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

A novel GH1 β-glucosidase Fpglu1 from Fervidobacterium pennivorans DSM9078 was successfully cloned and expressed in Escherichia coli. This hyperthermophilic enzyme possesses unique features that make it valuable in biochemistry and pharmacology. It exhibited optimal activity at temperatures exceeding 100 °C, a trait rarely observed in other enzymes, and demonstrated extraordinary thermostability.

Production of Gypenoside XVII from Ginsenoside Rb1 by Enzymatic Transformation and Their Anti-Inflammatory Activity In Vitro and In Vivo.

The enzymatic transformation of the sugar moiety of the gypenosides provides a new way to obtain more pharmacologically active components. A gene encoding a family 1 glycosyl hydrolase from was cloned and expressed in . The recombinant enzyme was purified, and its molecular weight was approximately 44 kDa.

Cloning and characterization of thermophilic endoglucanase and its application in the transformation of ginsenosides.

A novel endoglucanase (BcelFp) was identified from Fervidobaterium pennivorans DSM9078 which had biotransformation activity for protopanaxadiol (PPD)-type ginsenosides. Sequence analysis of BcelFp revealed that it could be classified into glycoside hydrolase family 5 (GH5). The gene encoding a 323-amino acid protein was cloned and expressed in Escherichia coli.

Characterization of a novel thermophilic beta-glucosidase from sp. and its application in the transformation of notoginsenoside R1.

A novel β-glucosidase (Thglu3) was identified from sp. which had biotransformation activity for notoginsenoside R1 (NR-R1). Sequence analysis of Thglu3 revealed that it could be classified into glycoside hydrolase family 3 (GH3).

Enzymatic Biotransformation of Gypenoside XLIX into Gylongiposide I and Their Antiviral Roles against Enterovirus 71 In Vitro.

Biotransformation of specific saponins in the valuable medical plants to increase their bioavailability and pharmaceutical activities has attracted more and more attention. A gene encoding a thermophilic glycoside hydrolase from DSM9078 was cloned and expressed in . The purified recombinant enzyme, exhibiting endoglucanase cellulase activity, was used to transform gypenoside XLIX into gylongiposide I via highly selective and efficient hydrolysis of the glucose moiety linked to the C21 position in gypenoside XLIX.

Down-Regulation of miR-7 in Gastric Cancer Is Associated With Elevated LDH-A Expression and Chemoresistance to Cisplatin.

MicroRNAs (miRNAs) are dysregulated in the context of many cancer types, making them potentially ideal diagnostic or therapeutic targets in patients in which they are aberrantly expressed. In the present study, we found miR-7 to be downregulated in gastric cancer (GC), and we further determined its expression to be closely linked to GC sensitivity to the chemotherapeutic compound cisplatin. This effect appears to be at least partially attributable to the regulation of LDH-A, which is a miR-7 target gene and expression of LDH-A is negatively correlated with miR-7 expression in primary GC tumor samples.