PARTIAL PURIFICATION AND SOME PROPERTIES OF EMODIN-O-METHYLTRANSFERASE FROM (+)-GEODIN PRODUCING STRAIN OF ASPERGILLUS TERREUS

Abstract

Emodin-1-O-methyltransferase (E-OMT), an enzyme catalysing methylation of emodin and involved in the biosynthesis of (+)-geodin, was purified upto 89 folds by two-step purification with Blue Sepharose and Sepharose 6B column chromatography. The molecular weight of E-OMT was estimated to be 3.4×10⁵, and Km values for emodin and S-adenosylmethionine (SAM) were 3.3×10^-7M and 3.1×10^-6M, respectively. Substrate specificity of E-OMT was extremely strict, and the enzyme seems to recognize whole the molecule of substrates.