Biochemical characterization and relative expression levels of multiple carbohydrate esterases of the xylanolytic rumen bacterium Prevotella ruminicola 23 grown on an ester-enriched substrate

Kabel, Mirjam A., Yeoman, Carl J., Han, Yejun, Dodd, Dylan, Abbas, Charles A., de Bont, Jan A. M., Morrison, Mark, Cann, Isaac K. O. and Mackie, Roderick I. (2011) Biochemical characterization and relative expression levels of multiple carbohydrate esterases of the xylanolytic rumen bacterium Prevotella ruminicola 23 grown on an ester-enriched substrate. Applied and Environmental Microbiology, 77 16: 5671-5681. doi:10.1128/AEM.05321-11

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Author Kabel, Mirjam A.
Yeoman, Carl J.
Han, Yejun
Dodd, Dylan
Abbas, Charles A.
de Bont, Jan A. M.
Morrison, Mark
Cann, Isaac K. O.
Mackie, Roderick I.
Title Biochemical characterization and relative expression levels of multiple carbohydrate esterases of the xylanolytic rumen bacterium Prevotella ruminicola 23 grown on an ester-enriched substrate
Journal name Applied and Environmental Microbiology   Check publisher's open access policy
ISSN 0099-2240
1098-5336
Publication date 2011-01-01
Year available 2011
Sub-type Article (original research)
DOI 10.1128/AEM.05321-11
Open Access Status File (Publisher version)
Volume 77
Issue 16
Start page 5671
End page 5681
Total pages 11
Place of publication Washington, DC United States
Publisher American Society for Microbiology
Language eng
Subject 2402 Applied Microbiology and Biotechnology
1106 Human Movement and Sports Science
1305 Biotechnology
2303 Ecology
Abstract We measured expression and used biochemical characterization of multiple carbohydrate esterases by the xylanolytic rumen bacterium Prevotella ruminicola 23 grown on an ester-enriched substrate to gain insight into the carbohydrate esterase activities of this hemicellulolytic rumen bacterium. The P. ruminicola 23 genome contains 16 genes predicted to encode carbohydrate esterase activity, and based on microarray data, four of these were upregulated >2-fold at the transcriptional level during growth on an ester-enriched oligosaccharide (XOS FA,Ac) from corn relative to a nonesterified fraction of corn oligosaccharides (AXOS). Four of the 16 esterases (Xyn10D-Fae1A, Axe1-6A, AxeA1, and Axe7A), including the two most highly induced esterases (Xyn10D-Fae1A and Axe1-6A), were heterologously expressed in Escherichia coli, purified, and biochemically characterized. All four enzymes showed the highest activity at physiologically relevant pH (6 to 7) and temperature (30 to 40°C) ranges. The P. ruminicola 23 Xyn10D-Fae1A (a carbohydrate esterase [CE] family 1 enzyme) released ferulic acid from methylferulate, wheat bran, corn fiber, and XOS FA,Ac, a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters, but exhibited negligible activity on sugar acetates. As expected, the P. ruminicola Axe1-6A enzyme, which was predicted to possess two distinct esterase family domains (CE1 and CE6), released ferulic acid from the same substrates as Xyn10D-Fae1 and was also able to cleave O-acetyl ester bonds from various acetylated oligosaccharides (AcXOS). The P. ruminicola 23 AxeA1, which is not assigned to a CE family, and Axe7A (CE7) were found to be acetyl esterases that had activity toward a broad range of mostly nonpolymeric acetylated substrates along with AcXOS. All enzymes were inhibited by the proximal location of other side groups like 4-O-methylglucuronic acid, ferulic acid, or acetyl groups. The unique diversity of carbohydrate esterases in P. ruminicola 23 likely gives it the ability to hydrolyze substituents on the xylan backbone and enhances its capacity to efficiently degrade hemicellulose.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes Supplemental material (read only) - http://aem.asm.org/content/77/16/5671/suppl/DC1

Document type: Journal Article
Sub-type: Article (original research)
Collection: UQ Diamantina Institute Publications
 
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