Biodecolorization and Biodegradation of Azo Dye Reactive Orange-16 by Marine Sp

Overview

Journal Iran J Biotechnol

Specialty Biotechnology

Date 2020 Mar 21

PMID 32195279

Citations 5

Authors

Vaibhavi Chittal

Magaly Gracias

Anagha Anu

Purbasha Saha

K V Bhaskara Rao

Affiliations

Soon will be listed here.

Abstract

Background: Azo dyes are xenobiotic compounds that have bioaccumulated in the environment due to escalated industrial development. These are hazardous in nature, possessing carcinogenic and mutagenic effects on human beings.

Objectives: The perspective of the present study was to isolate and to determine azo dye (Reactive Orange-16) degrading potential of marine actinobacteria isolated from sediment samples of Port Blair, India.

Material And Methods: Actinobacteria with dye decolorization potential were isolated from sea sediment samples. The actinobacterial isolate with the highest dye decolorizing percentage was identified with the help of phenotypic, biochemical and molecular studies. The different physico-chemical parameters for dye decolorization were also optimized. The nature of decolorization by the potent isolate was determined with the help of High Performance Liquid chromatography (HPLC) and Fourier Transformed Infrared spectroscopy (FTIR) techniques. Further the toxicity of RO-16 decolorized products was investigated with the help of phytotoxcity assay.

Results: Out of six actinobacterial isolates, VITVAMB 1 possessed the most efficient RO-16 decolorization property. It decolorized 85.6% of RO-16 (250 mg L) within 24hrs. Isolate VITVAMB 1 was identified to be sp. Maximum dye decolorization occurred at pH 8, temperature 35°C, 3% salt concentration and a dye concentration of 50 mg L.

Conclusions: The nature of decolorization by sp. was biodegradation. Additionally, the degraded dye metabolites were found to be less toxic than pure dye. The high decolorization potential of VITVAMB 1 and the low toxicity of its degradation products make it a prospective dye removal system. The marine origin of VITVAMB 1 also makes it an attractive source for novel azo dye reducing enzymes.

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