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Stabilization of free and immobilized enzymes using hyperthermophilic chaperonin

Paper ID Volume ID Publish Year Pages File Format Full-Text
22375 43273 2006 6 PDF Available
Title
Stabilization of free and immobilized enzymes using hyperthermophilic chaperonin
Abstract

Chaperonins suppress the denaturation of proteins and promote protein folding in vivo. Because hyperthermophilic chaperonins are expected to be used as a stabilizer for proteins, the effects of a group II chaperonin from a hyperthermophilic archaeum, Thermococcus strain KS-1 (T. KS-1 cpn), on the stabilization of mesophilic and thermophilic free enzymes and an enzyme co-immobilized with T. KS-1 cpn were studied. T. KS-1 cpn prevented the thermal inactivation of yeast alcohol dehydrogenase (ADH), jack bean urease, and Thermus flavus malate dehydrogenase (MDH) at high temperatures. T. KS-1 cpn also improved the long-term stability of ADH at lower temperatures. Moreover, the residual ADH activity of ADH co-entrapped with T. KS-1 cpn was improved and maintained at a higher level than that of the entrapped ADH without chaperonin. T. KS-1 cpn is useful for the stabilization of free and immobilized enzymes and applicable to various fields of biotechnology.

Keywords
archaea; chaperonin; heat stabilization; hyperthermophile; immobilized enzyme
First Page Preview
Stabilization of free and immobilized enzymes using hyperthermophilic chaperonin
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 101, Issue 2, February 2006, Pages 131–136
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering