gordonia terrae dsm 43342 (DSMZ)
86
Structured Review
DSMZ
gordonia terrae dsm 43342
Gordonia Terrae Dsm 43342, supplied by DSMZ, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/43277/Gordonia+terrae/goldsworthy_michael_john_howard__2011__hydrocarbon_biosynthesis_in_mycobacterium_sp_ncimb_10403_and_desulfovibrio_desulfuricans-1873-4-15
Average 86 stars, based on 3 article reviews
Gordonia Terrae Dsm 43342, supplied by DSMZ, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/43277/Gordonia+terrae/goldsworthy_michael_john_howard__2011__hydrocarbon_biosynthesis_in_mycobacterium_sp_ncimb_10403_and_desulfovibrio_desulfuricans-1873-4-15
Average 86 stars, based on 3 article reviews
gordonia terrae dsm 43342 - by Bioz Stars,
2026-09
86/100 stars
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Cloning:Article Title: Substrate specificity of β-glucosidase from Gordonia terrae for ginsenosides and its application in the production of ginsenosides Rg₃, Rg₂, and Rh₁ from ginseng root extract. Article Snippet: 1389-1723/$ http://dx.doi A b-glucosidase from Gordonia terrae was cloned and expressed in Escherichia coli.. The recombinant enzyme with a specific activity of 16.4 U/mg for ginsenoside Rb1 was purified using His-trap chromatography.. The purified enzyme specifically hydrolyzed the glucopyranosides at the C-20 position in protopanaxadiol (PPD)-type ginsenosides and hydrolyzed the glucopyranoside at the C-6 or C-20 position in protopanaxatriol (PPT)-type ginsenosides. Gene Expression:Article Title: Substrate specificity of β-glucosidase from Gordonia terrae for ginsenosides and its application in the production of ginsenosides Rg₃, Rg₂, and Rh₁ from ginseng root extract. Article Snippet: 1389-1723/$ http://dx.doi A b-glucosidase from Gordonia terrae was cloned and expressed in Escherichia coli.. The recombinant enzyme with a specific activity of 16.4 U/mg for ginsenoside Rb1 was purified using His-trap chromatography.. The purified enzyme specifically hydrolyzed the glucopyranosides at the C-20 position in protopanaxadiol (PPD)-type ginsenosides and hydrolyzed the glucopyranoside at the C-6 or C-20 position in protopanaxatriol (PPT)-type ginsenosides. Plasmid Preparation:Article Title: Substrate specificity of β-glucosidase from Gordonia terrae for ginsenosides and its application in the production of ginsenosides Rg₃, Rg₂, and Rh₁ from ginseng root extract. Article Snippet: 1389-1723/$ http://dx.doi A b-glucosidase from Gordonia terrae was cloned and expressed in Escherichia coli.. The recombinant enzyme with a specific activity of 16.4 U/mg for ginsenoside Rb1 was purified using His-trap chromatography.. The purified enzyme specifically hydrolyzed the glucopyranosides at the C-20 position in protopanaxadiol (PPD)-type ginsenosides and hydrolyzed the glucopyranoside at the C-6 or C-20 position in protopanaxatriol (PPT)-type ginsenosides. Expressing:Article Title: Substrate specificity of β-glucosidase from Gordonia terrae for ginsenosides and its application in the production of ginsenosides Rg₃, Rg₂, and Rh₁ from ginseng root extract. Article Snippet: 1389-1723/$ http://dx.doi A b-glucosidase from Gordonia terrae was cloned and expressed in Escherichia coli.. The recombinant enzyme with a specific activity of 16.4 U/mg for ginsenoside Rb1 was purified using His-trap chromatography.. The purified enzyme specifically hydrolyzed the glucopyranosides at the C-20 position in protopanaxadiol (PPD)-type ginsenosides and hydrolyzed the glucopyranoside at the C-6 or C-20 position in protopanaxatriol (PPT)-type ginsenosides. other:Article Title: Gordonia nitida sp. nov., a bacterium that degrades 3-ethylpyridine and 3-methylpyridine. Article Snippet: Article Title: Hydrocarbon Biosynthesis in Mycobacterium Sp. NCIMB 10403 and Desulfovibrio desulfuricans Article Snippet: Gordonia paraffinivorans HD321 (T), Gordonia terrae DSM 43342 and |