Gene cloning and heterologous expression of glycoside hydrolase family 55 beta-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium

Biotechnology Letters
Rie KawaiMasahiro Samejima

Abstract

The basidiomycete Phanerochaete chrysosporium produces several beta-1,3-glucanases when grown on laminarin, a beta-1,3/1,6-glucan, as the sole carbon source. To characterize one of the major unknown beta-1, 3-glucanases with a molecular mass of 83 kDa, identification, cloning, and heterologous over-expression were carried out using the total genomic information of P. chrysosporium. The cDNA encoding this enzyme included an ORF of 2337 bp and the deduced amino acid sequence contains a predicted signal peptide of 26 amino acids and the mature protein of 752 amino acids. The amino acid sequence showed a significant similarity with glycoside hydrolase family 55 enzymes from filamentous fungi and was named Lam55A. Since the recombinant Lam55A expressed in the methylotrophic yeast Pichia pastoris degraded branched beta-1,3/1,6-glucan as well as linear beta-1,3-glucan, the kinetic features of the enzyme were compared with those of other beta-1,3-glucanases.

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Citations

Apr 21, 2009·Applied and Environmental Microbiology·Amber Vanden WymelenbergDan Cullen
Jun 19, 2013·Applied and Environmental Microbiology·Karl-Magnus AnderssonAnders Tunlid
Jun 26, 2007·Bioscience, Biotechnology, and Biochemistry·Katsuichiro OkazakiShigeru Hayakawa
Sep 7, 2014·Biotechnology Advances·Katerina ZelenaRalf G Berger
Nov 18, 2016·Applied Biochemistry and Biotechnology·Cheng JiangQian Yang
Mar 11, 2015·The Journal of Biological Chemistry·Christopher M BianchettiBrian G Fox
Mar 26, 2021·Marine Biotechnology·Ashok S Jagtap, Cathrine S Manohar

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