fulltext.study @t Gmail

Activation of laccase by penicillin and derivatives

Paper ID Volume ID Publish Year Pages File Format Full-Text
36063 45119 2006 5 PDF Available
Title
Activation of laccase by penicillin and derivatives
Abstract

Capable of oxidizing a wide range of reducing substances, laccase has a great potential for various biocatalytic applications. Extensive research effort is being made for improving laccase's activity, specificity, and stability. We observed that pre-incubating with penicillin led to a significant activation of a Rhizoctonia solani laccase, although penicillin was not a redox substrate of the enzyme. The activation impacted mainly the kcat of the laccase, and the effect was optimal at pH 5. Ampicillin and penicilloic acid were also active on the laccase (although their effect were weaker than that of penicillin), but 6-aminopenicillanic acid, phenylacetic acid, and cephalexin were not active. The apparent effect from penicillin was attributed to a non-redox interaction with the polypeptide backbone of the laccase. The effect was significantly weaker on Myceliophthora thermophila and Trametes villosa laccases.

Keywords
Laccase; Penicillin; Activator; Rhizoctonia solani
First Page Preview
Activation of laccase by penicillin and derivatives
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
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 9, September 2006, Pages 2082–2086
Authors
, ,
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