{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T23:59:19Z","timestamp":1772841559676,"version":"3.50.1"},"reference-count":29,"publisher":"Elsevier BV","issue":"8-9","license":[{"start":{"date-parts":[[1999,6,1]],"date-time":"1999-06-01T00:00:00Z","timestamp":928195200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Enzyme and Microbial Technology"],"published-print":{"date-parts":[[1999,6]]},"DOI":"10.1016\/s0141-0229(98)00163-x","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T17:44:23Z","timestamp":1027619063000},"page":"569-576","source":"Crossref","is-referenced-by-count":34,"title":["Cutinase stability in AOT reversed micelles: system optimization using the factorial design methodology"],"prefix":"10.1016","volume":"24","author":[{"given":"C.M.L","family":"Carvalho","sequence":"first","affiliation":[]},{"given":"J.M.S","family":"Cabral","sequence":"additional","affiliation":[]},{"given":"M.R","family":"Aires-Barros","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0141-0229(98)00163-X_BIB1","doi-asserted-by":"crossref","unstructured":"Carvalho, C. M. L., Serralheiro, M. L. M., Cabral, J. M. S., and Aires-Barros, M. R. Application of factorial design to the study of transesterification reactions using cutinase in AOT reversed micelles. Enz. Microbiol. Technol. 1997, 21, 117\u2013123","DOI":"10.1016\/S0141-0229(96)00245-1"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB2","doi-asserted-by":"crossref","unstructured":"Martinez, C., De Geus, P., Lauwereys, M., Matthyssens, G., and Cambillau, C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 1992, 356, 615\u2013618","DOI":"10.1038\/356615a0"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB3","doi-asserted-by":"crossref","unstructured":"Martinez, C., Nicolas, A., van Tilbeurgh, H., Egloff, M., Cudrey, C., Verger, R., and Cambillau, C. Cutinase, a lipolytic enzyme with a preformed hole. Biochemistry 1994, 33, 83\u201389","DOI":"10.1021\/bi00167a011"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB4","doi-asserted-by":"crossref","unstructured":"Longhi, S., Manesse, M., Verheij, H. M., De Haas, G. H., Egmond, M., Knoops-Mouthuy, E., and Cambillau, C. Crystal stucture of cutinase covalently inhibited by a triglyceride analogue. Protein Sci. 1997, 6, 275\u2013286","DOI":"10.1002\/pro.5560060202"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB5","doi-asserted-by":"crossref","unstructured":"Melo, E. P., Aires-Barros, M. R., and Cabral, J. M. S. Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles. Appl. Biochem. Biotechnol. 1994, 49, 45\u201356","DOI":"10.1007\/BF02788039"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB6","doi-asserted-by":"crossref","unstructured":"Sebasti\u00e3o, M. J., Cabral, J. M. S., and Aires-Barros, M. R. Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles. Biotechnol. Bioeng. 1993, 42, 326\u2013332","DOI":"10.1002\/bit.260420309"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB7","unstructured":"Box, G. E. P., Hunter, W. G., and Hunter, J. S. In: Statistics for Experimenters. John Wiley and Sons, New York, 1985"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB8","unstructured":"Barker, T. B. In: Quality by Experimental Design. Marcel Dekker, Inc., New York, 1985"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB9","unstructured":"Lauwereys, M., De Geus, P., De Meutter, J., Stanssens, P., and Matthyssens, G. In: Lipases: Structure, Mechanism and Genetic Engineering (Alberghina, R. D. and Verger, R., Eds.). VCH, New York, 1990, 243\u2013251"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB10","unstructured":"Yates, F. The design and analysis of factorial experiments. Bulletin 1937, 35"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB11","unstructured":"Gupta, M. N. Thermostabilization of proteins. Biotechnol. Appl. Biochem. 1991, 14, 1\u201311"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB12","doi-asserted-by":"crossref","unstructured":"Levashov, A. V., Khmelnitsky, Y. L., Klyachko, N. L., Chernyak, V. Y., and Martinek, K. Enzymes entrapped into reversed micelles in organic solvents. Sedimentation analysis of the protein-aerosolOT-H2O- octane system. J Coll. Int. Sci. 1982, 88, 444\u2013457","DOI":"10.1016\/0021-9797(82)90273-9"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB13","doi-asserted-by":"crossref","unstructured":"Soliday, C. L. and Kolattukudy, P. E. Primary structure of the active site region of fungal cutinase, an enzyme involved in phytopathogenesis. Biochem. Biophys. Res. Commun. 1983, 114, 1017\u20131022","DOI":"10.1016\/0006-291X(83)90663-0"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB14","doi-asserted-by":"crossref","unstructured":"Melo, E. P., Carvalho, C. M. L., Aires-Barros, M. R., Costa, S. M. B., Cabral, J. M. S. Activity loss and conformational changes of cutinase in reverse micelles. Biotechnol. Bioeng. 1998, 58, 380\u2013386","DOI":"10.1002\/(SICI)1097-0290(19980520)58:4<380::AID-BIT5>3.0.CO;2-F"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB15","doi-asserted-by":"crossref","unstructured":"Barbaric, S. and Luisi, P. L. Micellar solubilization of biopolymers in organic solvents. 