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Optimization of culture conditions to express AA9 Polysaccharide monooxygenases AN3860 in Escherichia coli / Ngo Thi Cam Nhung, Le Quynh Loan, Vu Van Van // Tạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành . - 2022. - tr. 36-43. - ISSN: 2615-9015
Ký hiệu phân loại (DDC): 615
Lignocellulose biomass is a copious source for second generation biomaterial production. The participant of Polysaccharide monooxygenases enzyme (PMO) in the reactions which convert lignocellulose biomass into monosaccharides enhances the activity and improve the efficiency of hydrolysis of hydrolase enzymes on lignocellulose substrate. Enzyme AN3860, obtained from Aspergillus nidulans strain belonging to AA9 PMO, is expected to catalyze flexibly at C1 and C4 carbon positions of β-glycosidic linkage. As an enzyme with high potential of improving cellulose crystals hydrolysis capacity, AN3860 was successfully cloned into the expression system of E. coli BL21 (DE3) strain. In this study, the culture process of recombinant strain with AN3680 gene is optimized to increase the target proteins yield, thus ensure the outcome of purification process, and save production cost. The results demonstrate that the E. coli recombinant strains grow sufficiently in TB (Terrific Broth) culture media and the highest yield of AN3680 protein achieved when the concentration of Isopropyl β-D-1- thiogalactopyranoside (IPTG) is 0.05 mM and the temperature of the reaction is 30 0C at 150 rpm. After 6 hours of induction, the biomass reaches 500 mg/L and the yield of AN3860 account for (7-10) % total protein generated. The recombinant AN3860 protein is later harvested on larger scale and purified by Ni-NTA column chromatography method for analysis of bioactivities on lignocellulose substrates in the future.
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Situation of microbiological contamination in bottled drinking water products and some in uencing factors in Hau Giang province in 2020 / Vo Thi Thuy Loan, Tran Thi Tuyet Hanh // Tạp chí Khoa học Nghiên cứu Sức khỏe và Phát triển : Journal of Health and Development Studies- JHDS . - 2021. - p. 47-60. - ISSN: 2588-1442
Ký hiệu phân loại (DDC): 570
Bottled drinking water has become popular for consumption by customers. Bottled drinking water with pathogenic microbiological contamination is a public health concern. This study aimed to describe the current situation of microbiological contamination in bottled drinking water products, food safety conditions and some in uencing factors in production facilities in Hau Giang province in 2020. A cross-sectional study has been conducted in 2020 using quantitative and qualitative methods. The evaluation was carried out at 54 bottled drinking water production facilities, 108 workers/owners and 54 samples collected from facilities for microbiological analysis in the province. In-depth interviews were conducted with local government o cials on food safety, two owners of facilities and two workers. The quality of bottled drinking water in Hau Giang province was not good. The important factors a ecting the contaminated bottled drinking water products were identi ed. We recommend that: management agencies should frequently conduct sudden inspections and supervisions of facilities with no ensured food safety and strictly handle according to regulations. Owners of bottled water facilities should voluntarily comply with food safety. This study is particularly concerned with ensuring food safety conditions in the production of bottled drinking water to prevent products from microbiological contamination.
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Study on AA10 expression in E. coli / Vu Van Van, Ngo Thi Cam Nhung // Tạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành . - 2021. - tr. 01-05. - ISSN: 2615-9015
Tp. Hồ Chí Minh : Trường Đại học Nguyễn Tất Thành, 2021
5 tr.
Ký hiệu phân loại (DDC):
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.
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