Immobilisation of Enzimes Essay -- Chemistry

Immobilization of enzymes is maven of burnished methods in enzymes performances enhancement, such as stability, recovery, and reusability. However, investigation of suitable unassailable carry in enzyme immobilizing is still the one of problems to prevent the reduction of enzymes activity. Polyethersulfone (fundament) and aminated PES (PES-NH2) as novel strongs for the immobilization were successfully synthesized. Structure of synthesized polymers were characterized by NMR, FTIR, and MALDI-TOF. The membranes base 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 practicable 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 reception 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 give away 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.IntroductionLipase, also known as triacylglycerol ester hydrolase (EC3.1.1.3), is one of inter... ...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) 2169-217426 T. Tosa, T. Mori, N. Fuse, I. Chibata, Biotechnology and Bioengineering. 9 (1967) 603-61527 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 acquisition 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.