Immobilisation of Enzimes Essay -- Chemistry

Immobilization of enzymes is iodin of promising methods in enzymes performances enhancement, such as stability, recovery, and reusability. However, investigation of suitable impregnable 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 refreshful 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 make to be applied as bioreactor to increase the immobilized lipase performances. The influences of pore sizes, concentration of additives, and the figurehead 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, an d 5% of marijuana cigarette (872.62 g/cm2). Activity of immobilized lipase was determined by hydrolysis reaction of pNPA and methanol to incur pNP which showed the hydrolysis reaction catalyzed by immobilized lipase onto synthesized PES (10%) membrane represented the highest enzyme activity repute (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.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 diary of Cell Biology, 96 (1983) 1820-1823.25 M.G.Wolf, M. Hoe fling, 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 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.