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      저자 : Syazana Mohamad Pauzi (검색결과 2 건)
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        Immobilization of Alcohol Dehydrogenase in Membrane: Fouling Mechanism at Different Transmembrane Pressure

        Fauziah Marpani,Muhammad Kiflain Zulkifli,Farazatul Harnani Ismail,Syazana Mohamad Pauzi 대한화학회 2019 대한화학회지 Vol.63 No.4

        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 (CH3OH) 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.

      • SCOPUSKCI등재

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

        Marpani, Fauziah,Zulkifli, Muhammad Kiflain,Ismail, Farazatul Harnani,Pauzi, Syazana Mohamad Korean Chemical Society 2019 대한화학회지 Vol.63 No.4

        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.

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