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Breeding of better beta-D-xylosidase.

Zuo, Peijun.

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Breeding of better beta-D-xylosidase.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Breeding of better beta-D-xylosidase./
作者:	Zuo, Peijun.
面頁冊數:	212 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5337.
Contained By:	Dissertation Abstracts International64-11B.
標題:	Biology, Genetics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3113432
ISBN:	0496609254

Breeding of better beta-D-xylosidase.
Zuo, Peijun.

Breeding of better beta-D-xylosidase. - 212 p.

Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5337.

Thesis (Ph.D.)--The Chinese University of Hong Kong (People's Republic of China), 2004.

Xylan, the second most abundant renewable resource, is the major constituent of hemicellulose in plant cell walls. The complete degradation of xylan by microorganisms requires the concerted action of several enzymes. Two of these enzymes endoxylanase (EC 3.2.1.8) and beta-xylosidase (EC 3.2.1.37) participate in the breakdown of the main chain of the polymer. Endoxylanase randomly cleaves the internal beta-1,4-xylosidic linkages. beta-Xylosidase hydrolyses the resulting xylo-oligosaccharides from the non-reducing end to xylose. beta-Xylosidase can be used to improve the nutritional value of animal feeds.

ISBN: 0496609254Subjects--Topical Terms:

1017730
Biology, Genetics.

Breeding of better beta-D-xylosidase.
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502 $a Thesis (Ph.D.)--The Chinese University of Hong Kong (People's Republic of China), 2004.
520 $a Xylan, the second most abundant renewable resource, is the major constituent of hemicellulose in plant cell walls. The complete degradation of xylan by microorganisms requires the concerted action of several enzymes. Two of these enzymes endoxylanase (EC 3.2.1.8) and beta-xylosidase (EC 3.2.1.37) participate in the breakdown of the main chain of the polymer. Endoxylanase randomly cleaves the internal beta-1,4-xylosidic linkages. beta-Xylosidase hydrolyses the resulting xylo-oligosaccharides from the non-reducing end to xylose. beta-Xylosidase can be used to improve the nutritional value of animal feeds.
520 $a A wide variation in the level of the expression of beta-xylosidases from different origins in E. coli was observed. Of the twelve beta-xylosidase genes cloned and expressed under the same E. coli lac promoter, Selenomonas ruminarntium Xsa beta-xylosidase showed highest expression and constitutes up to 70% of total soluble proteins in the cell, Bacillus halodurans xynB and Clostridium acetobutylicum xynD varied in their expression and the rest of the clones produce less than 1% of the total cellular proteins. Lac operator like sequences, CreA repressor binding site or rare codons in the coding regions of the beta-xylosidase genes may interfere with their expression.
520 $a A high throughput assay for beta-D-xylosidase activity has been established and used to screen for clones of higher enzyme activities and better thermostability. A number of beta-D-xylosidase variants with higher activity and thermostability were identified after screening libraries of random mutants. These mutants will be valuable genetic materials for delineate amino acid residues responsible for the improvement.
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