α-Chitinase activity among lactic acid bacteria

• Published in: Systematic and applied microbiology Vol. 31; no. 2; pp. 151 - 156
• Main Authors: Leisner, Jørgen J., Vogensen, Finn K., Kollmann, Johannes, Aideh, Bashir, Vandamme, Peter, Vancanneyt, Marc, Ingmer, Hanne
• Format: Journal Article
• Language: English
• Published: München Elsevier GmbH 01.06.2008; Elsevier
• Subjects: Bacteriology; Biological and medical sciences; Carnobacterium; Carnobacterium divergens; Carnobacterium maltaromaticum; Chitin; chitinase; Chitinases - metabolism; enzyme activity; Enzyme Repression; food microbiology; Fundamental and applied biological sciences. Psychology; Glucose - metabolism; Gram-positive bacteria; Gram-Positive Bacteria - enzymology; Gram-Positive Bacteria - isolation & purification; Gram-Positive Bacteria - metabolism; Hydrolytic activity; Invertebrates; lactic acid bacteria; Lactococcus; Metabolism. Enzymes; Microbiology; Natural environment; ponds; Sphagnum; Sphagnum fallax; Temperature; Water Microbiology; Carnobacterium; Natural environment; Chitin; Hydrolytic activity; Invertebrates; Lactococcus; Chitinase; Lactic acid bacteria; Enzyme; Glycosylases; Streptococcaceae; Enzymatic activity; Glycosidases; Bacteria; Hydrolases; Micrococcales; Invertebrata
• ISSN: 0723-2020; 1618-0984
• DOI: 10.1016/j.syapm.2008.03.003

Chitin is a polysaccharide widely distributed in nature. Among 115 strains from 29 species of lactic acid bacteria only strains belonging to Carnobacterium divergens and Carnobacterium maltaromaticum hydrolyzed α-chitin. This activity was not affected by temperature (10 °C versus 30 °C) and in most cases not subject to glucose catabolite repression.