Xing Jiang, Ling Zhu,

Shuhan Xie

и другие.

Research Square (Research Square), Год журнала: 2023, Номер unknown

Опубликована: Ноя. 21, 2023

Abstract Minor ginsenosides exhibit superior pharmacological activity compared to major ginsenosides, yet their presence in plants is limited. Therefore, it crucial efficiently obtain minor ginsenosides. Specific glycoside hydrolases offer the advantage of converting into specific counterparts under mild reaction conditions while minimizing structural damage. In this study, we utilized total extracted from Panax notoginseng leaves as substrates stimulate growth Aspergillus niger NG1306. Transcriptome analysis revealed that Anglu 04478 potentially participates biotransformation process Subsequently, was cloned and expressed Transetta (DE3). The An Glu04478 protein purified by Ni 2+ column its enzymatic properties were characterized. results show optimum pH 4.5 temperature 40°C, Cu had a certain inhibitory effect on Glu04478, other metal ions little it. tolerance ethanol, not significantly affected product (glucose) feedback inhibition. Using p NPG substrate, kinetic parameter K m 1.55 mmol/L, V max 0.014 mmol/min. test with substrate showed could selectively hydrolyze glucose ginsenoside Rb1, Rb2, Rb3 Rc at C3, putative metabolic pathway Rb1 → GypXVII, Rb2 C-O, C-Mx1 C-Mx, →C-Mc1.These findings indicate exhibits promiscuity β-glucosidase, thereby expanding options for biotransformation.

Язык: Английский

Процитировано

0