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首页> 外文期刊>Biological & pharmaceutical bulletin >Metabolism of Ginsenoside Rb1 by Human Intestinal Microflora and Cloning of Its Metabolizing β-D-Glucosidase from Bifidobacterium longum H-1
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Metabolism of Ginsenoside Rb1 by Human Intestinal Microflora and Cloning of Its Metabolizing β-D-Glucosidase from Bifidobacterium longum H-1

机译：人肠道菌群对人参皂苷Rb1的代谢及其长双歧杆菌H-1的β-D-葡萄糖苷酶的克隆

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To understand the role of intestinal microflora in expressing the pharmacological effect of ginsenoside Rb1, the metabolic activity of ginsenoside Rb1 by 148 fecal specimens was measured and its metabolizing β-glucosidase was cloned. The average activities for p-nitrophenyl-β-D-glucopyranoside and ginsenoside Rb1 were 0.097±0.059 μmol/min/mg and 0.311±0.118 pmol/min/mg, respectively. These enzyme activities were not different between male and female, or between ages. A gene encoding β-D-glucosidase (BglX) was cloned from Bifidobacterium longum H-1, which transformed ginsenoside Rb1 to compound K. The probe for cloning was synthesized from the genes encoding a β-D-glucosidase of previously reported B. longum DJO10A. The sequences of the cloned gene revealed 2364 bp open reading frame (ORF) encoding a protein containing 787 amino acids (molecular weight of 95 kDa). The gene exhibited 99% homology (identities) to that of B. longum. The cloned gene was expressed under T7 promoter of the expression vector, pET-39b(+), in Escherichia coli BL21(DE3), and the expressed enzyme was purified by using HiTrap immobilized metal affinity chromatography (IMAC) HP. The enzyme potently biotransformed ginsenoside Rb1, loganin, arctiin and arbutin to ginsenoside Rd, loganetin, arctigenin and hydroquinone, respectively, but was not active in the case of hesperidin, and kakkalide. This is the first report on cloning and expression of β-D-glucosidase from B. longum. Based on these findings, ginsenoside Rb1 may be metabolized to bioactive compound(s) by exo-β-D-glucosidase(s) produced from the intestinal bacteria and its pharmacological effects may be dependent on intestinal bacterial exo-β-D-glucosidase(s) activity.
机译：为了了解肠道​​菌群在表达人参皂苷Rb1药理作用中的作用，测定了148个粪便样品中人参皂甙Rb1的代谢活性，并克隆了其代谢β-葡萄糖苷酶。对硝基苯基-β-D-吡喃葡萄糖苷和人参皂苷Rb1的平均活性分别为0.097±0.059μmol/ min / mg和0.311±0.118 pmol / min / mg。这些酶的活性在雄性和雌性之间或年龄之间没有差异。从长双歧杆菌H-1中克隆了一个编码β-D-葡萄糖苷酶（BglX）的基因，将人参皂苷Rb1转化为化合物K。克隆探针是由先前报道的长双歧杆菌β-D-葡萄糖苷酶的编码基因合成的。 DJO10A。克隆的基因序列揭示了2364 bp的开放阅读框（ORF），其编码包含787个氨基酸（分子量为95 kDa）的蛋白质。该基因与长双歧杆菌显示99％的同源性（同一性）。克隆的基因在大肠杆菌BL21（DE3）中的表达载体pET-39b（+）的T7启动子下表达，并使用HiTrap固定金属亲和色谱（IMAC）HP纯化表达的酶。该酶有效地将人参皂苷Rb1，loganin，arctiin和熊果苷生物转化为人参皂苷Rd，loganetin，arctigenin和对苯二酚，但对橙皮苷和kakkalide无效。这是关于长双歧杆菌β-D-葡萄糖苷酶的克隆和表达的首次报道。基于这些发现，人参皂甙Rb1可能会被肠道细菌产生的外泌β-D-D-葡萄糖苷酶代谢为生物活性化合物，其药理作用可能取决于肠道细菌外泌β-D-D-葡萄糖苷酶（ s）活动。

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