PURIFICATION AND PROPERTIES OF CYCLOMALTODEXTRINASE FROM ALKALOPHILIC BACILLUS SP

被引：29

作者：

YOSHIDA, A ^{[1
]}

IWASAKI, Y ^{[1
]}

AKIBA, T ^{[1
]}

HORIKOSHI, K ^{[1
]}

机构：

[1] INST PHYS & CHEM RES, WAKO, SAITAMA 35101, JAPAN

来源：

JOURNAL OF FERMENTATION AND BIOENGINEERING | 1991年 / 71卷 / 04期

关键词：

D O I：

10.1016/0922-338X(91)90272-I

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

An alkalophilic strain isolated from soil produced intracellular cyclomaltodextrinase on the culture medium at an initial pH of 10.6. The strain was identified as closely resembling Bacillus circulans. The enzyme was purified 252-fold from the cell extract by chitosan treatment, ammonium sulfate fractionation, DEAE-Toyopearl column chromatography, and gel filtration. The pH and temperature optima of the purified enzyme were 6.0 and 50-degrees-C. The molecular weight of the enzyme was 126,000, with two subunits of 67,000. The isoelectric point was pH 4.2. Enzyme activity was inhibited by Ag+, Hg2+, Cu2+, and p-chloromercuribenzoate. The enzyme hydrolyzed alpha-, beta-, and gamma-cyclodextrins, as well as linear maltodextrins, to yield maltooligosaccharides. Starch and maltose were not degraded by the enzyme.

引用

页码：226 / 229

页数：4

共 13 条

[1] ENZYMATIC DEGRADATION OF ALPHA-CYCLODEXTRINS AND BETA-CYCLODEXTRINS BY BACTEROIDES OF THE HUMAN-COLON [J].