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Chow, Yen Mei,Tey, Beng Ti,Ibrahim, Mohd Nordin,Ariff, Arbakariya,Ling, Tae Chuan The Korean Society for Biotechnology and Bioengine 2006 Biotechnology and Bioprocess Engineering Vol.11 No.3
A dense, pellicular UpFront adsorbent ($p=1.5 g/cm^3$, UpFront Chromatography, Cophenhagen, Denmark) was characterized in terms of hydrodynamic properties and protein adsorption performance in expanded bed chromatography. Cibacron Blue 3GA was immobilised into the adsorbent and protein adsorption of bovine serum albumin (BSA) was selected to test the setup. The Bodenstein number and axial dispersion coefficient estimated for this dense pellicular adsorbent was 54 and $1.63{\times}10^{-5}m^2/s$, respectively, indicating a stable expanded bed. It could be shown that the BSA protein was captured by the adsorbent in the presence of 30% (w/v) of whole-yeast cells with an estimated dynamic binding capacity $(C/C_o = 0.01)$ of approximately 6.5 mg/mL adsorbent.
Beng Ti Tey,Yen Mei Chow,Mohd Nordin Ibrahim,Arbakariya Ariff,Tau Chuan Ling 한국생물공학회 2006 Biotechnology and Bioprocess Engineering Vol.11 No.5
The bed stability of Streamline DEAE (ρ = 1.2 g/mL) in a 20 mm (i.d.) glass expanded bed contactor, and its performance on the recovery of glucose 6-phosphate dehydrogenase (G6PDH) from unclarified yeast homogenate were investigated. A residence time distribution study showed that a stable expanded bed was achieved. The theoretical plate and Bodenstein numbers determined were 25 and 53, respectively. A recovery yield of 87% and purification factor of 4.1 were achieved in the operation using 5% (w/v) biomass concentration feedstock. The performance of the anion exchange EBAC was still considerable good at a biomass concentration as high as 15% (w/v).
Chow, Yen Mei,Tey, Beng Ti,Ibrahim, Mohd Nordin,Ariff, Arbakariya,Ling, Tau Chuan The Korean Society for Biotechnology and Bioengine 2005 Biotechnology and Bioprocess Engineering Vol.10 No.6
The influence of whole yeast cells $(0{\sim}15%\;w/v)$ on the protein adsorption performance in dye-ligand chromatography was explored. The adsorption of a model protein, bovine serum albumin (BSA), was selected to demonstrate this approach. The UpFront adsorbent $(p=1.5\;g/cm^3)$ derivatised with Cibacron Blue 3GA and a commercially available expanded bed column (20 mm i.d.) from UpFront Chromatography, Denmark, were employed in the batch binding and expanded bed operation. The BSA binding capacity was demonstrated to not be adversely affected by the presence of yeast cells. The dynamic binding capacity of BSA at a $C/C_0=0.1$ biomass concentration of 5, 10, 15% w/v were 9, 8, and 7.5mg/mL of settled adsorbent, respectively.
Chow, Yen Mei,Tey, Beng Ti,Ibrahim, Mohd Nordin,Ariff, Arbakariya,Ling, Tau Chuan The Korean Society for Biotechnology and Bioengine 2006 Biotechnology and Bioprocess Engineering Vol.11 No.5
The bed stability of Streamline DEAE (p = 1.2 g/mL) in a 20mm (i.d.) glass expanded bed contactor, and its performance on the recovery of glucose 6-phosphate dehydrogenase (G6PDH) from unclarified yeast homogenate were investigated. A residence time distribution study showed that a stable expanded bed was achieved. The theoretical plate and Bodenstein numbers determined were 25 and 53, respectively. A recovery yield of 87% and purification factor of 4.1 were achieved in the operation using 5% (w/v) biomass concentration feedstock. The performance of the anion exchange EBAC was still considerable good at a biomass concentration as high as 15% (w/v).
Chong, Fui Chin,Tey, Beng Ti,Dom, Zanariah Mohd,Cheong, Kok Hing,Satiawihardja, Budiatman,Ibrahim, Mohd Nordin,Rahman, Russly Abdul,Biak, Dayang Radiah Awang,Ling, Tau Chuan Korean Society for Biotechnology and Bioengineerin 2007 Biotechnology and Bioprocess Engineering Vol.12 No.3
Rice bran lipase (RBL) was delipidated to enhance its stability in organic solvent and its esterification activity at elevated temperature. The esterification activity of delipidated RBL increased as temperature was increased from 45 to $65^{\circ}C$. The esterification activity of delipidated RBL at $65^{\circ}C$ was about 14 times greater than that of the non-delipidated RBL. As temperature was further increased to $75^{\circ}C$, the non-delipidated RBL lost all esterification activity, whereas the delipidated RBL retained approximately 48% of its esterification activity. The delipidated RBL maintained a relative esterification activity greater than 80% after 16 h of incubation in hexane, whereas the non-delipidated RBL maintained a relative esterification activity of only 50%. A method for production of acylglycerol using delipidated RBL to esterify palm oil fatty acid distillate (PFAD) with glycerol in hexane was successfully developed. The effects of reaction temperatures and type of water removal agents (silica gel and molecular sieve) on the degree of esterification were also examined. A 4 h reaction at $65^{\circ}C$, catalyzed by delipidated RBL and using silica gel as the water removal agent resulted in 53.8% esterification. Thin layer chromatography analysis suggested that the esterified product was primarily comprised of mono- and di-acylglycerols.
Tau Chuan Ling,Yen Mei Chow,Beng Ti Tey,Mohd Nordin Ibrahim,Arbakariya Ariff 한국생물공학회 2005 Biotechnology and Bioprocess Engineering Vol.10 No.6
The influence of whole yeast cells (0~15% w/v) on the protein adsorption performance in dye-ligand chromatography was explored. The adsorption of a model protein, bovine serum albumin (BSA), was selected to demonstrate this approach. The UpFront adsorbent (ρ = 1.5 g/cm3) derivatised with Cibacron Blue 3GA and a commercially available expanded bed column (20 mm i.d.) from UpFront Chromatography, Denmark, were employed in the batch binding and expanded bed operation. The BSA binding capacity was demonstrated to not be adversely affected by the presence of yeast cells. The dy-namic binding capacity of BSA at a C/C0 = 0.1 biomass concentration of 5, 10, 15% w/v were 9, 8, and 7.5 mg/mL of settled adsorbent, respectively.
Tau Chuan Ling,Yen Mei Chow,Beng Ti Tey,Mohd Nordin Ibrahim,Arbakariya Ariff 한국생물공학회 2006 Biotechnology and Bioprocess Engineering Vol.11 No.3
A dense, pellicular UpFront adsorbent (ρ = 1.5 g/cm3, UpFront Chromatography, Cophenhagen, Denmark) was characterized in terms of hydrodynamic properties and protein adsorption performance in expanded bed chromatography. Cibacron Blue 3GA was immobilised into the adsorbent and protein adsorption of bovine serum albumin (BSA) was selected to test the setup. The Bodenstein number and axial dispersion coefficient estimated for this dense pellicular adsorbent was 54 and 1.63 × 10-5 m2/s, respectively, indicating a stable expanded bed. It could be shown that the BSA protein was captured by the adsorbent in the presence of 30% (w/v) of whole-yeast cells with an estimated dynamic binding capacity (C/Co = 0.01) of approximately 6.5 mg/mL adsorbent.