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Purification and Characterization of a Novel Alcohol Oxidase from Paenibacillus sp.AIU 311

机译:一种来自Paenibacillus sp.AIU 311的新型醇氧化酶的纯化和鉴定

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An oxidase catalyzing the conversion of glycolaldehyde to glyoxal was purified to the homogeneous state from Paenibacillus sp.AIU 311,and its properties were revealed.This enzyme was specific to glycolaldehyde and glyceraldehyde,and the reaction rates to other alcohols and aldehydes were less than 6% of that of glycolaldehyde.The K_m values for glycolaldehyde and glyceraldehyde were estimated to be 13.2 and 7.5 mM,respectively.The glycolaldehyde oxidation was optimum at pH 6.5 and 50 deg C.The molecular mass of this enzyme was 49 kDa,and it consisted of two identical subunits of 24 kDa.The NH,-terminal sequence was not homologous to those of alcohol oxidases.This is the first report of an oxidase exhibiting high specificity to a hydroxy group of aldehyde alcohols.
机译:从Paenibacillus sp.AIU 311中纯化了一种催化乙醇醛转化为乙二醛的氧化酶,并揭示了其性质。该酶对乙醇醛和甘油醛具有特异性,与其他醇和醛的反应速率小于6乙醇醛和甘油醛的K_m值分别估计为13.2和7.5 mM。乙醇醛氧化在pH 6.5和50摄氏度时最合适。该酶的分子量为49 kDa,由以下组成这是两个相同的24 kDa亚基的一部分.NH,末端序列与醇氧化酶的序列不同源,这是首次报道一种氧化酶对醛醇的羟基具有高度特异性的报道。

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