References
- Andualema, B. and Gessesse, A. 2012. Microbial lipases and their industrial applications: review. Biotechnol. 11, 100-118. https://doi.org/10.3923/biotech.2012.100.118
- Bateman, A., Birney, E., Cerruti, L., Durbin, R., Etwiller, L., Eddy, S.R., Griffiths-Jones, S., Howe, K.L., Marshall, M., and Sonnhammer, E.L.L. 2002. The Pfam protein families database. Nucleic Acids Res. 30, 276-280. https://doi.org/10.1093/nar/30.1.276
- Blank, K., Morfill, J., Gumpp, H., and Gaub, H.E. 2006. Functional expression of Candida antarctica lipase B in Escherichia coli. J. Biotechnol. 125, 474-483. https://doi.org/10.1016/j.jbiotec.2006.04.004
- Boekhout, T. 1995. Pseudozyma Bandoni emend. Boekhout, a genus for yeast-like anamorphs of ustilaginales. J. Gen. Appl. Microbiol. 41, 359-366. https://doi.org/10.2323/jgam.41.359
- Bornscheuer, U.T. and Kazlauskas, R.J. 2006. Hydrolases in Organic Synthesis. 2nd. Wiley-VCH, Weinheim, Germany.
- Bornscheuer, U.T. and Pohl, M. 2001. Improved biocatalysts by directed evolution and rational protein design. Curr. Opin. Chem. Biol. 5, 137-143. https://doi.org/10.1016/S1367-5931(00)00182-4
- Brady, L., Brzozowski, A.M., Derewenda, Z.S., Dodson, E., Dodson, G., Tolley, S., Turkenburg, J.P., Christiansen, L., Huge-Jensen, B., Norskov, L., et al. 1990. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343, 767-770. https://doi.org/10.1038/343767a0
- Brzozowski, A.M., Derewenda, U., Derewenda, Z.S., Dodson, G.G., Lawson, D.M., Turkenburg, J.P., Bjorkling, F., Huge-Jensen, B., Patkar, S.A., and Thim, L. 1991. A model for interfacial activation in lipases from the structure of a fungal lipaseinhibitor complex. Nature 351, 491-494. https://doi.org/10.1038/351491a0
- Carbone, M.N. and Arnold, F.H. 2007. Engineering by homologous recombination: exploring sequence and function within a conserved fold. Curr. Opin. Struct. Biol. 17, 454-459. https://doi.org/10.1016/j.sbi.2007.08.005
- Chodorge, M., Fourage, L., Ullmann, C., Duvivier, V., Masson, J.M., and Lefevre, F. 2005. Rational strategies for directed evolution of biocatalysts-application to Candida antarctica lipase B (CALB). Adv. Synth. Catal. 347, 1022-1026. https://doi.org/10.1002/adsc.200505055
- Crameri, A., Raillard, S.A., Bermudez, E., and Stemmer, W.P.C. 1998. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391, 288-291. https://doi.org/10.1038/34663
- Grochulski, P., Li, Y., Schrag, J.D., Bouthillier, F., Smith, P., Harrison, D., Rubin, B., and Cygler, M. 1993. Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem. 268, 12843-12847.
- Grochulski, P., Li, Y., Schrag, J.D., and Cygler, M. 1994. Two conformational states of Candida rugosa lipase. Protein Sci. 3, 82-91.
