Oxidation of carbonyl compounds by whole-cell biocatalyst
World Journal of Microbiology and Biotechnology (Impact Factor: 1.78). 01/2005; 21(4):457-461. DOI: 10.1007/s11274-004-2467-y
Acinetobacter junii was found to catalyse the oxidative biotransformation of benzaldehyde, 4-methoxybenzaldehyde, vanillin, 3,4-dimethoxybenzaldehyde, 3-methoxybenzaldehyde and phthalaldehyde within 48 h of incubation. During this process, the activities of drug-metabolizing enzymes, such as cytochrome P-450 and acetanilide hydroxylase were found to be increased significantly. Such an increase in activity indicates their involvement in the biotransformation processes. The purified biotransformed products of each carbonyl compound were characterized by H1 NMR and IR spectroscopy, confirming that oxidation to the corresponding carboxylic acid had occurred.
- [Show abstract] [Hide abstract]
ABSTRACT: Acinetobacter junii A8 was able to biotransform nitroaromatic compounds like o-nitroaniline, o-nitrotoluene, m-nitrotoluene, 2,4,6-trinitrotoluene and o-nitrophenol under aerobic condition, within 36 h of incubation. These compounds, which are normally considered to be toxic to microorganisms, caused the induction of drug metabolizing enzymes such as cytochrome P-450, aminopyrine N-demethylase, acetanilide hydroxylase and glutathione S-transferase. These enzymes constitute the bacterial mixed function oxidase system. Induction of this system implies its involvement in biotransformation of these nitro compounds. The biotransformed metabolites were characterized by IR, 1H NMR and GC–mass spectroscopy. It was observed that o-nitroaniline and m-nitrotoluene were reduced to their respective amines, whereas o-nitrotoluene was oxidized to acid. However, 2,4,6-trinitrotoluene (TNT) and o-nitrophenol were completely mineralized. The metabolites of TNT biotransformation were characterized as 2,6-dinitro-4-nitrosotoluene, 4-amino-2,6-dinitrotoluene and 4-amino-2,6-dinitrobenzoic acid. The result of this study showed that these nitroaromatics induced the mixed function oxidase system, which resulted in the degradation of these compounds.Enzyme and Microbial Technology 10/2005; 37(5-37):527-533. DOI:10.1016/j.enzmictec.2005.03.011 · 2.32 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.