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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001 | 35116 |
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002 | 9 |
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004 | 7B84C608-3B0B-433C-806E-E032EFB9E606 |
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005 | 202201191140 |
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008 | 081223s2021 vm| vie |
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009 | 1 0 |
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039 | |y20220119114003|zngantk |
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100 | |aVu, Van Van |
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245 | |aStudy on AA10 expression in E. coli / |cVu Van Van, Ngo Thi Cam Nhung |
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260 | |aTp. Hồ Chí Minh : |bTrường Đại học Nguyễn Tất Thành, |c2021 |
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300 | |a5 tr. |
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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. |
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653 | |aPolysaccharide monooxygenase |
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653 | |aE. coli |
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653 | |aAA10 |
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653 | |aExpression |
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653 | |aGbpA |
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690 | |aViện Kỹ thuật Công nghệ cao NTT |
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700 | |aNgo, Thi Cam Nhung |
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773 | |tTạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành |d2021|gtr. 01-05|x2615-9015|i14 |
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890 | |a0|b0|c1|d12 |
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