Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2
AlyQ gene from Persicobacter sp.CCB-QB2encodes alginate lyase which is comprised of two carbohydrate-bindingdomains, domains A and B,at the N-terminus of the alginate lyase domain, domain C. Alginate lyase domain from AlyQ belongs to the polysaccharide lyase 7 (PL7) family, while the first domain of...
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my-usm-ep.477832020-10-27T02:17:07Z Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 2017-11 Sim, Pei Fang QD1-999 Chemistry AlyQ gene from Persicobacter sp.CCB-QB2encodes alginate lyase which is comprised of two carbohydrate-bindingdomains, domains A and B,at the N-terminus of the alginate lyase domain, domain C. Alginate lyase domain from AlyQ belongs to the polysaccharide lyase 7 (PL7) family, while the first domain of the carbohydrate-bindingmodule resembles carbohydrate-bindingmodule 16 (CBM 16), and the second domain a CBM 32. Previous studies had mainly focused on activity characterization of alginate lyase or carbohydrate-binding modules individually but rarely on studies of the enzyme characteristics after combining these two domains and even less on the structural studies between alginate lyase and CBM domains. Therefore, this study focused on the alginate lyase enzymatic activity differences with or without the inclusion of the two carbohydrate-bindingdomains, and to elucidate the structural relationship between carbohydrate-bindingdomains and alginate lyase 2017-11 Thesis http://eprints.usm.my/47783/ http://eprints.usm.my/47783/1/FUNCTIONAL%20AND%20STRUCTURAL%20STUDIES%20OF%20ALGINATE%20LYASE%20FROM%20Persicobacter%20sp.%20CCB-QB2.pdf%20cut.pdf application/pdf en public masters Universiti Sains Malaysia Pusat Pengajian Sains Kimia (School of Chemistry) |
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QD1-999 Chemistry |
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QD1-999 Chemistry Sim, Pei Fang Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 |
description |
AlyQ gene from Persicobacter sp.CCB-QB2encodes alginate lyase which is comprised of two carbohydrate-bindingdomains, domains A and B,at the N-terminus of the alginate lyase domain, domain C. Alginate lyase domain from AlyQ belongs to the polysaccharide lyase 7 (PL7) family, while the first domain of the carbohydrate-bindingmodule resembles carbohydrate-bindingmodule 16 (CBM 16), and the second domain a CBM 32. Previous studies had mainly focused on activity characterization of alginate lyase or carbohydrate-binding modules individually but rarely on studies of the enzyme characteristics after combining these two domains and even less on the structural studies between alginate lyase and CBM domains. Therefore, this study focused on the alginate lyase enzymatic activity differences with or without the inclusion of the two carbohydrate-bindingdomains, and to elucidate the structural relationship between carbohydrate-bindingdomains and alginate lyase |
format |
Thesis |
qualification_level |
Master's degree |
author |
Sim, Pei Fang |
author_facet |
Sim, Pei Fang |
author_sort |
Sim, Pei Fang |
title |
Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 |
title_short |
Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 |
title_full |
Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 |
title_fullStr |
Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 |
title_full_unstemmed |
Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 |
title_sort |
functional and structural studies of alginate lyase from persicobacter sp. ccb-qb2 |
granting_institution |
Universiti Sains Malaysia |
granting_department |
Pusat Pengajian Sains Kimia (School of Chemistry) |
publishDate |
2017 |
url |
http://eprints.usm.my/47783/1/FUNCTIONAL%20AND%20STRUCTURAL%20STUDIES%20OF%20ALGINATE%20LYASE%20FROM%20Persicobacter%20sp.%20CCB-QB2.pdf%20cut.pdf |
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