Microsome-bound alcohol oxidase catalyzed production of carbonyl compounds from alcohol substrates

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• 作者：Ankana Kakoti^a ; Adepu Kiran Kumar^a ; ^b ; ¹ ; Pranab Goswami^a ; ^{pgoswami@iitg.ernet.in}
• 关键词：AOX ; alcohol oxidase ; ADH ; alcohol dehydrogenase ; DNPH ; dinitrophenyl hydrazine
• 刊名：Journal of Molecular Catalysis B ; Enzymatic
• 出版年：2012
• 期刊代码：55_13811177
• 类别：ce
• 出版时间：June, 2012
• 卷：78
• 期：Complete
• 页码：98-104
• 文件大小：939 K

摘要

High yield conversion of a wide range of alcohol substrates to their corresponding aldehydes was demonstrated using a microsomal alcohol oxidase (AOx) from Aspergillus terreus. The microsome bound AOx preparation was then immobilized into polyurethane foam matrix following a simple adsorption technique. The successful immobilization of the enzyme into the foam matrix was demonstrated microscopically and by biological staining. The enzyme loading was measured as 鈭?.02 U mg^鈭? (76.6 mg protein%) of polyurethane foam. The optimum activity of the immobilized enzyme was detected in the pH range 7.0-8.0. The catalytic activity of the immobilized AOx was utilized for the production of n-heptanal. A maximum n-heptanal yield of 20.7 卤 1.2%(w/w) was achieved at a substrate concentration of 10 mM n-heptanol; beyond this concentration substrate dependent inhibition of the catalytic reaction was observed. The operational stability of the immobilized enzyme was determined and found to be 鈭?0%of the initial activity till the fifth reaction cycle, thus providing high cumulative yield of the product. The deactivation (k_d) and half-life time (t_1/2) of the immobilized enzyme were 5.17 脳 10^鈭? min^鈭? and 鈭? days, respectively. The results demonstrated the potential application of the polyurethane foam immobilized microsomal AOx-based environmentally benign biocatalytic process for the production of industrially important n-heptanal.