EFFECT OF THE ENZYME FORM ON THE ACTIVITY, STABILITY AND ENANTIOSELECTIVITY OF LIPOPROTEIN-LIPASE IN TOLUENE

被引：47

作者：

OTTOLINA, G

CARREA, G

RIVA, S

SARTORE, L

VERONESE, FM

机构：

[1] CNR,IST CHIM ORMONI,VIA MARIO BIANCO 9,I-20131 MILAN,ITALY

[2] DIPARTIMENTO SCI FARMACEUT,I-35131 PADUA,ITALY

来源：

BIOTECHNOLOGY LETTERS | 1992年 / 14卷 / 10期

关键词：

D O I：

10.1007/BF01020635

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 properties of various forms of lipoprotein lipase (powder, adsorbed onto Celite, covalently linked to PEG, with additives) in toluene were investigated. The form of the enzyme dramatically influenced the activity and stability of the enzyme with the highest activity obtained with PEG-lipase and the highest stability with Celite -immobilized lipase. By contrast, the enantioselectivity was only marginally affected.

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页码：947 / 952

页数：6

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