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.
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