NDLI: Cloning, expression, and characterization of a highly thermostable family 18 chitinase from Rhodothermus marinus

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Cloning, expression, and characterization of a highly thermostable family 18 chitinase from Rhodothermus marinus

Content Provider	Springer Nature Link
Author	Hobel, Cédric F. V. Hreggvidsson, Gudmundur Ó. Marteinsson, Viggó T. Bahrani Mougeot, Farah Einarsson, Jón M. Kristjánsson, Jakob K.
Copyright Year	2004
Abstract	A family 18 chitinase gene chiA from the thermophile Rhodothermus marinus was cloned and expressed in Escherichia coli. The gene consisted of an open reading frame of 1,131 nucleotides encoding a protein of 377 amino acids with a calculated molecular weight of 42,341 Da. The deduced ChiA was a non-modular enzyme with one unique glycoside hydrolase family 18 catalytic domain. The catalytic domain exhibited 43% amino acid identity with Bacillus circulans chitinase C. Due to poor expression of ChiA, a signal peptide-lacking mutant, chiAΔsp, was designed and used subsequently. The optimal temperature and pH for chitinase activity of both ChiA and ChiAΔsp were 70°C and 4.5–5, respectively. The enzyme maintained 100% activity after 16 h incubation at 70°C, with half-lives of 3 h at 90°C and 45 min at 95°C. Results of activity measurements with chromogenic substrates, thin-layer chromatography, and viscosity measurements demonstrated that the chitinase is an endoacting enzyme releasing chitobiose as a major end product, although it acted as an exochitobiohydrolase with chitin oligomers shorter than five residues. The enzyme was fully inhibited by 5 mM HgCl2, but excess ethylenediamine tetraacetic acid relieved completely the inhibition. The enzyme hydrolyzed 73% deacetylated chitosan, offering an attractive alternative for enzymatic production of chitooligosaccharides at high temperature and low pH. Our results show that the R. marinus chitinase is the most thermostable family 18 chitinase isolated from Bacteria so far.
Starting Page	53
Ending Page	64
Page Count	12
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	9
Issue Number	1
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-10-02
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cloning Expression Family 18 chitinase Highly thermostable Rhodothermus marinus Thin layer chromatography Viscosity measurements
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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