Immobilisation of Enzimes

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Immobilization of enzymes is one of promising methods in enzymes performances enhancement, such as stability, recovery, and reusability. However, investigation of suitable solid support in enzyme immobilization is still the one of problems to prevent the reduction of enzymes activity. Polyethersulfone (PES) and aminated PES (PES-NH2) as novel materials for the immobilization were successfully synthesized. Structure of synthesized polymers were characterized by NMR, FTIR, and MALDI-TOF. The membranes based on PES and PES-NH2 with various pore sizes (from 10 to 600 nm) was fabricated to be applied as bioreactor to increase the immobilized lipase performances. The influences of pore sizes, concentration of additives, and the presence of functional groups on PES backbone toward enzyme loading and enzyme activities were studied. The largest enzyme loading was obtained by the immobilization of Mucor miehei onto PES-NH2 membrane composed of 10% of PES-NH2, 8% of DBP, and 5% of PEG (872.62 g/cm2). Activity of immobilized lipase was determined by hydrolysis reaction of pNPA and methanol to produce pNP which showed the hydrolysis reaction catalyzed by immobilized lipase onto synthesized PES (10%) membrane represented the highest enzyme activity value (568.48 mmol pNP min-1 cm-2). From the reusability test, the immobilized lipase onto PES-NH2 showed better constancy than the immobilized lipase onto PES by four times of reactions which indicated that this novel material is potential to be developed as bioreactor on enzymatic reaction. Keywords: Aminated PES, solid support, Mucor miehei, enzymatic reaction, lipase immobilization 1. Introduction Lipase, also known as triacylglycerol ester hydrolase (EC3.1.1.3), is one of inter... ... middle of paper ... ...ovic, Appl. Microbiol. Biotechol. 49 (1998), 267-271. [23] L. Giorno, E. Drioli, TIBTECH 18 (2000) 339-349. [24] S.C. Stamatoglou and J.M. Keller, The Journal of Cell Biology, 96 (1983) 1820-1823. [25] M.G.Wolf, M. Hoefling, C.A. Santamaria, H. Grupmuller, G. Groenhof, Journal of Computational Chem. 31 (2010) 2169-2174 [26] T. Tosa, T. Mori, N. Fuse, I. Chibata, Biotechnology and Bioengineering. 9 (1967) 603-615 [27] L.A. Nelson, T.A. Foglia, W.N. Marmer, JAOCS, 73 (1996) 1191-1195. [28] G. Pozinak, B. Krajewska, and W. Trochimczuk, Biomaterials, 16 (1995) 129-134. [29] M.T. Sho, F. R. Eirich, H. Strathmann, and R. W. Baker, Journal of Polymer Science: Polymer Letters Edition, 11 (1973) 201-205. [30] D.S. Marsman, NTP Toxicity Report, 30 (1995) 5-93. [31] N. Handayani, N. Miletic, K. Loos, S. Achmad, and D. Wahyuningrum, Sains Malaysiana, 40 (2011) 965-972.
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