Studies on the Stability of Lipase from Candida Cylindracea, Free and Incorporated in Polymerisable Zwitterionic Surfactant Vesicles

References

• Ahern T. J., Klibanov A. M. The mechanism of irreversible enzyme inactivation at 100°C. Science 1985; 228: 1280–1284
   PubMed Web of Science ®Google Scholar
• Lipases, B. Borgström, H. L. Brockman. Elsevier, Amsterdam 1984; 527
   Google Scholar
• Brady L., Brzozowski A. M., Derewenda Z. S., Dodson E., Dodson G., Tolley S., et al. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 1991; 343: 767–770
   Google Scholar
• Brzozowski A. M., Derewenda U., Derewenda Z. S., Dodson G. G., Lawson D. M., Turkenburg J. P., et al. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 1991; 351: 491–494
   PubMed Web of Science ®Google Scholar
• Dawson R. M. C., Elliott D. C., Elliott W. H., Jones K. M. Data for biochemical research. 3rd edn. Oxford University Press, Oxford 1991; 580
   Google Scholar
• Derewenda U., Brzozowski A. M., Lawson D. M., Derewenda Z. S. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry 1992; 31: 1532–1541
   PubMed Web of Science ®Google Scholar
• Devaux D. F., Seigneuret M. Specificity of lipid-protein interactions as determined by spectroscopic techniques. Biochim. Biophys. Acta 1985; 822: 63–125
   PubMedGoogle Scholar
• Dini L., Di Giulio A., Pavan A., Ravagnan G., Mossa G. Size and stability of dipalmitoylphosphatidylcholine/cholesterol unilamellar vesicles are affected by interaction with proteins. Biochim, Biophys. Acta 1991; 1062(1)108–112
   PubMedGoogle Scholar
• Dziezak J. D. Enzyme modification of dairy products. Food Technol 1986; 40(4)114–120
   Google Scholar
• Eytan G. A. Use of liposomes for reconstitution of biological functions. Biochim. Biophys. Acta 1982; 694: 185–202
   PubMed Web of Science ®Google Scholar
• Fendler J. H. Membrane Mimetic Chemistry. John Wiley & Sons, New York 1982
   Google Scholar
• Fendler J. H. Membrane mimetic systems that contain catalysts, semiconductors and magnets. Chemtech 1985; 15: 686–691
   Google Scholar
• Freeman A. Understanding enzyme stabilization. Trends Biotechnol 1984; 2: 147–148
   Google Scholar
• Liposome Technology, G. Gregoriadis. Boca CRC Press, Raton 1984; Vol. 1, (Preparation of liposomes)
   Google Scholar
• Gregoriadis G. Encapsulation of enzymes and other agents in liposomes. Spec. Publ.-R. Soc. Chem. 1987; 63: 94–105
   Google Scholar
• Gubernator K., Müller K., Winkler F. K. The structure of human pancreatic lipase suggests a locally inverted, trypsin-like mechanism. Lipases: structure, mechanism and genetic engineering, L. Alberghina, R. D. Schmid, R. Verger. VCH Verlagsgesellschaft, Weinheim 1991; Vol. 16: 9–16, GBF Monographs
   Google Scholar
• Hebdon G. M., Le Vine H., III, Minard R B., Sahyoun N. E., Schmitges C. J., Cuatrecasas P. Incorporation of rat brain adenylate cyclase into artificial phospholipid vesicles. J. Biol. Chem. 1979; 254: 10459–10465
   PubMedGoogle Scholar
• Hub H.-H., Hupfer B., Ringsdorf H. Polymerization of lipid and lysolipid like diacetylenes in monolayers and liposomes. Org. Coal. Plast. Chem. 1980; 42: 2–7
   Google Scholar
• Klibanov A. M. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci. 1989; 14: 141–144
   PubMed Web of Science ®Google Scholar
• Koch H., Ringsdorf H. Polyreactions in oriented systems, 22: Topochemical polymerization of a diacetylene sulfolipid analog in monolayers and liposomes. Makromol. Chem. 1981; 182: 255–259
   Google Scholar
