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Characterization and decolorization ability of a laccase from Panus rudis

Paper ID Volume ID Publish Year Pages File Format Full-Text
18756 42741 2006 6 PDF Available
Title
Characterization and decolorization ability of a laccase from Panus rudis
Abstract

A laccase from Panus rudis was produced constitutively in defined shaken liquid culture without induction. The purified enzyme of 58 kDa contained 8% carbohydrate and had an isoelectric point of 3.5. The optimal pH of the enzyme is 3.5 and the optimal temperature is 60 °C with ABTS as the substrate. The Km of ABTS is 0.10 mM. The first 20 residues at the amino terminus were determined and the cDNA sequence encoding the enzyme was isolated by RT-PCR. The highest identity of the predicted amino acid sequence is 67% with the sequence of laccase from Lentinula edodes. The enzyme had excellent ability to decolorize anthraquinone dye (Acid Green 27) without any redox mediators, as well as azo and indigo dyes (Acid Violet 7 and Indigo Carmine) mediated by ABTS. Compared with other laccases in dyes decolorization, a very small amount of PrL could lead to effective dyes decolorization.

Keywords
ABTS, 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid); LeL, laccase from Lentinula edodes; PrL, laccase from Panus rudis; TvL, laccase from Trametes versicolorLaccase; Panus rudis; Characterization; Decolorization; cDNA
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Characterization and decolorization ability of a laccase from Panus rudis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 1, 1 June 2006, Pages 92–97
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us