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Measurement and Study of Substrate Specificity of Exoglucosidase Activity in Eutrophic Water

机译:富营养化水中外切葡糖苷酶活性的底物特异性的测定和研究

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The α- and β-glucosidase activity in natural samples can be readily measured during short incubation times (20 min) by using the artificial substrates 4-methylumbelliferyl-α-d-glucoside and 4-methylumbelliferyl-β-d-glucoside. The apparent Km of both α- and β-glucosidase for these respective substrates is 0.01 μM. The homologous disaccharides maltose and cellobiose competitively inhibit α- and β-glucosidase, respectively. Absolute substrate specificity of the α- and β-glucosidase is observed with respect to the configuration of carbon atoms 1 and 4. Enrichment cultures on either α- and β-glucoside result in increasing activity of the corresponding glucosidase, both in absolute terms and with respect to the other glucosidase.
机译:通过使用人工底物4-甲基伞形基-α-d-葡萄糖苷和4-甲基伞形基-β-d-葡萄糖苷,可以在较短的孵育时间(20分钟)内轻松测量天然样品中的α-和β-葡萄糖苷酶活性。这些相应底物的α-和β-葡萄糖苷酶的表观Km为0.01μM。同源二糖麦芽糖和纤维二糖分别竞争性抑制α-和β-葡萄糖苷酶。相对于碳原子1和4的构型,可以观察到α-和β-葡萄糖苷酶的绝对底物特异性。无论在绝对值上还是在绝对值上,在α-和β-葡萄糖苷上进行的富集培养都会增加相应的葡萄糖苷酶的活性。关于其他葡糖苷酶。

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