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RISS 인기검색어
- 검색키워드
- 저자 : John Chi Wei Lan (검색결과 3 건)
- 무료
- 기관 내 무료
- 유료
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A Fermentation Strategy for Anti-MUC1 C595 Diabody Expression in Recombinant Escherichia Coli
Lan, John Chi-Wei,Ling, Tau Chuan,Hamilton, Grant,Lyddiatt, Andrew The Korean Society for Biotechnology and Bioengine 2006 Biotechnology and Bioprocess Engineering Vol.11 No.5
The development of fermentation conditions for the production of C595 diabody fragment (dbFv) in E. coli HB2151 clone has been explored. Investigations were carried out to study the effect of carbon supplements over the expression period, the comparison of C595 dbfv production in synthetic and complex media, the influence of acetic acid upon antibody production, and comparison of one-stage and two-stage processes operated at batch or fed-batch modes in bioreactor. Yeast extract supplied during expression yielded more antibody fragment than any other carbon supply. The synthetic medium presented higher specific productivity (0.066 mg dbFv $g^{-1}$ dry cell weight) when compared to the complex medium (0.044 mg dbFv $g^{-1}$ DCW). The comparison of fermentation strategies demonstrated that (1) one-stage fed-batch fermentation performed higher C595 dbFv production than that operated in batch mode which was significantly affected by acetate concentration; (2) a two-stage batch operation could enhance C595 dbFv production. It was found that a concentration of 12.3 mg $L^{-1}$ broth of C595 dbFv and a cell concentration of 10.8g $L^{-1}$ broth were achieved at the end of two-stage operation in 5-L fermentation.
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A Fermentation Strategy for Anti-MUC1 C595 Diabody Expression in Recombinant Escherichia coli
John Chi-Wei Lan,Tau Chuan Ling,Grant Hamilton,Andrew Lyddiatt 한국생물공학회 2006 Biotechnology and Bioprocess Engineering Vol.11 No.5
The development of fermentation conditions for the production of C595 diabody fragment (dbFv) in E. coli HB2151 clone has been explored. Investigations were carried out to study the effect of carbon supplements over the expression period, the comparison of C595 dbfv production in synthetic and complex media, the influence of acetic acid upon antibody production, and comparison of one-stage and two-stage processes operated at batch or fed-batch modes in bioreactor. Yeast extract supplied during expression yielded more antibody fragment than any other carbon supply. The synthetic medium presented higher specific productivity (0.066 mg dbFv g-1 dry cell weight) when compared to the complex medium (0.044 mg dbFv g-1 DCW). The comparison of fermentation strategies demonstrated that (1) one-stage fed-batch fermentation performed higher C595 dbFv production than that operated in batch mode which was significantly affected by acetate concentration; (2) a two-stage batch operation could enhance C595 dbFv production. It was found that a concentration of 12.3 mg L-1 broth of C595 dbFv and a cell concentration of 10.8 g L-1 broth were achieved at the end of two-stage operation in 5-L fermentation.
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Chien Wei Ooi,Beng Ti Tey,Siew Ling Hii,Arbakariya Ariff,Ho Shing Wu,John Chi Wei Lan,Ruey Shin Juang,Siti Mazlina Mustapa Kamal,Tau Chuan Ling 한국생물공학회 2009 Biotechnology and Bioprocess Engineering Vol.14 No.6
An aqueous two-phase purification process was employed for the recovery of Burkholderia pseudomallei from fermentation broth. The partition behavior of B.pseudmallei lipase was investigated with various parameters such as phase composition, tie-line length (TLL), volume ratio (VR), sample loading, system pH, and addition of neutral salts. Optimum conditions for the purification of lipase were obtained in polyethylene glycol (PEG) 6000-potassium phosphate system using TLL of 42.2% (w/w), with VR of 2.70, and 1% (w/w) NaCl addition at pH 7 for 20% (w/w) crude load. Based on this system, the purification factor of lipase was enhanced to 12.42 fold, with a high yield of 93%. Hence, the simplicity and effectiveness of aqueous two-phase systems (ATPS) in the purification of lipase were proven in this study An aqueous two-phase purification process was employed for the recovery of Burkholderia pseudomallei from fermentation broth. The partition behavior of B.pseudmallei lipase was investigated with various parameters such as phase composition, tie-line length (TLL), volume ratio (VR), sample loading, system pH, and addition of neutral salts. Optimum conditions for the purification of lipase were obtained in polyethylene glycol (PEG) 6000-potassium phosphate system using TLL of 42.2% (w/w), with VR of 2.70, and 1% (w/w) NaCl addition at pH 7 for 20% (w/w) crude load. Based on this system, the purification factor of lipase was enhanced to 12.42 fold, with a high yield of 93%. Hence, the simplicity and effectiveness of aqueous two-phase systems (ATPS) in the purification of lipase were proven in this study
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