A Kinetic Study of an Extracellular Dextrin Dextranase * from Acetobacter capsulatum ATCC 11894
A Kinetic Study of an Extracellular Dextrin Dextranase * from Acetobacter capsulatum ATCC 11894
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DOI：
10.5458/jag.47.27
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发表时间：
2000-03
影响因子：
1.1
通讯作者：
Masayuki Suzuki;T. Unno;G. Okada
中科院分区：
文献类型：
--
作者：
Masayuki Suzuki;T. Unno;G. Okada
在荚膜醋酸杆菌ATCC 11894或粘质醋酸杆菌ATCC 11895培养基中分泌糊精葡聚糖酶（DDase，糊精6-葡萄糖基转移酶，1,4a - d -葡聚糖：1,6a - d -葡聚糖6a -葡萄糖基转移酶：EC 2.4.1.2）。Hehre和Hamilton证明，这些细菌的无细胞提取物通过将供体底物中的葡萄糖基转糖基化到受体分子的非还原末端，从各种麦芽糖低聚物中产生a-1,6葡聚糖（麦芽糖除外）。Yamamoto等人报道了A. capsulatus ATCC 11894.4 6'胞内DDase的纯化、理化和酶学性质、作用机制和底物特异性。然而，DDase合成葡聚糖的动力学尚未被研究。在此之前，我们报道了荚膜芽孢杆菌ATCC 11894胞外DDase的简单纯化和鉴定。在本文中，我们描述了DDase的动力学研究和酶转糖基化产物的分析。
Dextrin dextranase (DDase, Dextrin 6-glucosyltransferase, 1,4a -D-Glucan: 1,6a -D-glucan 6a D-glucosyltransferase: EC 2.4.1.2) was secreted in a culture medium of Acetobacter capsulatum ATCC 11894 or Acetobacter viscosum ATCC 11895.'' Hehre and Hamilton demonstrated that the cell-free extracts of these bacteria produced a-1,6 glucan from various maltooligosaccharides except maltose by the transglucosylation of glucosyl groups in donor substrates to the non-reducing termini of acceptor molecules.2'3' Yamamoto et al. reported the purification, physicochemical and enzymatic properties, action mechanism and substrate specificity of an intracellular DDase from A. capsulatus ATCC 11894.4 6' However, the kinetics for dextran synthesis by DDase have not been investigated. Previously, we reported the simple purification and characterization of an extracellular DDase from A. capsulatum ATCC 11894.'' In this paper, we describe some kinetic studies of DDase and analyses of enzymatic transglucosylation products.