• Kordel M., Menge U., Morelle G., Erdman H., Schmid R. D. Comparative analysis of lipases in view of protein design. Lipases: Structure, mechanism and genetic engineering, L. Alberghina, R. D. Schmid, R. Verger. VCH Verlagsgesellschaft, Weinheim 1991; Vol. 16: 421–424, GBF Monographs
   Google Scholar
• Lopez E., O'Brien D. F., Whitesides T. H. Effect of membrane composition and lipid structure on the photopolymerization of lipid diacetylenes in bilayer membranes. Biochim. Biophys. Acta 1982; 693: 437–443
   PubMed Web of Science ®Google Scholar
• Malcata F. X., Reyes H. R., Garcia H. S., Hill C. G. J., Amundson C. H. Kinetics and mechanisms of reactions catalyzed by immobilized lipases. Enzyme Microb. Technol. 1992; 14: 426–446
   PubMed Web of Science ®Google Scholar
• Martinek K., Klyachko N. L., Kabanov A. V., Khmelnitsky Y. L., Levashov A. V. Micellar enzymology: its relation to membranology. Biochim. Biophys. Acta. 1989; 981: 161–172
   PubMed Web of Science ®Google Scholar
• Mattson F. H., Volpenhein R. A. Synthesis and properties of glycerides. J. Lipid Res. 1962; 3: 281–296
   Web of Science ®Google Scholar
• Miranda M., Amicarelli F., Ragnelli A. M., Poma A., Arcadi A. Effect of cholesterol on the DOPA oxidase of liposome-integrated mushroom tyrosinase. Colloids Surf. 1989; 35: 353–358
   Google Scholar
• Mosmuller E. W. J., Engbersen J. F. J. (1990) Activity of enzymes entrapped in synthetic surfactant vesicles. Proceedings 3rd Netherlands Biotechnology Congress. 1990, H. Breteler, R. F. Beudeker, K. C. A. M. Luyben. Netherlands Biotechnological Society, Zeist, Vol. 1
   Google Scholar
• Mosmuller E. W. J., Franssen M. C. R., Engbersen J. F. J. Lipase activity in vesicular systems: Characterisation of Candida cylindracea lipase and its activity in polymerisable dialkylammonium surfactant vesicles. Biotechnol. Bioeng. 1992; 48: 196–204
   Google Scholar
• Mukherjee K. D. Lipase-catalyzed reactions for modification of fats and other lipids. Biocatalysis 1990; 3: 277–293
   Google Scholar
• Nome F., Reed W., Politi M., Tundo P., Fendler J. H. Cleft formation upon polymerization of surfactant vesicles. J. Am. Chem. Soc. 1984; 106: 8086–8093
   Google Scholar
• Norde W., Lyklema J. Why proteins prefer interfaces. J. Biomater. Sci., Polym. Ed. 1991; 2: 183–202
   PubMed Web of Science ®Google Scholar
• Otero C, Ballesteros A., Guisan J. M. Immobilization/stabilization of lipase from Candida rugosa. Appl. Biochem. Biotechnol. 1988; 19: 163–175
   PubMed Web of Science ®Google Scholar
• Pabst R., Ringsdorf H., Koch H., Dose K. Light-driven proton transport of bacteriorhodopsin incorporated into long-term stable liposomes of a polymerizable sulfolipid. FEBS Lett. 1983; 154: 5–9
   Web of Science ®Google Scholar
• Paleos C. N. Polymerization of monomeric to polymeric vesicles. Characterization and applications. J. Macromol. Sci., Rev. Macromol. Chem. Phys. 1990; C30(3&4)379–404
   Google Scholar
• Liposomes and their uses in biology and medicine. Annals of the New York Academy of Sciences, D. Papahadjopoulos. The New York Academy of Sciences, New York 1978; Vol. 308: 462
   Google Scholar
• Rialdi G., Battistel E., Barisas B. G. Thermodynamics of enzymes in unusual environments. Thermochim. Acta 1991; 193: 349–361
   Google Scholar
• Ringsdorf H., Schlarb B., Venzmer J. Molecular architecture and function of polymeric oriented systems: models for the study of organization, surface recognition and dynamics of biomembranes. Angew. Chem. Int. Ed. Eng. 1988; 27: 113–158
