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Journal of Bacteriology, March 2001, p. 2093-2100, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2093-2100.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Functional Characterization of a Novel Xylanase from a Corn Strain of Erwinia chrysanthemi†

Jason C. Hurlbert and James F. Preston III*

Institute of Food and Agricultural Sciences, Department of Microbiology & Cell Science, University of Florida, Gainesville, Florida 32611

Received 18 September 2000/Accepted 10 December 2000

A beta -1,4-xylan hydrolase (xylanase A) produced by Erwinia chrysanthemi D1 isolated from corn was analyzed with respect to its secondary structure and enzymatic function. The pH and temperature optima for the enzyme were found to be pH 6.0 and 35°C, with a secondary structure under those conditions that consists of approximately 10 to 15% alpha -helices. The enzyme was still active at temperatures higher than 40°C and at pHs of up to 9.0. The loss of enzymatic activity at temperatures above 45°C was accompanied by significant loss of secondary structure. The enzyme was most active on xylan substrates with low ratios of xylose to 4-O-methyl-D-glucuronic acid and appears to require two 4-O-methyl-D-glucuronic acid residues for substrate recognition and/or cleavage of a beta -1,4-xylosidic bond. The enzyme hydrolyzed sweetgum xylan, generating products with a 4-O-methyl-glucuronic acid-substituted xylose residue one position from the nonreducing terminus of the oligoxyloside product. No internal cleavages of the xylan backbone between substituted xylose residues were observed, giving the enzyme a unique mode of action in the hydrolysis compared to all other xylanases that have been described. Given the size of the oligoxyloside products generated by the enzyme during depolymerization of xylan substrates, the function of the enzyme may be to render substrate available for other depolymerizing enzymes instead of producing oligoxylosides for cellular metabolism and may serve to produce elicitors during the initiation of the infectious process.

* Corresponding author. Mailing address: Dept. of Microbiology and Cell Science, P.O. Box 110700, University of Florida, Gainesville, FL 32611. Phone: (352) 392-5923. Fax: (352) 392-5922. E-mail: jpreston{at}ufl.edu.

dagger Florida Agricultural Experiment Station Journal Series no. R-07770.

Journal of Bacteriology, March 2001, p. 2093-2100, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2093-2100.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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