Title: A novel family 19 chitinase from the marine-derived Pseudoalteromonas tunicata CCUG 44952T: Heterologous expression, characterization and antifungal activity
Abstract: The Ptchi19 gene of the marine Pseudoalteromonas tunicata CCUG 44952T was cloned and expressed in Escherichia coli. The recombinant chitinase PtChi19p of 483 amino acids has a molecular weight of 53.5 kDa and a multi-domain structure characteristic of family 19 chitinases. The relevant constituents of this multi-domain structure are the domain (D132–A155) where the active site is located, and the domain (A437–W479) that includes a C-terminal carbohydrate-binding module 5. The purified protein was active in the temperature range of 20–50 °C and at pH values of 6–9.5, maintaining a high stability under suboptimal conditions and in the presence of different metal ions. The recombinant enzyme hydrolyzed colloidal and crystalline chitin, as well as p-NP N-acetyl-β-d-glucosaminide. As PtChi19p exhibited antifungal activity against phytopathogenic and human pathogenic fungi, it could be used as an alternative biofungicide.
Publication Year: 2015
Publication Date: 2015-01-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 55
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