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Team:WLC-Milwaukee/Cellulases
From 2014.igem.org
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Our team selected three cellulases to begin the breakdown of cellulose: yesZ, bglS, and xynA. | Our team selected three cellulases to begin the breakdown of cellulose: yesZ, bglS, and xynA. | ||
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| - | <h2>xynA</h2> | + | <h2>Enzyme xynA</h2> |
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| - | + | The enzyme 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 <i>Bacillus subtilis</i>. It was found that <i>Bacillus subtitis</i> 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. | |
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| - | <h2>bglS</h2> | + | <h2>Enzyme bglS</h2> |
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| - | + | The enzyme bglS hydrolyzes linked beta-D-glucans, which are commonly found in lichen. Beta-D-glucans are 5.5% of dry weight in grains, and 75% of carbohydrates in barley endospores. [2] They showed bglS to have an optimum pH of 6.0 and temperature of 50 degrees Celsius. | |
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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> | ||
| + | [2] Furtado, Ribeiro, Santos, Tonoli, et al. (2011) Biochemical and structural characterization of a -1,3–1,4-glucanase from Bacillus subtilis 168. Process Biochemistry 46, 1202-1206.</ br> | ||
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Revision as of 19:08, 17 October 2014
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Our team selected three cellulases to begin the breakdown of cellulose: yesZ, bglS, and xynA.
Enzyme xynA
The enzyme 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.
Enzyme bglS
The enzyme bglS hydrolyzes linked beta-D-glucans, which are commonly found in lichen. Beta-D-glucans are 5.5% of dry weight in grains, and 75% of carbohydrates in barley endospores. [2] They showed bglS to have an optimum pH of 6.0 and temperature of 50 degrees Celsius.
Written by: Sierra Tackett
