PURIFICATION AND PROPERTIES OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM BREVIBACTERIUM SP NO-9605

被引：36

作者：

MORI, S ^{[1
]}

HIROSE, S ^{[1
]}

OYA, T ^{[1
]}

KITAHATA, S ^{[1
]}

机构：

[1] OSAKA MUNICIPAL TECH RES INST, JOTO KU, OSAKA 536, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1994年 / 58卷 / 11期

关键词：

D O I：

10.1271/bbb.58.1968

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 (EC 2.4.1.19) from Brevibacterium sp. No. 9605 was purified to homogeneity by chromatography on butyl-Toyopearl 650M, gamma-cyclodextrin-Sepharose 4B, and Toyopearl HW-55S. The molecular weight of the purified enzyme was estimated to be 75,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of the purified enzyme was 2.8. The optimum pH and temperature were pH 10 and 45 degrees C, respectively. The enzyme was stable at the range of pH 6-8 and at temperatures 50 degrees C or less in the presence of CaCl2. The enzyme produced mainly gamma-cyclodextrin from starch in the initial stage of reaction, but later, the proportion of beta-cyclodextrin was increased.

引用

页码：1968 / 1972

页数：5

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