A fungal peroxidase from Coprinus cinereus (CiP) was successfully being used for the oxidative polymerization of phenolic compounds. During polymerization reaction, CiP showed low stability in organic solvent especially water miscible solvent such as 2-propanol. Generally speaking, the thermostability of enzyme can be related with the stability in organic solvent. CiP variants were created by site directed mutagenesis and their enzymatic activities in organic solvent and the thermostability were studied. In various CiP variants, the C50 values were remarkably higher for the thermostable variants than for the other mutated variants. The stability in organic solvent is proportionate to thermal stability for CiP variants. Furthermore, the strongly stable CiP variant against thermal inactivation also showed the resistance against to organic solvent, which suggests that the mechanism of irreversible thermal and solvent-induced inactivation seem to be similar.
키워드
peroxidasethermostabilityorganic solvent
저자
Su Jin KIM [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
Yong Hwan KIM [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
Bong Keun SONG [ Korea Research Institute of Chemical Technology. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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