Abstract
Lipase (EC 3.1.1.3) fromCandida rugosa (Syn.C.cylindmcea) was immobilized on the polyacrylamide-gel (Bio-Gel P-l0) by covalent binding. Since the substrates, triglycerides with long chained fatty acids, are insoluble in water, emulsification of the substrates is necessary for lipase to react. Emulsions containing gum arabic were prepared by homogenization followed by sonication. Tributyrin and triolein were chosen as the substrates in order to compare the reaction properties in terms of the fatty acids chain-length. Kinetics of the enzymatic hydrolysis by soluble and immobilized lipases of tributyrin and triolein have been investigated in a batch-reactor. Soluble lipase was inhibited severely by the substrate at higher concentration of substrate emulsion, whereas immobilization of lipase reduced the substrate inhibition. This was especially true for triolein. Effects of pH and temperature on the lipase were studied. Thermal stability of the lipase was increased considerably when the lipase was immobilized.
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References
Bailey, A.E.: “Bailey’s Industrial Oil and Fat Products”, John Wiley & Sons, Vol. 2, p. 97 (1982).
Lavayre, J. and Baratti, J.: Biotechnol. Bioeng.,24, 1007 (1982).
Semeriva, M. and Desunelle, P.: “Advances in Endymology”, John Wiley & Sons, Vol. 48, p. 319 (1979).
Verger, R. and Haas, G.H.:“Annual Review of Biophysics and Bioengineering”, Annual Reviews, Vol. 5, p. 97 (1976).
Brockerhoff, H., and Jensen, R.G.:“Lipolytic Enzymes”, Academic Press, p. 34 (1974).
Benzonana, G. and Desnulle, P.: Biochim. Biophys. Acta.,105, 121 (1965).
Brockman, H.L., Lee, J.H. and Kezdy, F.J.: J. Biol. Chem.,248, 4965 (1973).
Wells, M.A.: Biochem.,13, 2248 (1974).
Wells, M.A.: Biochem.,13, 4937 (1974).
Sarda, L. and Desnuelle, P.: Biochim. Biophys. Acta,30, 513 (1958).
Chapus, C. and Semeriva, M.: Biochem.15, 4988 (1976).
Yokozeki, K., Yamanaka, S., Takinami, K., Hirose, Y., Tanaka, A., Sonomoto, K. and Fukui, S.: Europ. J. Appl. Microb. Biotech.,14, 1 (1982).
Tsujisaka, Y. and Iwai, M.: Yukagaku,31, 772 (1982).
Carr, P.W. and Bowers, L.D.:“Chemical Analysis”, John Wiley & Sons, Vol. 56, p. 148 (1981).
Turkova, J.: J. Chromatography Library,12, 30 (1974).
Lieberman, R.B. and Ollis, D.F.: Biotechnol. Bioeng.,17, 1401 (1975).
Inman, J.K. & Dintzis, H.M.: Biochem.,8, 4074 (1969).
Inman, J.K.:“Methods in Enzymology”, Academic Press, Vol. 34, p. 30 (1974).
Lowry, O.H., Rosebrough, N.J., Farrand, A.L. and Randall, R.J.: J. Biol. Chem.,193, 265 (1951).
Jensen, R.G.: Lipids,18, 650 (1983).
Brockman, H.L.: “Methods in Enzymology”, Academic Press, Vol. 71, p. 619 (1981).
Çelebi, S.S., Uçar, T. and Çaglar, M.A.:“Advances in Biotechnology”, Pergamon Press, Vol. 1, p. 691 (1980).
Aiba, S., Humphrey, A.E. and Millis, N.F.:“Biochemical Engineering”, University of Tokyo Press, p. 393 (1973).
Chibata, I.:“Immobilized Enzymes”, John Wiley & Sons, p. 111 (1978).
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Kwon, D.Y., Rhee, J.S. Immobilization of lipase for fat spliting. Korean J. Chem. Eng. 1, 153–158 (1984). https://doi.org/10.1007/BF02697447
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DOI: https://doi.org/10.1007/BF02697447