NDLI: Rapid decolorization of azo dyes by crude manganese peroxidase from Schizophyllum sp. F17 in solid-state fermentation

Content Provider	Springer Nature Link
Author	Yao, Juntao Jia, Rong Zheng, Leilei Wang, Bangxing
Copyright Year	2013
Abstract	The production of ligninolytic enzymes by the fungus Schizophyllum sp. F17 using a cost-effective medium comprised of agro-industrial residues in solid-state fermentation (SSF) was optimized. The maximum activities of the enzymes manganese peroxidase (MnP), laccase (Lac), and lignin peroxidases (LiP) were 1,200, 586, and 109 U/L, respectively, on day 5 of SSF. In vitro decolorization of three structurally different azo dyes by the extracellular enzymes was monitored to determine its decolorization capability. The results indicated that crude MnP, but not LiP and Lac, played a crucial role in the decolorization of azo dyes. After optimization of the dye decolorization system with crude MnP, the decolorization rates of Orange IV and Orange G, at an initial dye concentration of 50 mg/L, were enhanced to 76 and 57%, respectively, after 20 min of reaction at pH 4 and 35°C. However, only 8% decolorization of Congo red was observed. This enzymatic reaction system revealed a rapid decolorization of azo dyes with a low MnP activity of 24 U/L. Thus, this study could be the basis for the production and application of MnP on a larger scale using a low-cost substrate.
Starting Page	868
Ending Page	877
Page Count	10
File Format	PDF
ISSN	12268372
Journal	Biotechnology and Bioprocess Engineering
Volume Number	18
Issue Number	5
e-ISSN	19763816
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2013-10-23
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	decolorization azo dye manganese peroxidase Schizophyllum sp. F17 Biotechnology Industrial and Production Engineering
Content Type	Text
Resource Type	Article
Subject	Bioengineering Biomedical Engineering Applied Microbiology and Biotechnology Biotechnology

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