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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.
Mei Chow Yen,Ti Tey Beng,Ibrahim Mohammad Nordin,Ariff Arbakariya,Chuan Ling Tau The Korean Society for Biotechnology and Bioengine 2005 Biotechnology and Bioprocess Engineering Vol.10 No.3
The adsorption of a model protein bovine serum albumin (BSA) in expanded bed chromatography was undertaken by exploiting a commercially available expanded bed column (20 mm i.d.) from UpFront Chromatography and Streamline DEAE $(\rho=1.2g/cm^3)$ from Amersham Pharmacia Biotechnology. The influence of whole yeast cells on the adsorption capacity of column was explored by employing yeast cells in a concentration ranged of 0 to $15\%(w/v)$. Equilibrium isotherms for adsorption of BSA on Streamline DEAE were correlated by using Langmuir equation. The presence of yeast cells resulted in decreased of BSA binding capacity in both batch binding and expanded bed chromatography. Results indicated that the yeast cells act as competitor for proteins to bind to the sites on adsorbents.
Mei Chow Yen,Ti Tey Beng,Ibrahim Mohammad Nordin,Ariff Arbakariya,Chuan Ling Tau The Korean Society for Biotechnology and Bioengine 2005 Biotechnology and Bioprocess Engineering Vol.10 No.3
Baker's yeast was disrupted in a 1.4-L stainless steel horizontal bead mill under a continuous recycle mode using 0.3 mm diameter zirconia beads as abrasive. A single pass in continuous mode bead mill operation liberates half of the maximally released protein. The maximum total protein release can only be achieved after passaging the cells 5 times through the disruption chamber. The degree of cell disruption was increased with the increase in feeding rate, but the total protein release was highest at the middle range of feeding rate (45 L/h). The total protein release was increased with an increase in biomass concentration from 10 to $50\%$(w/v). However, higher heat dissipation as a result of high viscosity of concentrated biomass led to the denaturation of labile protein such as glucose 6-phosphate dehydrogenase (G6PDH). As a result the highest specific activity of G6PDH was achieved at biomass concentration of $20\%$(ww/v). Generally, the degree of cell disruption and total protein released were increased with an increase in impeller tip speed, but the specific activity of G6PDH was decreased substantially at higher impeller tip speed (14 m/s). Both the degree of cell disruption and total protein release increased, as the bead loading increased from 75 to $85\% (v/v)$. Hence, in order to obtain a higher yield of labile protein such as G6PDH, the yeast cell should not be disrupted at biomass concentration and impeller tip speed higher than $20\%(w/v)$ and 10 m/s, 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).
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).
Ling Tau Chuan,Chow Yen Mei,Tey Beng Ti,Mohammad Nordin Ibrahim,Arbakariya Ariff 한국생물공학회 2005 Biotechnology and Bioprocess Engineering Vol.10 No.3
The adsorption of a model protein bovine serum albumin (BSA) in expanded bed chromatography was undertaken by exploiting a commercially available expanded bed column (20 mm i.d.) from UpFront Chromatography and Streamline DEAE ( = 1.2 g/cm3) from Amersham Pharmacia Biotechnology. The influence of whole yeast cells on the adsorption capacity of column was explored by employing yeast cells in a concentration ranged of 0 to 15% (w/v). Equilibrium isotherms for adsorption of BSA on Streamline DEAE were correlated by using Langmuir equation. The presence of yeast cells resulted in decreased of BSA binding capacity in both batch binding and expanded bed chromatography. Results indicated that the yeast cells act as competitor for proteins to bind to the sites on adsorbents.
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.
Ling Tau Chuan,Chow Yen Mei,Tey Beng Ti,Mohammad Nordin Ibrahim,Arbakariya Ariff 한국생물공학회 2005 Biotechnology and Bioprocess Engineering Vol.10 No.3
Bakers yeast was disrupted in a 1.4-L stainless steel horizontal bead mill under a continuous recycle mode using 0.3 mm diameter zirconia beads as abrasive. A single pass in continuous mode bead mill operation liberates half of the maximally released protein. The maximum total protein release can only be achieved after passaging the cells 5 times through the disruption chamber. The degree of cell disruption was increased with the increase in feeding rate, but the total protein release was highest at the middle range of feeding rate (45 L/h). The total protein release was increased with an increase in biomass concentration from 10 to 50% (w/v). However, higher heat dissipation as a result of high viscosity of concentrated biomass led to the denaturation of labile protein such as glucose 6-phosphate dehydrogenase (G6PDH). As a result the highest specific activity of G6PDH was achieved at biomass concentration of 20% (ww/v). Generally, the degree of cell disruption and total protein released were increased with an increase in impeller tip speed, but the specific activity of G6PDH was decreased substantially at higher impeller tip speed (14 m/s). Both the degree of cell disruption and total protein release increased, as the bead loading increased from 75 to 85% (v/v). Hence, in order to obtain a higher yield of labile protein such as G6PDH, the yeast cell should not be disrupted at biomass concentration and impeller tip speed higher than 20% (w/v) and 10 m/s, respectively.