期刊
BIOCATALYSIS AND BIOTRANSFORMATION
卷 28, 期 3, 页码 222-226出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/10242422.2010.489943
关键词
Peroxidase; N-oxidation; metalloenzyme; Musa paradisiaca; arylamine; nitrosobenzene
N-Oxidation of arylamines to their corresponding nitrosobenzenes using a new chloroperoxidase purified from Musa paradisiaca stem juice has been examined. The enzymatic characteristics of the stem chloroperoxidase using 4-chloroaniline as substrate were determined. The K-m values for 4-chloroaniline and H2O2 were 770 mu M and 154 mu M respectively, while the pH and temperature optima were 4.4 and 30 degrees C respectively. The substrate specificities of the enzyme for the arylamines 3,4-dichloroamine, p-aminobenzoic acid, p-toluidine, p-anisidine, m-anisidine, p-aminophenol, o-aminophenol and m-aminophenol have been characterized. The feasibility of using concentrated M. paradisiaca stem juice for the specific conversion of 4-chloroaniline to 4-chloronitrosobenzene has been demonstrated. This enzyme can be used for the N-oxidation of other arylamines.
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