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Team:WLC-Milwaukee/Cellulases
From 2014.igem.org
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[1] Lindner, Stulke, Hecker. (1994) Regulation of xylanolytic enzymes in Bacillus subtilis. Microbiology 140, 753-757. </ br> | [1] Lindner, Stulke, Hecker. (1994) Regulation of xylanolytic enzymes in Bacillus subtilis. Microbiology 140, 753-757. </ br> | ||
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Revision as of 17:05, 17 October 2014
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Our team selected three cellulases to begin the breakdown of cellulose: yesZ, bglS, and xynA.
xynA
XynA is a endo-1,4-beta xylanase or is referred to as beta xylanase. It catalyzes the hydrolysis of the xylan main chain in hemicellulose. Xylan is abundant in the cell wall structures of many plants. Lindner [1] investigated the regulation of xylanase within Bacillus subtilis. It was found that Bacillus subtitis had a slow rate of growth on xylan plates and did not grow on xylose plates. It was also found that the synthesis of xynA is not dependent on the environment, but instead was found to be highly synthesized during the exponential growth phase. {{This is a potential advantage to our project because the probiotic may not have time to reach the stationary phase in the ruminant.}} The presence of glucose also showed to have no effect on the presence of the mRNA sequence for xynA. It is now known that xynA has “glucose resistant synthesis”. This differs from most extracellular catabolic enzymes. Lindner also found that xynA is synthesized constitutively; meaning it is produced in constant amounts regardless of the surrounding environment of the bacterial cell.
bglS
Written by: Sierra Tackett
