Purification and characterization of veratryl alcohol oxidase from Comamonas sp UVS and its role in decolorization of textile dyes

被引：65

作者：

Jadhav, Umesh U. ^{[1
]}

Dawkar, Vishal V. ^{[1
]}

Tamboli, Dhawal P. ^{[2
]}

Govindwar, Sanjay P. ^{[1
]}

机构：

[1] Shivaji Univ, Dept Biochem, Kolhapur 416004, Maharashtra, India

[2] Shivaji Univ, Dept Biotechnol, Kolhapur 416004, Maharashtra, India

来源：

BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | 2009年 / 14卷 / 03期

关键词：

Veratryl alcohol oxidase; Comamonas sp UVS; dye decolorization; metal ions; GC-MS; MANGANESE PEROXIDASE; WASTE-WATER; LACCASE; FUNGUS; DEGRADATION; AZO; BIODEGRADATION; MINERALIZATION; TRANSFORMATION; OXIDATION;

D O I：

10.1007/s12257-008-0300-4

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In the present work, we have purified veratryl alcohol oxidase (VAO) enzyme from Comamonas UVS to evaluate its potential to decolorize textile dyes. VAO was purified (13.9 fold) by an ion exchange followed by the size exclusion chromatography. Molecular weight of the VAO was estimated to be about 66 kDa by SDS-PAGE. The optimum pH and temperature of oxidase were 30A degrees C and 65A degrees C, respectively. VAO showed maximum activity with n-propanol among the various substrates (n-propanol, veratryl alcohol, L-dopa, tryptophan, etc.). Under standard assay conditions, K-m value of the enzyme was 2.5 mM towards veratrole. The enzyme activity was completely inhibited by 0.5 mM sodium azide. L-cysteine, dithiothreitol, and the metal chelator, EDTA had a slight inhibitory effect. The purified enzyme was able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 40 mu g/mL concentration. GC-MS analysis of the metabolites suggested oxidative cleavage and desulphonation of these dyes.

引用

页码：369 / 376

页数：8

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