Expression and Characterization of a Novel Antifungal Exo-β-1,3-glucanase from Chaetomium cupreum View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-11-16

AUTHORS

Cheng Jiang, Jinzhu Song, Hua Cong, Junzheng Zhang, Qian Yang

ABSTRACT

A novel β-1,3-glucanase gene, designated Ccglu17A, was cloned from the biological control fungus Chaetomium cupreum Ame. Its 1626-bp open reading frame encoded 541 amino acids. The corresponding amino acid sequence showed highest identity (67 %) with a glycoside hydrolase family 17 β-1,3-glucanase from Chaetomium globosum. The recombinant protein Ccglu17A was successfully expressed in Pichia pastoris, and the enzyme was purified to homogeneity with 10.1-fold purification and 47.8 % recovery yield. The protein’s molecular mass was approximately 65 kDa, and its maximum activity appeared at pH 5.0 and temperature 45 °C. Heavy metal ions Fe2+, Mn2+, Cu2+, Co2+, Ag+, and Hg2+ had inhibitory effects on Ccglu17A, but Ba2+ promoted the enzyme’s activity. Ccglu17A exhibited high substrate specificity, almost exclusively catalyzing β-1,3-glycosidic bond cleavage in various polysaccharoses to liberate glucose. The enzyme had a Km of 2.84 mg/mL and Vmax of 10.7 μmol glucose/min/mg protein for laminarin degradation under optimal conditions. Ccglu17A was an exoglucanase with transglycosylation activity based on its hydrolytic properties. It showed potential antifungal activity with a degradative effect on cell walls and inhibitory action against the germination of pathogenic fungus. In conclusion, Ccglu17A is the first functional exo-1,3-β-glucanase to be identified from C. cupreum and has potential applicability in industry and agriculture. More... »

PAGES

261-275

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12010-016-2325-z

DOI

http://dx.doi.org/10.1007/s12010-016-2325-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1023035322

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27854040


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