PURIFICATION AND CHARACTERIZATION OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM AN ALKALOPHILIC BACILLUS SPECIES AND TRANSGLYCOSYLATION AT ALKALINE PHS

被引：35

作者：

KOMETANI, T

TERADA, Y

NISHIMURA, T

TAKII, H

OKADA, S

机构：

[1] Biochemical Research Laboratory, Ezaki Glico Co., Ltd., Osaka, Utajima 4-6-5, Nishiyodogawa

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1994年 / 58卷 / 03期

关键词：

D O I：

10.1271/bbb.58.517

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cyclodextrin glucanotransferase (1,4-alpha-D-glucan 4-alpha-D-(1,4-alpha-D-glucano)-transferase (cyclizing), EC 2.4.1.19, CGTase) from an alkalophilic Bacillus species was purified by starch adsorption and Q-Sepharose chromatography. The purified enzyme had cyclizing activity, transglycosylating (coupling) activity, and starch-hydrolyzing activity, and their pH-activity curves had a single peak (pH 5.5 as the optimum pH) with a broad shoulder at alkaline pHs. Transglycosylation to various saccharides and flavonoids at alkaline pH was more effective than that at neutral pH. Among flavonoids, those containing rutinose (diosmin and hesperidin) were transglycosylated more effectively than those containing neohesperidose (naringin and neohesperidin).

引用

页码：517 / 520

页数：4

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