PURIFICATION AND PROPERTIES OF ASPERGILLUS-NIGER BETA-GLUCOSIDASE

被引：106

作者：

WATANABE, T ^{[1
]}

SATO, T ^{[1
]}

YOSHIOKA, S ^{[1
]}

KOSHIJIMA, T ^{[1
]}

KUWAHARA, M ^{[1
]}

机构：

[1] KINKI UNIV, FAC AGR, NARA, JAPAN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 209卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb17332.x

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：

Beta-Glucosidase was purified from a crude cellulase preparation from Aspergillus niger by affinity chromatography on a methacrylamide-N-methylene-bis-methacrylamide copolymer bearing cellobiamine. The purified enzyme was a dimer with an isoelectric point of 4.0. The molecular mass of the enzyme was estimated to be 240 kDa by gel-permeation chromatography. The enzyme hydrolyzed specificically beta-glucosidic bonds and catalyzed transglucosylation of the beta-glucosyl group of cellobiose to yield 4-O-beta-gentiobiosylglucose in the presence of organic solvents or under neutral conditions.

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页码：651 / 659

页数：9

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