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  • Nhan đề: Study on AA10 expression in E. coli /
Tác giả CN Vu, Van Van
Nhan đề Study on AA10 expression in E. coli / Vu Van Van, Ngo Thi Cam Nhung
Thông tin xuất bản Tp. Hồ Chí Minh : Trường Đại học Nguyễn Tất Thành, 2021
Mô tả vật lý 5 tr.
Tóm tắt The 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.
Từ khóa tự do Polysaccharide monooxygenase
Từ khóa tự do E. coli
Từ khóa tự do AA10
Từ khóa tự do Expression
Từ khóa tự do GbpA
Tác giả(bs) CN Ngo, Thi Cam Nhung
Nguồn trích Tạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành 2021tr. 01-05 Số: 14
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100 |aVu, Van Van
245 |aStudy on AA10 expression in E. coli / |cVu Van Van, Ngo Thi Cam Nhung
260 |aTp. Hồ Chí Minh : |bTrường Đại học Nguyễn Tất Thành, |c2021
300 |a5 tr.
520 |aThe 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.
653 |aPolysaccharide monooxygenase
653 |aE. coli
653 |aAA10
653 |aExpression
653 |aGbpA
690 |aViện Kỹ thuật Công nghệ cao NTT
700 |aNgo, Thi Cam Nhung
773 |tTạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành |d2021|gtr. 01-05|x2615-9015|i14
890|a0|b0|c1|d12
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