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Immobilization of Alcohol Dehydrogenase in Membrane: Fouling Mechanism at Different Transmembrane Pressure

Marpani, Fauziah;Zulkifli, Muhammad Kiflain;Ismail, Farazatul Harnani;Pauzi, Syazana Mohamad

  • Received : 2019.02.19
  • Accepted : 2019.04.20
  • Published : 2019.08.20

Abstract

Alcohol dehydrogenase (ADH) (EC 1.1.1.1) was selected as the enzyme which will be immobilized on ultrafiltration membrane by fouling with different transmembrane pressure of 1, 2 and 3 bars. ADH will catalyze formaldehyde (CHOH) to methanol ($CH_3OH$) and simultaneously oxidized nicotinamide adenine dinucleotide (NADH) to $NAD^+$. The concentration of enzyme and pH are fixed at 0.1 mg/ml and pH 7.0 respectively. The objective of the study focuses on the effect of different transmembrane pressure (TMP) on enzyme immobilization in term of permeate flux, observed rejection, enzyme loading and fouling mechanism. The results showed that at 1 bar holds the lowest enzyme loading which is 1.085 mg while 2 bar holds the highest enzyme loading which is 1.357 mg out of 3.0 mg as the initial enzyme feed. The permeate flux for each TMP decreased with increasing cumulative permeate volume. The observed rejection is linearly correlated with the TMP where increase in TMP will cause a higher observed rejection. Hermia model predicted that at irreversible fouling with standard blocking dominates at TMP of 3 bar, while cake layer and intermediate blocking dominates at 1 and 2 bar respectively.

Keywords

Biocatalysis;Enzyme immobilization;Membrane bioreactor;Reactive separation;Ultrafiltration