IMMOBILIZATION OF THE SERINE PROTEASE FROM THERMOMONOSPORA-FUSCA YX ON POROUS-GLASS

被引：7

作者：

GUSEK, TW ^{[1
]}

TYN, MT ^{[1
]}

KINSELLA, JE ^{[1
]}

机构：

[1] CORNELL UNIV,INST FOOD SCI,STOCKING HALL,ITHACA,NY 14853

来源：

BIOTECHNOLOGY AND BIOENGINEERING | 1990年 / 36卷 / 04期

关键词：

D O I：

10.1002/bit.260360412

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：

As much as 84% of the thermostable serine protease from Thermomonospora fusca strain YX was covalently attached to silanized glass using glutaraldehyde. The immobilized protease exhibited a higher temperature optimum (86°C) and pH optimum (9.4) for activity compared to soluble YX‐protease (80°C and pH 9.0, respectively). Immobilization improved enzyme thermo‐stability above 90°C and reduced inactivation during prolonged storage (9% loss of activity after 90 days at 12°C). A continuous‐flow column reactor packed with immobilized protease readily hydrolyzed casein over broad ranges of temperature and pH. Copyright © 1990 John Wiley & Sons, Inc.

引用

页码：411 / 416

页数：6

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