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Thermodynamic stabled CO2 molecules can be biocatalytically reduced to methanol via three cascade dehydrogenases (formate, formaldehyde and alcohol) with the aid of cofactor as the electron donor. In this study, Alcohol dehydrogenase (EC 1.1.1.1), the third step of the cascade enzymatic reaction which catalyzed formaldehyde (CHOH) to methanol (CH3OH) will be immobilized in an ultrafiltration membrane. The enzyme will be immobilized in the support layer of a poly(ether)sulfone (PES) membrane via a technique called fouling induced enzyme immobilization. The objective of this study is to evaluate the effect of varying pH (acid (pH 5), neutral (pH 7) and alkaline (pH 9)) of the feed solution during immobilization process of ADH in the membrane in terms of permeate flux, observed rejection, enzyme loading and fouling mechanism. The experiment was conducted in a pressure driven, dead-end stirred filtration cell. Reaction conversion and biocatalytic productivity will be also evaluated. The results showed that permeate flux for acid solution were the lowest during immobilization. High concentration polarization and fouling resistance cause lower observed rejection for pH 7 and 9. Enzyme loading for pH 5 give 73.8% loading rate which is the highest compared to 62.4% at pH 7 and 70.1% at pH 9. Meanwhile, the conversion rate during the reaction shows that reaction on fouled membrane showed more than 90% conversion for pH 5 and 7. The fouling model predicted that irreversible fouling occurs during enzyme immobilization at pH 7 with standard blocking mechanism while reversible fouling occurs at pH 5 and 9 with intermediate and complete blocking, respectively. [ABSTRACT FROM AUTHOR]

Combination of the reaction simultaneously with separation inside a single process unit or commonly known as reactive separation technology is widely studied nowadays as it would give mutual benefits for both enzymatic catalysis and membrane separation process. Alcohol dehydrogenase (ADH) at 0.10 g/L (dissolved in 0.10 M Tris-HCl buffer) was immobilized on commercially available PES and PVDF membrane at pH 7 and TMP 2 bar by reverse filtration method. Then the immobilized enzyme was subjected to the biocatalytic conversion of formaldehyde to methanol. The immobilization process successfully immobilized 87.67% and 70.94% of ADH enzyme in/on the PVDF and PES membrane, respectively. The subsequent reaction was able to convert formaldehyde to methanol as high as 90% conversion and a high biocatalytic productivity of 460 µmol CH3OH/mgenzyme·h for PVDF membranes. Enzyme relative activity could be retained for at least seven consecutive cycles. This study suggested that immobilization of ADH on the polymer membrane can increase enzyme loading and also retain its activity for a simultaneous conversion and separation of formaldehyde to methanol. [ABSTRACT FROM AUTHOR]

Abstract: In this work, fouling principles in force in ultrafiltration were deployed to understand the role of selected variables—applied pressure (1–3bar), enzyme concentration (0.05–0.2gL−1), pH (5–9) and membrane properties—on fouling-induced enzyme immobilization. The immobilization and subsequent enzymatic reaction efficiency were evaluated in terms of enzyme loading, conversion rate and biocatalytic stability. Alcohol dehydrogenase (ADH) was selected as a model enzyme. Lower pressure, higher enzyme concentration and lower pH resulted in higher irreversible fouling resistance and lower permeate flux. High pH during immobilization produced increased permeate flux but declines in conversion rates, likely because of the weak immobilization resulting from strong electrostatic repulsion between enzymes and membrane. The results showed that pore blocking as a fouling mechanism permitted a higher enzyme loading but generated more permeability loss, while cake layer formation increased enzyme stability but resulted in low loading rate. Low pH (near isoelectric point) favored hydrophobic and electrostatic adsorption of enzymes on the membrane, which reduced the enzyme stability. Neutral pH, however, promoted entrapment and hydrogen bonding of enzymes on the membrane, which improved the enzyme stability. This study suggests that a compromise between different fouling/immobilization mechanisms must be found in order to maximize the immobilization performance, both in terms of enzyme loading and also of enzyme activity. [Copyright &y& Elsevier]