Cytochrome P450 isolated from Streptomyces peucetius (CYP107AJ1; molecular mass 45kDa) showing high homology with peroxygenases is believed to catalyze variety of biological reactions which uses peroxides to provide electrons, protons and oxygen, and further evading requirement for a protein partner. Cytochrome P450 used in this study was cloned into pET28(a) to express in E. coli. Soluble protein was subjected to column-chromatographic purification for carrying out enzyme assay. As an attempt to prove its catalytic function, dealkylation of 7-Ethoxycoumarin was carried out. HPLC analysis of the extracted product corresponding to its LC-MS analysis showed dealkylated 7-ethoxycoumarin which was further established by subsequent GC mass spectra.
키워드
Cytochrome P450PeroxygenaseStreptomyces peucetius
저자
Narayan PRASAD NIRAULA [ Institute of Biomolecule Reconstruction (iBR), Department of Pharmaceutical Engineering, Sun Moon University ]
Tae-Jin OH [ Institute of Biomolecule Reconstruction (iBR), Department of Pharmaceutical Engineering, Sun Moon University ]
Eun Young AHN [ Institute of Biomolecule Reconstruction (iBR), Department of Pharmaceutical Engineering, Sun Moon University ]
Jae Kyung SOHNG [ Institute of Biomolecule Reconstruction (iBR), Department of Pharmaceutical Engineering, Sun Moon University ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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