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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मुख्य लेखक: Sim, Pei Fang
स्वरूप: थीसिस
भाषा:अंग्रेज़ी
प्रकाशित: 2017
विषय:
ऑनलाइन पहुंच:http://eprints.usm.my/47783/
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author Sim, Pei Fang
author_facet Sim, Pei Fang
author_sort Sim, Pei Fang
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
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spelling usm-477832020-10-27T02:17:07Z http://eprints.usm.my/47783/ Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2 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 NonPeerReviewed application/pdf en http://eprints.usm.my/47783/1/FUNCTIONAL%20AND%20STRUCTURAL%20STUDIES%20OF%20ALGINATE%20LYASE%20FROM%20Persicobacter%20sp.%20CCB-QB2.pdf%20cut.pdf Sim, Pei Fang (2017) Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2. Masters thesis, Universiti Sains Malaysia.
spellingShingle QD1-999 Chemistry
Sim, Pei Fang
Functional And Structural Studies Of Alginate Lyase From Persicobacter sp. CCB-QB2
title 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_short 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
topic QD1-999 Chemistry
url http://eprints.usm.my/47783/
work_keys_str_mv AT simpeifang functionalandstructuralstudiesofalginatelyasefrompersicobacterspccbqb2