Increased thermal stability of cold-adapted esterase at ambient temperatures by immobilization on graphene oxide.
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.
Department of Biomedical Science, Daegu University, Gyeongsan 712-714, South Korea; Center for Bio-Nanomaterials, Daegu University, Gyeongsan 712-714, South Korea.
Heeyoung
H
Lee
Hae Kyung
HK
Jeong
Jinwoo
J
Han
Hye-Shin
HS
Chung
Sei-Heon
SH
Jang
Changwoo
C
Lee
D003080:Cold Temperature; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004950:Esterases / Q000378:metabolism*; D006108:Graphite / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010087:Oxides / Q000737:chemistry*; D011549:Pseudomonas / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism; D059027:Recycling; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D004800:Enzymes, Immobilized; D010087:Oxides; D011994:Recombinant Proteins; D006108:Graphite; D004950:Esterases
Cold-adapted enzyme; Graphene oxide; Immobilization; Thermal stability