Fouling-induced enzyme immobilization is a technique to immobilize enzyme by positively manipulating the knowledge of membrane fouling. In this study, Alcohol dehydrogenase (ADH) (EC 1.1.1.1) was immobilized in the support layer of ultrafiltration PES membrane at different solution pH (acid, neutral and alkaline). ADH catalyses formaldehyde (CHOH) to methanol (CH3OH) and simultaneously oxidised nicotinamide adenine dinucleotide (NADH) to NAD+. The initial feed amount of enzyme is 3.0 mg. The objective of the study aims at the effect of different pH of feed solution during enzyme immobilization, in terms of permeate flux, observed rejection, enzyme loading and fouling mechanism. The results showed that, pH 5 holds the highest enzyme loading which is 65% while pH 7 holds the lowest at 52% out of 3.0 mg as the initial enzyme feed. The permeate flux for each pH decreased with increasing cumulative permeate volume. The observed rejection is inversely correlated with the pH where increase in pH will cause a lower observed rejection. 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.
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