5. Activity and conformation of \u03b1-chymotrypsin in isooctane-AOT reverse micelles. J. Am. Chem. Soc. 1981, 103, 4239\u20134244","DOI":"10.1021\/ja00404a044"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB16","doi-asserted-by":"crossref","unstructured":"Papadimitriou, V., Xenakis, A., Cazianis, C. T., Stamatis, H., Egmond, M., and Kolisis, F. N. EPR studies of cutinase in microemulsions. Ann. N.Y. Acad. Sci. 1996, 799, 275\u2013280","DOI":"10.1111\/j.1749-6632.1996.tb33213.x"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB17","doi-asserted-by":"crossref","unstructured":"Hasegawa, M. and Kitahara, A. Microviscosity in water pool of aerosol-OT reversed micelle determined with viscosity-sensitive fluorescence probe, auramine O, and fluorescence depolarization of xanthene dyes. J. Phys. Chem. 1994, 98, 2120\u20132124","DOI":"10.1021\/j100059a024"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB18","doi-asserted-by":"crossref","unstructured":"Andrade, S. M. and Costa, S. M. B. Fluorescence studies of the drug piroxicam in reverse micelles of AOT and microemulsions of Triton X-100. Prog. Colloid Polym. Sci. 1996, 100, 195\u2013200","DOI":"10.1007\/BFb0115779"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB19","doi-asserted-by":"crossref","unstructured":"Goto, A., Yoshioka, H., Manabe, M., and Goto R. NMR, spectroscopic study on the dissolution of water in sodium bis(2-ethlylhexyl) sulfosuccinate\/toluene solution. Langmuir 1995, 11, 4873\u20134875","DOI":"10.1021\/la00012a046"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB20","doi-asserted-by":"crossref","unstructured":"Ayyagari, M. S. and John, V. T. Substrate-induced stability of the lipase from Candida cylindracea in reversed micelles. Biotechnol. Lett. 1995, 17, 177\u2013182","DOI":"10.1007\/BF00127984"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB21","doi-asserted-by":"crossref","unstructured":"Larreta-Garde, V., Xu, Z.F., and Thomas, D. Behaviour of enzymes in the presence of additives. Ann. N.Y. Acad. Sci. 1988, 542, 294\u2013298","DOI":"10.1111\/j.1749-6632.1988.tb25845.x"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB22","doi-asserted-by":"crossref","unstructured":"Mannesse, M. L. M., Cox, R. C., Koops, B. C., Verheij, H. M., de Haas, D. H., Egmond, M. R., van der Hijden, H. T. W. M., and de Vlieg, J. Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length in the substrate molecule on activity and enantioselectivity. Biochemistry 1995, 34, 6400\u20136407","DOI":"10.1021\/bi00019a020"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB23","doi-asserted-by":"crossref","unstructured":"Prang\u00e9, T., Schiltz, M., Pernot, L., Colloc'h, N., Longhi, S., Bourguet, W., and Fourme, R. Exploring hydrophobic sites in proteins with xenon or kripton. Proteins 1998, 30, 61\u201373","DOI":"10.1002\/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.0.CO;2-N"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB24","doi-asserted-by":"crossref","unstructured":"Hayes, D. G. and Gulari, E. Improvement of enzyme activity and stability for reverse micellar-encapsulated lipases in the presence of short-chain and polar alcohols. Biochemistry 1994, 11, 223\u2013231","DOI":"10.3109\/10242429408998142"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB25","doi-asserted-by":"crossref","unstructured":"Zana, R., Yiv, S., Strazielle, C., and Lianos, P. Effect of alcohol on the properties of micellar system. 1. Critical micellization, micelle molecular weight and ionization degree, and solubility of alcohols in micellar solutions. J. Coll. Inter. Sci. 1981, 80, 208\u2013223","DOI":"10.1016\/0021-9797(81)90177-6"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB26","doi-asserted-by":"crossref","unstructured":"Egmond, M. R., Vlieg, J., Verheij, H. M., and de Haas, G. H. In: Engineering of\/with Lipases (Malcata, F. X., Ed.). Kluwer Academic Publishers, Dordrecht, 1995, 193\u2013202","DOI":"10.1007\/978-94-009-1671-5_12"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB27","doi-asserted-by":"crossref","unstructured":"Gon\u00e7alves, A. P. V., Lopes, J. M., Lemos, F., Ram\u00f4a Ribeiro, F., Prazeres, D. M. F., Cabral, J. M. S., and Aires-Barros, M. R. Zeolites as supports for enzymatic hydrolysis reactions. Comparative study of several zeolites. J. Mol. Cat. B: Enzymatic 1996, 1, 53\u201360","DOI":"10.1016\/1381-1177(95)00013-5"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB28","doi-asserted-by":"crossref","unstructured":"Petersen, M. T., Martel, P., Petersen, E. I., Drabl\u00f8s, F., and Petersen, S. B. Surface and electrostatics of cutinases. In: Methods in Enzymology (Rubin, B. and Dennis, E. A., Eds.). Academic Press, London, U.K., 1997, 284, 130\u2013153","DOI":"10.1016\/S0076-6879(97)84009-8"},{"key":"10.1016\/S0141-0229(98)00163-X_BIB29","doi-asserted-by":"crossref","unstructured":"Henley, J. P. and Sadana, A. Categorization of enzyme deactivations using series-type mechanism. Enz. Microbiol. Technol. 1985, 7, 50\u201360","DOI":"10.1016\/0141-0229(85)90013-4"}],"container-title":["Enzyme and Microbial Technology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S014102299800163X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S014102299800163X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,1,14]],"date-time":"2020-01-14T17:48:48Z","timestamp":1579024128000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S014102299800163X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,6]]},"references-count":29,"journal-issue":{"issue":"8-9","published-print":{"date-parts":[[1999,6]]}},"alternative-id":["S014102299800163X"],"URL":"https:\/\/doi.org\/10.1016\/s0141-0229(98)00163-x","relation":{},"ISSN":["0141-0229"],"issn-type":[{"value":"0141-0229","type":"print"}],"subject":[],"published":{"date-parts":[[1999,6]]}}}