Simple Purification and Characterization of an Extracellular Dextrin Dextranase from Acetobacter capsulatum ATCC 11894

Simple Purification and Characterization of an Extracellular Dextrin Dextranase from Acetobacter capsulatum ATCC 11894
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DOI:
10.5458/jag.46.469
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发表时间:
1999-12
影响因子:
1.1
通讯作者:
Masayuki Suzuki;T. Unno;Gentaro Okadal
Masayuki Suzuki;T. Unno;Gentaro Okadal
中科院分区:
--
文献类型:
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作者:
Masayuki Suzuki;T. Unno;Gentaro Okadal

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到目前为止,关于糊精转酶(DDase, EC 2.4.1.2)的报道很少。1947年,Shimwell在粘稠的啤酒中发现了一种醋酸细菌,并仔细地将其分离出来。1951年Hehre和Hamilton报道(1)利用荚膜醋酸杆菌ATCC 11894或a . viscosum ATCC 11895中的DDase,以糊精作为葡萄糖基供体制备了一种粘性物质;(2)DDase主要与麦芽糖以外的一系列麦芽糖低聚糖反应,不与直链淀粉、支链淀粉、糖原、环糊精、蔗糖、葡萄糖等反应。但是,在那个时候,酶本身只是一种无细胞提取物,没有进行高水平的酶纯化。1992-1994年,Yamamoto等人报道了胞内DDase的纯化方法及其理化和酶学性质。6,7)他们还提到(1)DDase产生的葡聚糖的分子结构与Leuconostoc葡聚糖有很大的不同,5)和(2)通过DDase的a-1,6转糖基化有效地产生糖基甜菊苷。8)最近,我们发现A. capsulatum ATCC 11894能有效地产生胞外DDase。在本文中,我们报告了简单的。净化
Only a few reports concerning dextrin dex tranase (DDase, EC 2.4.1.2) have been published so f ar.1-8) In 1947, Shimwell found an acetic acid bacteria grown in a ropy beer and isolated it carefully.' In 1951, Hehre and Hamilton reported that (1) a viscous material was pro duced from dextrin as glucosyl donor by DDase from Acetobacter capsulatum ATCC 11894 or A. viscosum ATCC 11895, and (2) DDase mainly reacted with a series of malto oligosaccharides except maltose and did not react with amylose, amylopectin, glycogen, cyclodextrin, sucrose, glucose and others.2-4) But, at that time, the enzyme itself was only a cell-free extract and a high level of enzyme purification was not done. In 1992-1994, Yamamoto et al. reported the purification procedures of intracellular DDase from A. capsulatus ATCC 118945) and some of its physico chemical and enzymatic properties. 6,7) They also referred (1) that the molecular structure of dextran produced by DDase was quite different from that of Leuconostoc dextran,5) and (2) the effective production of glucosyl-steviosides by a-1,6 transglucosylation of DDase.8) Recently, we found that A. capsulatum ATCC 11894 effectively produced extracellular DDase. In this paper, we report the simple. purification