   Web of Science ®Google Scholar
• Schmid R. D. Stabilized soluble enzymes. Immobilized enzymes, II, T. K. Ghose, A. Fleichter, N. Blakebrough. Springer Verlag, Berlin 1979; Vol. 12: 42–118, Advances in Biochemical Engineering
   Google Scholar
• Schomäcker R., Robinson B. H., Fletcher P. D. I. Interaction of enzymes with surfactants in aqueous solution and in water-in-oil microemulsions. J. Chem. Soc., Faraday Trans. 1 1988; 84: 4203–4212
   Google Scholar
• Schrag J. D., Li Y., Wu S., Cygler M. Ser-His-Glu triad forms the catlytic site of the lipase from Geotrichum candidum. Nature 1991; 351: 761–764
   PubMed Web of Science ®Google Scholar
• Sobotka H., Glick D. Lipolytic enzymes. I. The mechanism of lipolytic enzyme. J. Biol. Chem. 1934; 105: 199–219
   Google Scholar
• Sohn H. S., Chung S. S., Rhee J. S. Deactivation of Candida rugosa lipase. Biotechnol. Lett. 1987; 9: 117–122
   Google Scholar
• Tanford C. Protein denaturation. Part A: characterization of the denatured sate. Part B: the transition from native to denatured state. Adv. Prot. Chem. 1968; 23: 121–282
   PubMedGoogle Scholar
• Tanford C. Protein denaturation. Part C: theoretical models for the mechanism of denaturation. Adv. Prot. Chem. 1970; 24: 1–95
   PubMedGoogle Scholar
• Tatara T., Fujii T., Kawase T., Minagawa M. Studies on applications of lipolytic enzymes in detergency: II. Evaluation of adaptability of various kinds of lipases in practical laundry conditions. J. Am. Oil Chim. Soc 1985; 62: 1053–1058
   Google Scholar
• Tomizuka N., Ota Y., Yamada K. Studies on lipase from Candida cylindracea. Part I. Purification and Properties. Agric. Biol. Chem. 1966; 30: 576–584
   Web of Science ®Google Scholar
• Torchilin V. P., Klibanov A. L. Immobilization of proteins on liposome surface. Enzyme Microb. Technol. 1981; 3: 297–304
   Web of Science ®Google Scholar
• Vaz W. L. C., Kaufmann K., Nicksch A. Use of energy transfer to assay the association of proteins with lipid membranes. Anal. Biochem. 1977; 83: 385–393
   PubMedGoogle Scholar
• Verger R. Enzyme kinetics of lipolysis. Meth. Enzymol. 1980; 64: 340–392
   PubMedGoogle Scholar
• Volkin D. B., Klibanov A. M. Minimizing protein inactivation. Protein structure and function: a practical approach, T. E. Creighton. The practical approach series, IRL Press, Oxford 1990; 1–24
   Google Scholar
• Vuillemard J. C. Recent advances in the large-scale production of lipid vesicles for use in food products: microfluidization. J. Microencapsulation 1991; 8: 547–562
   PubMed Web of Science ®Google Scholar
• Wagner N., Dose K., Koch H., Ringsdorf H. Incorporation of ATP synthetase into long-term stable liposomes of a polymerizable synthetic sulfolipid. FEBS Lett. 1981; 132: 313–318
   PubMedGoogle Scholar
• Winkler F. K., D'Arcy A., Hunziker. Structure of human pancreatic lipase. Nature 1990; 343: 771–774
   PubMed Web of Science ®Google Scholar
• Wolbert R. B. G., Hilhorst R., Voskuilen G., Nachtegaal H., Dekker M., Van't Riet K., et al. Protein transfer from an aqueous phase into reversed micelles. The effect of protein size and charge distribution. Eur. J. Biochem. 1989; 184: 627–633
   PubMedGoogle Scholar
• Zakim D., Scotto A. W. Spontaneous insertion of integral membrane proteins into preformed unilamellar vesicles. Metk, Enzymol. 1989; 171: 253–264
   PubMedGoogle Scholar
• Zale S. E., Klibanov A. M. Why does ribonuclease irreversibly inactivate at high temperatures?. Biochemistry 1986; 25: 5432–5444
   PubMed Web of Science ®Google Scholar