Document Detail


In Silico and in Vitro Physicochemical Screening of Rigidoporus sp. Crude Laccase-assisted Decolorization of Synthetic Dyes-Approaches for a Cost-effective Enzyme-based Remediation Methodology.
MedLine Citation:
PMID:  23292904     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The objective of this paper is to compare in silico data with wet lab physicochemical properties of crude laccase enzyme isolated from Rigidoporus sp. using wheat bran as solid substrate support towards dye decolorization. Molecular docking analysis of selected nine textile and non-textile dyes were performed using laccase from Rigidoporus lignosus as reference protein. Enzyme-based remediation methodology using crude enzyme enriched from solid state fermentation was applied to screen the effect of four influencing variables such as pH, temperature, dye concentration, and incubation time toward dye decolorization. The extracellular crude enzyme decolorized 69.8 % Acid Blue 113, 45.07 % Reactive Blue 19, 36.61 % Reactive Orange 122, 30.55 % Acid Red 88, 24.59 % Direct Blue 14, 18.48 % Reactive Black B, 16.49 % Reactive Blue RGB, and 11.66 % Acid Blue 9 at 100 mg/l dye concentration at their optimal pH at room temperature under static and dark conditions after 1 h of incubation without addition of any externally added mediators. Our wet lab studies approach, barring other factors, validate in silico for screening and ranking textile dyes based on their proximity to the T1 site. We are reporting for the first time a combinatorial approach involving in silico methods and wet lab-based crude laccase-mediated dye decolorization without any external mediators.
Authors:
S Sridhar; V Chinnathambi; P Arumugam; P K Suresh
Related Documents :
25040124 - Kinetic studies of a ferredoxin-dependent cyanobacterial nitrate reductase.
24586134 - Pathway thermodynamics highlights kinetic obstacles in central metabolism.
170624 - Concerning the subcellular distribution of 3beta-hydroxysteroid dehydrogenase/isomerase...
10304 - Conversion of proparathyroid hormone to parathyroid hormone by a particulate enzyme of ...
8661544 - Evaluation of extracellular, high-affinity beta-n-acetylglucosaminidase measurements fr...
3912004 - Guanosine thiophosphate derivatives as substrate analogues for phosphoenolpyruvate carb...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-6
Journal Detail:
Title:  Applied biochemistry and biotechnology     Volume:  -     ISSN:  1559-0291     ISO Abbreviation:  Appl. Biochem. Biotechnol.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8208561     Medline TA:  Appl Biochem Biotechnol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
R&D division, Bharathiar University, Coimbatore, Tamil Nadu, India.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Aldehyde Oxidase Activity and Stability in Water-Miscible Organic Solvents.
Next Document:  Physicochemical and Biochemical Profiling of Diphenyl Diselenide.