Characterization of recombinant β-glucosidase from Arthrobacter chlorophenolicus and biotransformation of ginsenosides Rb1, Rb2, Rc, and Rd

Park, Myung Keun; Cui, Chang-Hao; Park, Sung Chul; Park, Seul-Ki; Kim, Jin-Kwang; Jung, Mi-Sun; Jung, Suk-Chae; Kim, Sun-Chang; Im, Wan‐Taek

doi:10.1007/s12275-014-3601-7

Cited by 13 publications

(3 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AbpBs activity was weakly affected by β-mercaptoethanol in accordance with concentration, which is well known of thiol group inhibitors. These results suggested that sulfhydryl groups may be involved in the catalytic center of the enzyme [27][28][29]. The enzyme did not require Mg 2+ for activity and was enhanced by 1 mM of Na + , K + , Mg 2+ , Mn 2+ , Ca 2+ , and Co 2+ .…”

Section: Enzyme Characterizationmentioning

confidence: 87%

Enzymatic Biotransformation of Ginsenoside Rb2 into Rd by Recombinant ��-L-Arabinopyranosidase from Blastococcus saxobsidens

Kim

Chun

et al. 2020

Journal of Microbiology and Biotechnology

Self Cite

View full text Add to dashboard Cite

In this study, we used a novel α-L-arabinopyranosidase (AbpBs) obtained from ginsenosideconverting Blastococcus saxobsidens that was cloned and expressed in Escherichia coli BL21 (DE3), and then applied it in the biotransformation of ginsenoside Rb 2 into Rd. The gene, termed AbpBs, consisting of 2,406 nucleotides (801 amino acid residues), and with a predicted translated protein molecular mass of 86.4 kDa, was cloned into a pGEX4T-1 vector. A BLAST search using the AbpBs amino acid sequence revealed significant homology with a family 2 glycoside hydrolase (GH2). The over-expressed recombinant AbpBs in Escherichia coli BL21 (DE3) catalyzed the hydrolysis of the arabinopyranose moiety attached to the C-20 position of ginsenoside Rb 2 under optimal conditions (pH 7.0 and 40°C). Kinetic parameters for α-Larabinopyranosidase showed apparent K m and V max values of 0.078 ± 0.0002 μM and 1.4 ± 0.1 μmol/min/mg of protein against p-nitrophenyl-α-L-arabinopyranoside. Using a purified AbpBs (1 μg/ml), 0.1% of ginsenoside Rb 2 was completely converted to ginsenoside Rd within 1 h. The recombinant AbpBs could be useful for high-yield, rapid, and low-cost preparation of ginsenoside Rd from Rb 2 .

show abstract

Section: Enzyme Characterizationmentioning

confidence: 87%

Enzymatic Biotransformation of Ginsenoside Rb2 into Rd by Recombinant ��-L-Arabinopyranosidase from Blastococcus saxobsidens

Kim

Chun

et al. 2020

Journal of Microbiology and Biotechnology

Self Cite

View full text Add to dashboard Cite

show abstract

“…These minor ginsenosides show highly significant pharmacological activities including anti-fatigue, anti-inflammation, anti-neoplastic, anti-fatigue, anti-oxidant and anti-diabetic effects. The enzymatic transformation on these compounds is advantageous as it results in fewer byproducts, better environmental protection and higher stereo-specificity [29].…”

Section: Production Of Enzymes With Biomedical Applications By Arthromentioning

confidence: 99%

Arthrobacter as Biofactory of Therapeutic Enzymes

Azmi¹,

Chaudhary²

2018

Int J Pharm Pharm Sci

View full text Add to dashboard Cite

Therapeutic enzymes are proteins which can be used to treat rare and deadly diseases. They represent a small but profitable market. Therapeutic enzymes are superior to non-enzymatic drugs owing to their high specificity toward the target and also their ability to multiple substrate conversion. They are essential for speeding up all the metabolic processes and many a life-supporting chemical inter-conversions. Actinomycetes including Arthrobacter form an enormous reservoir of secondary metabolites and enzymes. The characterization of L-asparaginase, β-glucosidase, urate oxidase, methionine γ-lyase, acetyl cholinesterase, and arginase activities from actinomycetes Arthrobacter clearly demonstrate the potential of Arthrobacter as potent producer of therapeutic enzymes. These metabolic enzymes can be used either separately or in combination with other therapies for the treatment of several diseases such as leukemia, gout, asthma, and neurological disorders. The objective of this review is to compile the information on the application of therapeutic enzymes produced by Arthrobacter and their future prospects as drugs.

show abstract

“…Many enzymes have been explored to efficiently convert major ginsenosides into pharmacologically active, rare minor ginsenosides [5,13,14]. Prior to this study, our research group cloned, characterized and applied many efficient glycoside hydrolases for the gram-scale production and purification of minor ginsenosides [15][16][17][18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Ginsenoside MT1 Produced by an Enzymatic Transrhamnosylation of Protopanaxatriol-Type Ginsenosides Re

et al. 2020

Self Cite

View full text Add to dashboard Cite

Background: Ginsenosides, triterpene saponins of Panax species, are considered the main active ingredients responsible for various pharmacological activities. Herein, a new protopanaxatriol-type ginsenoside called “ginsenoside MT1” is described; it was accidentally found among the enzymatic conversion products of ginsenoside Re. Method: We analyzed the conversion mechanism and found that recombinant β-glucosidase (MT619) transglycosylated the outer rhamnopyranoside of Re at the C-6 position to glucopyranoside at C-20. The production of MT1 by trans-rhamnosylation was optimized and pure MT1 was obtained through various chromatographic processes. Results: The structure of MT1 was elucidated based on spectral data: (20S)-3β,6α,12β,20-tetrahydroxydammarene-20-O-[α-L-rhamnopyranosyl(1→2)-β-D-glucopyranoside]. This dammarane-type triterpene saponin was confirmed as a novel compound. Conclusion: Based on the functions of ginsenosides with similar structures, we believe that this ginsenoside MT1 may have great potential in the development of nutraceutical, pharmaceutical or cosmeceutical products.

show abstract

Characterization of recombinant β-glucosidase from Arthrobacter chlorophenolicus and biotransformation of ginsenosides Rb1, Rb2, Rc, and Rd

Cited by 13 publications

References 35 publications

Enzymatic Biotransformation of Ginsenoside Rb2 into Rd by Recombinant ��-L-Arabinopyranosidase from Blastococcus saxobsidens

Enzymatic Biotransformation of Ginsenoside Rb2 into Rd by Recombinant ��-L-Arabinopyranosidase from Blastococcus saxobsidens

Arthrobacter as Biofactory of Therapeutic Enzymes

Characterization of a Novel Ginsenoside MT1 Produced by an Enzymatic Transrhamnosylation of Protopanaxatriol-Type Ginsenosides Re

Contact Info

Product

Resources

About