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Purification and characterization of alginate lyase extracted from marine bacteria / Nawal Magdy Mohamed ; Supervised Zeinat Kamel Mohamed , Mohamed Gamal Salah Faraht

By: Contributor(s): Material type: TextTextLanguage: English Publication details: Cairo : Nawal Magdy Mohamed , 2021Description: 119, (45) P. : charts , facimiles ; 25cmOther title:
  • تنقية وتوصيف ألجينات لاييز المستخلص من البكتيريا البحرية [Added title page title]
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Dissertation note: Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Microbiology Summary: Alginate lyase-producing bacteria were isolated from brown algae collected from the Red Sea, Egypt. The isolated strains were subjected to molecular characterization and phylogenetic analysis. The alginate lyase gene from Cobetia litoralis P65a was cloned and over-expressed in Escherichia coli as a soluble and functional protein. The recombinant enzyme (Alg-P65a) was purified to homogeneity by Ni-NTA affinity chromatography yielding a single distinct band with an apparent molecular mass of 36 kDa on SDS-PAGE.The optimum temperature and pH values for Alg-P65a were 45 {u00B0}C and 8, respectively. Alg-P65a has an ability to hydrolyze sodium alginate, polymannuronic acid (polyM), and poly-guluronic acid (polyG) indicating that it is a bifunctional alginate lyase. The purified enzyme exhibited antibiofilm activity against Pseudomonas aeruginosa, in vitro. Furthermore, alginate-hydrolysates produced by Alg-P65a showed promising antioxidant properties.These results suggest the great potential of alginate lyase from C. litoralis P65a to be employed in biotechnological fields
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Thesis Thesis قاعة الرسائل الجامعية - الدور الاول المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.18.Ph.D.2021.Na.P (Browse shelf(Opens below)) Not for loan 01010110083560000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.18.Ph.D.2021.Na.P (Browse shelf(Opens below)) 83560.CD Not for loan 01020110083560000

Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Microbiology

Alginate lyase-producing bacteria were isolated from brown algae collected from the Red Sea, Egypt. The isolated strains were subjected to molecular characterization and phylogenetic analysis. The alginate lyase gene from Cobetia litoralis P65a was cloned and over-expressed in Escherichia coli as a soluble and functional protein. The recombinant enzyme (Alg-P65a) was purified to homogeneity by Ni-NTA affinity chromatography yielding a single distinct band with an apparent molecular mass of 36 kDa on SDS-PAGE.The optimum temperature and pH values for Alg-P65a were 45 {u00B0}C and 8, respectively. Alg-P65a has an ability to hydrolyze sodium alginate, polymannuronic acid (polyM), and poly-guluronic acid (polyG) indicating that it is a bifunctional alginate lyase. The purified enzyme exhibited antibiofilm activity against Pseudomonas aeruginosa, in vitro. Furthermore, alginate-hydrolysates produced by Alg-P65a showed promising antioxidant properties.These results suggest the great potential of alginate lyase from C. litoralis P65a to be employed in biotechnological fields

Issued also as CD

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