Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat)

…, H Komeda, Y Asano, A H-KITTIKUN

Index: Ueatrongchit, Techawaree; Kayo, Ai; Komeda, Hidenobu; Asano, Yasuhisa; H-Kittikun, Aran Bioscience, Biotechnology and Biochemistry, 2008 , vol. 72, # 6 p. 1513 - 1522

Full Text: HTML

Citation Number: 19

Abstract

A hydroxynitrile lyase was isolated and purified to homogeneity from seeds of Eriobotrya japonica (loquat). The final yield, of 36% with 49-fold purification, was obtained by 30– 80%(NH4) 2SO4 fractionation and column chromatography on DEAE-Toyopearl and Concanavalin A Sepharose 4B, which suggested the presence of a carbohydrate side chain. The purified enzyme was a monomer with a molecular mass of 72 kDa as determined by ...