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Applied and Environmental Microbiology, November 2005, p. 7559-7561, Vol. 71, No. 11
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.11.7559-7561.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Putative Exposed Aromatic and Hydroxyl Residues on the Surface of the N-Terminal Domains of Chi1 from Aeromonas caviae CB101 Are Essential for Chitin Binding and Hydrolysis

Qiang Li,1,2,{dagger} Fengping Wang,2,{dagger} Ying Zhou,2 and Xiang Xiao2*

School of Life Science, Xiamen University, Xiamen, People's Republic of China,1 Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen, People's Republic of China2

Received 18 April 2005/ Accepted 6 June 2005

Chitinase Chi1 of Aeromonas caviae CB101 possesses chitin binding sites at both its N and C termini. Four putative exposed residues aligned in a line on the surface of the N-terminal domains of Chi1 were found to contribute to the enzyme-chitin binding and hydrolysis via site-directed mutagenesis. Also, it was found that Chi1 requires the cooperation of the N- and C-terminal domains to bind fully with crystalline and colloidal chitin.

* Corresponding author. Mailing address: Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen, People's Republic of China. Phone: 86-592-2195236. Fax: 86-592-2085376. E-mail: xxwfp{at}public.xm.fj.cn.

{dagger} Q.L. and F.W. contributed equally to this paper.

Applied and Environmental Microbiology, November 2005, p. 7559-7561, Vol. 71, No. 11
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.11.7559-7561.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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