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Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica

Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica The cDNA encoding for lignin peroxidase of Phanerochaete chrysosporium was expressed in the Pichia methanolica under the control of the alcohol oxidase (AUG1) promoter which was followed by either the lignin peroxidase leader peptide of Phanerochaete chrysosporium or the Saccharomyces cerevisiaeα-factor signal peptide. Both peptides efficiently directed the secretion of lignin peroxidase from the recombinant yeast cell. The extracellular lignin peroxidase activity in two recombinants was 932 U l−1 and 1933 U l−1. The purity of the recombinant product was confirmed by SDS-PAGE. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Letters Springer Journals

Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica

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References (13)

Publisher
Springer Journals
Copyright
Copyright © 2004 by Kluwer Academic Publishers
Subject
Life Sciences; Biotechnology; Organic Chemistry; Biochemistry, general; Microbiology; Animal Anatomy / Morphology / Histology
ISSN
0141-5492
eISSN
1573-6776
DOI
10.1023/B:BILE.0000045654.66689.b4
pmid
15604798
Publisher site
See Article on Publisher Site

Abstract

The cDNA encoding for lignin peroxidase of Phanerochaete chrysosporium was expressed in the Pichia methanolica under the control of the alcohol oxidase (AUG1) promoter which was followed by either the lignin peroxidase leader peptide of Phanerochaete chrysosporium or the Saccharomyces cerevisiaeα-factor signal peptide. Both peptides efficiently directed the secretion of lignin peroxidase from the recombinant yeast cell. The extracellular lignin peroxidase activity in two recombinants was 932 U l−1 and 1933 U l−1. The purity of the recombinant product was confirmed by SDS-PAGE.

Journal

Biotechnology LettersSpringer Journals

Published: Nov 3, 2004

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