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The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase

Paper ID Volume ID Publish Year Pages File Format Full-Text
17450 42669 2009 7 PDF Available
Title
The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase
Abstract

Protein glycosylation, a major post-translational modification, plays essential roles in eukaryotic cells. The glycosylation of fungal laccases has been proposed to be the bottleneck for the heterologous production of the enzyme, so it is important to determine its structure and function. We describe here the detailed N-glycosylation profile of Pycnoporus sanguineus laccase and its influence on some of its enzymatic properties. In this enzyme only high mannose structures were found, being those with 5- and 8-mannose units the most abundant. No other type of sugars was found in contrast to other fungal laccases. Enzymatic cleavage of the N-glycans present in the laccase provoked slight changes in the kinetic parameters, in the thermal stability and in the pH optimum of the enzyme.

Keywords
N-Glycosylation; Enzymatic activity; Laccase; Pycnoporus sanguineus
First Page Preview
The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 45, Issue 3, 7 September 2009, Pages 233–239
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering