期刊
BIOCHEMICAL ENGINEERING JOURNAL
卷 93, 期 -, 页码 84-93出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bej.2014.09.014
关键词
Pseudoalteromonas tunicata; Family 19 glycosyl hydrolase; Enzyme biocatalysis; Recombinant DNA; Purification; Enzyme activity
资金
- Xunta de Galicia-Campus do Mar
- University of Vigo
- [10PXIB310278PR]
The Ptchi19 gene of the marine Pseudoatteromonas 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 (D-132-A(155)) where the active site is located, and the domain (A(437)-W-479) that includes a C-terminal carbohydrate-binding module 5. The purified protein was active in the temperature range of 20-50 degrees 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-beta-D-glucosaminide. As PtChi19p exhibited antifungal activity against phytopathogenic and human pathogenic fungi, it could be used as an alternative biofungicide. (C) 2014 Elsevier B.V. All rights reserved.
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