Immobilized-enzyme activity under isothermal and non-isothermal conditions: Studies on beta-galactosidase as a model enzyme

被引：0
|
作者：
Mita, DG
Portaccio, M
Russo, P
Stellato, S
Toscano, G
Bencivenga, U
Canciglia, P
DAcunto, A
Pagliuca, N
Rossi, S
Gaeta, FS
机构：
[1] UNIV NAPLES 2,FAC MED & SURG,DIPARTIMENTO FISIOL UMANA & FUNZIONI BIOL INTEGRA,I-80138 NAPLES,ITALY
[2] UNIV MESSINA,FAC SCI,INST GEN PHYSIOL,I-98020 MESSINA,ITALY
[3] CNR,IST SCI ALIMENTAZ,I-83100 AVELLINO,ITALY
来源：
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY | 1995年 / 22卷
关键词：
D O I：
暂无
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：
The behaviour of catalytic reactions was studied when an enzyme is immobilized to a membrane interposed between two solutions of identical substrate concentration, kept at different temperatures. beta-Galactosidase was studied as a model enzyme. In the presence of a temperature gradient the apparent enzyme activity is higher than in comparable isothermal conditions. The activity increase is proportional to the applied transmembrane temperature difference. Two possible explanations are proposed for this behaviour. Various biotechnological applications are suggested.
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收藏
页码：281 / 294
页数：14
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