Study on AA10 expression in E. coli

dc.contributor.authorVu, Van Van
dc.contributor.authorNgo, Thi Cam Nhung
dc.date.accessioned2024-08-23T07:01:31Z
dc.date.available2024-08-23T07:01:31Z
dc.date.issued2021
dc.description5 p.
dc.description.abstractThe GlcNAc-binding protein A (GbpA) has been known as a virulent factor of Vibrio vulnificus pathogen. Domain 1 of GbpA adhesion takes responsibility of binding both human intestine and the chitinous surface. The domain 1 structure is similar to a polysaccharide monooxygenase (PMO) AA10-type (PMO), which catalyzed oxidation toward the recalcitrant chitin polymer. The role of the VvPMO10 module in catalytic functions has not been fulfilled characterized. To aim of the VvPMO10 study, this protein was cloned to the pET22b system and transformed into the E. coli BL21 (DE3) strain. The recombinant enzyme was expressed at 37 0C with IPTG induced. Total protein was checked by SDS-PAGE method and stained using Coomassie blue solution. The target band showed a band of 20 kDa as expectation. Thus, the heterologous protein was expressed successfully in E. coli BL21 (DE3) strain and becomes the materials for future study.
dc.identifier.citationNguyen Tat Thanh University. (2021). Journal of Science and Technology - NTTU, Issue 14. ISSN 2615-9015.
dc.identifier.issn2615-9015
dc.identifier.urihttps://oerrepository.ntt.edu.vn/handle/298300331/199
dc.language.isoen
dc.publisherTrường Đại học Nguyễn Tất Thành
dc.relation.ispartofseriesJournal of Science and Technology - NTTU; Issue 14
dc.subjectAA10
dc.subjectE. coli
dc.subjectExpression
dc.subjectGbpA
dc.subjectPolysaccharide monooxygenase
dc.subjectProtein
dc.subjectMầm bệnh
dc.subjectVirut
dc.titleStudy on AA10 expression in E. coli
dc.typeArticle
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