INCREASING CATALYST ACTIVITY BY IMMOBILIZATION OF ENZYME CONJUGATES

被引：4

作者：

ATALLAH, MT ^{[1
]}

WASSERMAN, BP ^{[1
]}

HULTIN, HO ^{[1
]}

机构：

[1] UNIV MASSACHUSETTS, DEPT FOOD SCI & NUTR, AMHERST, MA 01002 USA

来源：

BIOTECHNOLOGY AND BIOENGINEERING | 1976年 / 18卷 / 12期

关键词：

D O I：

10.1002/bit.260181218

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：

The feasibility and advantages of immobilizing more than 1 enzyme molecule/binding site were studied. By using glutaraldehyde as the crosslinking agent, soluble conjugates of glucose oxidase (GOX) [Aspergillus niger] and catalase (CAT) [A. niger] were prepared and immobilized to a solid matrix. Activities of catalysts prepared with conjugated and with nonconjugated enzymes were compared. The specific activities of the nonporous glass catalysts obtained were 40-fold higher when GOX conjugates were used as compared to untreated enzymes.

引用

页码：1833 / 1837

页数：5