Title of article
Increased thermal stability of cold-adapted esterase at ambient temperatures by immobilization on graphene oxide
Author/Authors
Lee، نويسنده , , Heeyoung and Jeong، نويسنده , , Hae Kyung and Han، نويسنده , , Jinwoo and Chung، نويسنده , , Hye-Shin and Jang، نويسنده , , Sei-Heon and Lee، نويسنده , , ChangWoo، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2013
Pages
4
From page
620
To page
623
Abstract
In this study, the effect of graphene oxide (GO) on the thermal stability of a recombinant esterase from cold-adapted Pseudomonas mandelii, rEstKp, was investigated. The complex GO-rEstKp was formed by cross-linking. Both free rEstKp and GO-rEstKp complex showed similar optimum pH and temperatures. GO-rEstKp complex exhibited enhanced thermal stability at ambient temperatures than rEstKp, which prevented the denaturation of the enzyme by hydrophilic interactions. However, the catalytic efficiency of GO-rEstKp complex was lowered to approximately 40% of that of free rEstKp. This study provides an insight into the addition of GO for industrial applications of cold-adapted enzymes at ambient temperatures.
Keywords
thermal stability , Graphene oxide , Cold-adapted enzyme , Immobilization
Journal title
Bioresource Technology
Serial Year
2013
Journal title
Bioresource Technology
Record number
1934576
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