First crenarchaeal chitinase found in Sulfolobus tokodaii

Staufenberger, Tim, Imhoff, Johannes F. and Labes, Antje (2012) First crenarchaeal chitinase found in Sulfolobus tokodaii Microbiological Research, 167 (5). pp. 262-269. DOI 10.1016/j.micres.2011.11.001.

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Abstract

This is the first description of a functional chitinase gene within the crenarchaeotes. Here we report of the heterologues expression of the ORF BAB65950 from Sulfolobus tokodaii in E. coli. The resulting protein degraded chitin and was hence classified as chitinase (EC 3.2.4.14). The protein characterization revealed a specific activity of 75 mU/mg using colloidal chitin as substrate. The optimal activity of the enzyme was measured at pH 2.5 and 70 °C, respectively. A dimeric enzyme configuration is proposed. According to amino acid sequence similarities chitinases are attributed to the two glycoside hydrolase families 18 and 19. The derived amino acid sequence of the S. tokodaii gene differed from sequences of these two glycoside hydrolase families. However, within a phylogenetic tree of protein sequences, the crenarchaeal sequence of S. tokodaii clustered in close proximity to members of the glycoside hydrolase family 18.

Document Type: Article
Keywords: Microbiology; Chitinase; Glycoside hydrolase; Crenarchaea; Protein overexpression; Chitinase; Glycoside hydrolase; Crenarchaea; Protein overexpression
Research affiliation: OceanRep > GEOMAR > FB3 Marine Ecology > FB3-MI Marine Microbiology
OceanRep > GEOMAR > Applied R&D > Centre for Marine Substances (KiWiZ)
Kiel University
OceanRep > The Future Ocean - Cluster of Excellence
Refereed: Yes
DOI etc.: 10.1016/j.micres.2011.11.001
ISSN: 0944-5013
Projects: KIWIZ, Future Ocean
Date Deposited: 09 Dec 2011 09:26
Last Modified: 22 Mar 2017 13:06
URI: http://eprints.uni-kiel.de/id/eprint/12897

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