Purification and Properties of Benzyl Alcohol Oxidase from Botrytis cinerea

Autor:	Suzanne Brun, Michel Nicolas, Mireille Goetghebeur, Pierre Galzy
Rok vydání:	1992
Předmět:	Ethanol Cinnamyl alcohol Organic Chemistry Alcohol General Medicine Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Alcohol oxidase Furfuryl alcohol Benzaldehyde chemistry.chemical_compound chemistry Benzyl alcohol Organic chemistry Methanol Molecular Biology Biotechnology
Zdroj:	Bioscience, Biotechnology, and Biochemistry. 56:298-303
ISSN:	1347-6947 0916-8451
DOI:	10.1271/bbb.56.298
Popis:	A benzyl alcohol oxidase (BAO) was purified to homogeneity from Botrytis cinerea. The enzyme was found to have a molecular mass of 214 kD with a trimeric structure, and optimal pH and temperature of 5.0 and 30°C, respectively. The enzyme activity was not sensitive to metal ions or to metal ion chelators, while thiol blocking reagents strongly inhibited BAO activity. Sulfur dioxide irreversibly inhibited the enzyme activity and the inhibitory effect of ethanol was weak and reversible. Benzyl alcohol was the most effective alcohol substrate for BAO. Para or meta monosubstituted benzyl alcohol with methyl or methoxy groups were good substrates. BAO also oxidized cinnamyl alcohol, furfuryl alcohol, and some terpenic alcohols· with an alkenyl group near the reactive carbinol. Secondary alcohol, methanol and phenol were not substrates. Product inhibition studies suggested that benzaldehyde and benzyl alcohol were bound at different places to the active site. O2 was the only electron acceptor identified and Botr...
Databáze:	OpenAIRE
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