STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A

碩士 === 大同大學 === 生物工程學系(所) === 97 === Cellulose is the most abundant and renewable biopolymer on Earth. Cellulose has been used for centuries; however, it's enormous potential as a renewable source of energy was recognized only after the cellulose degrading enzymes or "cellulases" had...

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Main Authors: Hsing-Ren Wang, 王興仁
Other Authors: Trong-Rong Yan
Format: Others
Language:zh-TW
Published: 2009
Online Access:http://ndltd.ncl.edu.tw/handle/38070499680139155789
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spelling ndltd-TW-097TTU051060102016-05-02T04:11:10Z http://ndltd.ncl.edu.tw/handle/38070499680139155789 STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A 黑麴菌內切型纖維素酵素B與外切型纖維素酵素A基因選殖與結構分析 Hsing-Ren Wang 王興仁 碩士 大同大學 生物工程學系(所) 97 Cellulose is the most abundant and renewable biopolymer on Earth. Cellulose has been used for centuries; however, it's enormous potential as a renewable source of energy was recognized only after the cellulose degrading enzymes or "cellulases" had been identified. Microorganisms including fungi, bacteria and actinomycetes produce mainly three types of cellulase: endoglucanase, exoglucanase and β-glucosidase. Aspergillus niger can be used in function food and pharmaceutical industrial. For the purpose of enzyme cloning, propertise enhancement, and regulation comprehension; we designed primers from known endoglucanase and cellobiohydrolase sequence and succeed in obtaining the DNA and RNA-reversed transcribed cDNA sequence of A. niger endoglucanase and cellobiohydrolase. The endoglucanase B cloned genomic sequence revealed a 1,217 bp open reading frame with 5 introns and 6 exons. The cDNA showed a 996 bp sequence encoding an 331 amino acid protein that belongs to glycosyl hydrolase family 5. The full length of cellobiohydrolase A is 1,512 bp. Its cDNA shows 1,359 bp. There are 3 intron in the cbhA gene. The CBHA belongs of glycosyl hydrolase 7. Trong-Rong Yan 顏聰榮 2009 學位論文 ; thesis 81 zh-TW
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language zh-TW
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sources NDLTD
description 碩士 === 大同大學 === 生物工程學系(所) === 97 === Cellulose is the most abundant and renewable biopolymer on Earth. Cellulose has been used for centuries; however, it's enormous potential as a renewable source of energy was recognized only after the cellulose degrading enzymes or "cellulases" had been identified. Microorganisms including fungi, bacteria and actinomycetes produce mainly three types of cellulase: endoglucanase, exoglucanase and β-glucosidase. Aspergillus niger can be used in function food and pharmaceutical industrial. For the purpose of enzyme cloning, propertise enhancement, and regulation comprehension; we designed primers from known endoglucanase and cellobiohydrolase sequence and succeed in obtaining the DNA and RNA-reversed transcribed cDNA sequence of A. niger endoglucanase and cellobiohydrolase. The endoglucanase B cloned genomic sequence revealed a 1,217 bp open reading frame with 5 introns and 6 exons. The cDNA showed a 996 bp sequence encoding an 331 amino acid protein that belongs to glycosyl hydrolase family 5. The full length of cellobiohydrolase A is 1,512 bp. Its cDNA shows 1,359 bp. There are 3 intron in the cbhA gene. The CBHA belongs of glycosyl hydrolase 7.
author2 Trong-Rong Yan
author_facet Trong-Rong Yan
Hsing-Ren Wang
王興仁
author Hsing-Ren Wang
王興仁
spellingShingle Hsing-Ren Wang
王興仁
STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A
author_sort Hsing-Ren Wang
title STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A
title_short STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A
title_full STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A
title_fullStr STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A
title_full_unstemmed STRUCTRURE GENE ANALYSIS OF ASPERGILLUS NIGER ENDOGLUCANASE B AND CELLUBIOHYDROLASE A
title_sort structrure gene analysis of aspergillus niger endoglucanase b and cellubiohydrolase a
publishDate 2009
url http://ndltd.ncl.edu.tw/handle/38070499680139155789
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