- Gross, R.A., Kumar, A., and Kalra, B. 2001. Polymer synthesis by in vitro enzyme catalysis. Chem. Rev. 101, 2097-2124. https://doi.org/10.1021/cr0002590
- Hoegh, I., Patkar, S., Halkier, T., and Hansen, M.T. 1995. Two lipases from Candida antarctica: Cloning and expression in Aspergillus oryzae. Can. J. Bot. 73, 869-875. https://doi.org/10.1139/b95-333
- Janes, L.E., Cimpoia, A., and Kazlauskas, R.J. 1999. Proteasemediated separation of cis and trans diastereomers of 2(R,S)-benzyloxymethyl-4(S)-carboxylic acid 1,3-dioxolane methyl ester: intermediates for the synthesis of dioxolane nucleosides. J. Org. Chem. 64, 9019-9029. https://doi.org/10.1021/jo990757c
- Jung, S. and Park, S. 2008. Improving the expression yield of Candida antarctica lipase B in Escherichia coli by mutagenesis. Biotechnol. Lett. 30, 717-722. https://doi.org/10.1007/s10529-007-9591-3
- Liu, D., Schmid, R.D., and Rusnak, M. 2006. Functional expression of Candida antarctica lipase B in the Escherichia coli cytoplasm - a screening system for a frequently used biocatalyst. Appl. Microbiol. Biotechnol. 72, 1024-103. https://doi.org/10.1007/s00253-006-0369-7
- Martinelle, M., Holmquist, M., and Hult, K. 1995. On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase. Biochim. Biophys. Acta 1258, 272-276. https://doi.org/10.1016/0005-2760(95)00131-U
- Neylon, C. 2004. Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution. Nucleic Acids Res. 32, 1448-1459. https://doi.org/10.1093/nar/gkh315
- Ollis, D.L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S.M., Harel, M., Remington, S.J., and Silman, I. 1992. The alpha/beta hydrolase fold. Protein Eng. 5, 197-211. https://doi.org/10.1093/protein/5.3.197
- Rotticci, D. 2003. Understanding and engineering the enantioselectivity of Candida antarctica lipase B towards sec-alcohols, Ph.D. thesis, KTH, Stockholm, Sweden.
- Rotticci-Mulder, J.C., Gustavsson, M., Holmquist, M., Hult, K., and Martinelle, M. 2001. Expression in Pichia pastoris of Candida antarctica lipase B and lipase B fused to a cellulose-binding domain. Protein Expr. Purif. 21, 386-392. https://doi.org/10.1006/prep.2000.1387
- Schmid, R.D. and Verger, R. 1998. Lipases: interfacial enzymes with attractive applications. Angew. Chem. Int. Ed. 37, 1608-1633. https://doi.org/10.1002/(SICI)1521-3773(19980703)37:12<1608::AID-ANIE1608>3.0.CO;2-V
- Takwa, M., Wittrup Larsen, M., Hult, K., and Martinelle, M. 2011. Rational redesign of Candida antarctica lipase B for the ring opening polymerization of D,D-lactide. Chem. Commun. 47, 7392-7394. https://doi.org/10.1039/c1cc10865d
- Uppenberg, J., Oehrner, N., Norin, M., Hult, K., Kleywegt, G.J., Patkar, S., Waagen, V., Anthonsen, T., and Jones, T.A. 1995. Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochem. 34, 16838-16851. https://doi.org/10.1021/bi00051a035
- van der Mee, L., Helmich, F., de Bruijn, R., Vekemans, J.A.J.M., Palmans, A.R.A., and Meijer, E.W. 2006. Investigation of lipase-catalyzed ring-opening polymerizations of lactones with various ring sizes: kinetic evaluation. Macromolecules 39, 5021-5027. https://doi.org/10.1021/ma060668j
- Verger, R. 1997. Interfacial activation of lipases: facts and artifacts. Trends Biotechnol. 15, 32-38. https://doi.org/10.1016/S0167-7799(96)10064-0
- Wu, Q., Soni, P., and Reetz, M.T. 2013. Laboratory evolution of enantiocomplementary Candida antarctica lipase B mutants with broad substrate scope. J. Am. Chem. Soc. 135, 1872-1881. https://doi.org/10.1021/ja310455t
- Zhang, N., Suen, W.C., Windsor, W., Xiao, L., Madison, V., and Zaks, A. 2003. Improving tolerance of Candida antartica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng. 16, 599-605. https://doi.org/10.1093/protein/gzg074
Cited by
- Mapping the Substrate Selectivity of Novel Lipase fromPseudozyma hubeiensisSY62 vol.37, pp.10, 2016, https://doi.org/10.1002/bkcs.10918
- Surveying Enantioselectivity of Two Candida antarctica -lipase-B Homologs Towards Chiral sec -Alcohols vol.38, pp.11, 2017, https://doi.org/10.1002/bkcs.11289
- Expression and characterization of a CALB-type lipase from Sporisorium reilianum SRZ2 and its potential in short-chain flavor ester synthesis vol.14, pp.5, 2015, https://doi.org/10.1007/s11705-019-1889-x