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Characterization of pectate lyase produced by Pseudomonas marginalis and cloning of pectate lyase genes

Characterization of pectate lyase produced by Pseudomonas marginalis and cloning of pectate lyase genes

Physiological and Molecular Plant Pathology 46(2): 109-119

ISSN/ISBN: 0885-5765

DOI: 10.1006/pmpp.1995.1009

Pseudomonas marginalis produced two pectate lyase isozymes in a medium containing sodium polypectate. Of the two, one had alkaline pI, 9.5, and the other had neutral pI, 7.0. Extracellular pectate lyase secretion started during mid-log phase and reached a maximum during the stationary phase of growth. Pectate lyase production was improved by the addition of 1 mM CaCl-2 which also enhanced the extracellular secretion in the medium containing glucose as carbon source. Ca-2+ facilitated the utilization of polygalacturonic acid as carbon source. Pectate lyase (pel) genes were cloned in pUC18 vector. One pel clone (pME1) containing a 7.7 kb BamHI fragment coded for both alkaline and neutral isozymes. A restriction map was constructed for the plasmid pME1. pel genes were sub-cloned from plasmid pME1. Sub-cloning and restriction mapping indicated that a 2.3 kb PstI-BamH1 fragment coded for one isozyme and a 2.8 kb Pst1 fragment coded for another isozyme; these two genes were separated by 2.6 kb. Southern hybridization analysis indicated that P. marginalis pel genes are homologous with Erwinia pel genes. Escherichia coli containing pel genes efficiently macerated potato tuber tissue.

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Accession: 002577419

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