All Title Author
Keywords Abstract

Publish in OALib Journal
ISSN: 2333-9721
APC: Only $99

ViewsDownloads

Relative Articles

Properties of a triphenylmethane dyes decolorization enzyme TpmD from Aeromonas hydrophila strain DN322
细菌脱色酶TpmD对三苯基甲烷类染料脱色的酶学特性研究

Over-expression of Highly Active Triphenylmethane Dyes Decolorization Enzyme (TpmD) Induced by Lactose Instead of IPTG in Escherichia coli BL21 (DE3)
乳糖替代IPTG诱导脱色酶TpmD基因在大肠杆菌中的高效表达

Non-induced expression of the gene for triphenylmethane dye oxidase (tpmD) in E.coli
三苯基甲烷类染料氧化酶基因(tpmD)在大肠杆菌中的无诱导表达

Effects of organic solvents and inhibitors on the decolorization activity of TpmD expressed in Pichia Pastoris
有机溶剂和抑制剂对毕赤酵母表达TpmD酶活性影响

三苯基甲烷类染料氧化酶基因(tpmD)在大肠杆菌中的无诱导表达

Physical, Thermal and Spectroscopical Characterization of Biofield Treated Triphenylmethane: An Impact of Biofield Treatment

Recent Advances in Microbial Decolorization of Triphenylmethane Dyes
微生物对三苯基甲烷类染料脱色的研究进展

Spectrophotometric determination of fluoride in drinking water using aluminium complexes of triphenylmethane dyes

Tungstate ion resonance Rayleigh scattering method for determination of basic triphenylmethane dyes

Study on Decolorization of Triphenylmethane Dyes by DTT
DTT对三苯基甲烷染料脱色的研究

More...

Properties of a triphenylmethane dyes decolorization enzyme (TpmD) from Aeromonas hydrophila strain DN322
细菌脱色酶TpmD的酶学特性研究

Keywords: Decolorization enzyme,Aeromonas hydrophila,Enzymological properties
脱色酶
,三苯基甲烷类染料,酶学特性

Full-Text   Cite this paper   Add to My Lib

Abstract:

A novel bacterial enzyme for decolorization of triphenylmethane dyes from Aeromonas hydrophila strain DN322 was purified and named TpmD.The basic properties of this enzyme including molecular weight,isoelectric point Km as well as the optimum temperature and pH were determined and the enzyme was identified as an NADH/NADPH-dependent oxygenase in previous research.Based on previous results,the effect of different inhibitor including Vc,metyrapone,rotenone,antimycin A and NaN-3 as well as the effect of FAD and FMN on the activity of TpmD were measured.The results indicated that the activity of the decolorization enzyme was inhibited by Vc and metyrapone in a concentration-dependent manner,but wasn't inhibited by rotenone,antimycin A and NaN-3.The activity of the decolorization enzyme was not enhanced by addition of FAD or FMN.The solution of the enzyme protein displayed only a single peak at 408nm in the Soret region,a characteristic peak of porphyrin,but did not show the characteristic peak of the cytochrome P450 proteins at 450nm in sodium dithionite(DTN)-reduced enzyme solution after treatment with carbon monoxide.The amino acid sequence of N-terminal of TpmD provided further evidence that the enzyme is an oxygenase.All these results suggest that decolorization enzyme TpmD is a new hemo-containing oxygenase.The decolorization enzyme would be a good material for further research of the enzymological mechanism of triphenylmethane dyes decolorization by bacteria.

Full-Text

comments powered by Disqus