[1]
|
Ventura, S., Vega, M.C., Lacroix, E., Angrand, I., Spagnolo, L. and Serrano, L. (2002) Conformational strain in the hydrophobic core and its implications for protein folding and design. Nature: Structural Biology, 9, 485-493. doi:10.1038/nsb799
|
[2]
|
Kim, D.E., Gu, H. and Baker, D. (1998) The sequences of small proteins are not extensively optimized for rapid folding by natural selection. Proceedings of the National Academy of Science USA, 95, 4981-4986.
doi:10.1073/pnas.95.9.4982
|
[3]
|
Demetrius, L. (2002) Thermodynamics and kinetics of protein folding an evolutionary perspective. Journal of Theoretical Biology, 217, 397-411.
doi:10.1006/jtbi.2002.3006
|
[4]
|
Saraboji, K., Michael Gromiha, M. and Ponnuswamy, M.N. (2005) Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetic on T4 and human lysozymes. Computational Biology and Chemistry, 29, 25-35.
doi:10.1016/j.compbiolchem.2004.12.002
|
[5]
|
Rose, G.D., Fleming, P.J., Banawar, J.R. and Maritan A. (2006) A backbone-based theory of protein folding. Proceedings of the National Academy of Science USA, 45, 16623-16633. doi:10.1073/pnas.0606843103
|
[6]
|
Yutani, K., Ogasahara, K., Tsujita, T. and Yoshinobu, S. (1987) Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α subunit. Proceedings of the National Academy of Science USA, 84, 4441-4444.
doi:10.1073/pnas.84.13.4441
|
[7]
|
Leow, T.C., Rahman, R.N.Z.R.A., Basri, M. and Salleh, A.B. (2007) High temperature crystallization of thermostable T1 lipase. Crystal Growth Design, 7, 406-410.
doi:10.1021/cg050506z
|
[8]
|
Leow, T.C., Rahman, R.N.Z., Basri, M. and Salleh, A.B. (2007) A thermoalkaliphilic lipase of Geobacillus sp. T1. Extremophiles, 11, 527-535.
doi:10.1007/s00792-007-0069-y
|
[9]
|
Matsumura, H., Yamamoto, T., Leow, T.C., Mori, T., Basri, M., Rahman, R.N.Z., Inoue, T., Inoue, T., Kai, Y. and Salleh, A.B. (2008) Novel cation-π interaction revealed by crystal structure of thermoalkalophilic lipase. Proteins: Structure, Function and Bioinformatics, 70, 592-598. doi:10.1002/prot.21799
|
[10]
|
Carrasco-López, C., Godoy, C., de las Rivas, B., Fernández-Lorente, G., Palomo, J.M., Guisan, G.M., Fernández-Lorente, R., Martinez-Ripoll, M. and Hermoso, J.A. (2009) Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements. Journal of Biological Chemistry, 284, 4365-4372.
|
[11]
|
Rother, K., Hildebrand, P.W., Goede, A., Gruening, B. and Preissner, R. (2009) Voronoia: Analyzing packing in protein structures. Nucleic Acids Reviews, 37, D393-D395. doi:10.1093/nar/gkn769
|
[12]
|
http://bioinformatics.charite.de/voronoia
|
[13]
|
Kwon, D.K. and Rhee, J.S. (1986) A simple and rapid colorimetric method for determination of free fatty acids for lipase assay. Journal of American Oil Chemistry Society, 63, 89-92. doi:10.1007/BF02676129
|
[14]
|
Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
doi:10.1016/0003-2697(76)90527-3
|
[15]
|
Ishikawa, K., Nakamura, H., Morikawa, K. and Kanaya, S. (1993). Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. Biochemistry, 32, 6171-6178. doi:10.1021/bi00075a009
|
[16]
|
Zhang, W.M. and Lei, X.G. (2008) Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis. Applied Microbiology and Biotechnology, 77, 1033- 1040. doi:10.1007/s00253-007-1239-7
|
[17]
|
Eyal, E., Najmanovich, R., Edelman, M. and Sobolev, V. (2003) Protein side-chain rearrangement in regions of point mutations. Protein Structure, Function, and Bioinformatics, 50, 272-282. doi:10.1002/prot.10276
|
[18]
|
Eriksson, A.E., Baase, W.A., Zhang, X-J., Heinz, D.W., Blaber, M., Baldwin, E.P. and Matthews, B.W. (1992) Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science, 255, 178-183. doi:10.1126/science.1553543
|
[19]
|
Ventura, S. and Serrano, L. (2004) Designing protein from the inside out. Proteins Structure, Function and Bioinformatics, 56, 1-10. doi:10.1002/prot.20142
|
[20]
|
Fu, D., Li, Z.-Y., Huang, H.-Q., Yuan, T., Shi, P., Luo, H., Meng, K., Yang, P. and Yao, B. (2011) Catalytic efficiency of HAP phytases is determined by a key residue in close proximity to the active site. Applied Environmental Microbiology, 90, 1295-1302.
|
[21]
|
Seo, H.S., Koo, Y.J., Lim, J.Y., Song, J.T., Kim, C.H., Kim, J.K., Lee, J.S. and Choi, Y.D. (2000) Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli. Applied Environmental Microbiology, 66, 2484-2490.
doi:10.1128/AEM.66.6.2484-2490.2000
|
[22]
|
Kim, S.-H., Pokhrel, S. and Yoo, Y.-J. (2008) Mutation of non-conserved amino acids surrounding catalytic site to shift pH optimum of Bacillus circulans xylanase. Journal of Molecular Catalysis B: Enzymatic, 55, 130-136.
doi:10.1016/j.molcatb.2008.02.006
|
[23]
|
Laane, C., Boeren, S., Hilhorst, R. and Veeger, C. (1987) Optimization of biocatalysis in organic media. In: Laane, C., Tramper, J. and Lilly, M.D., Eds., Biocatalysis in Organic Media, Elsevier Science Publishers, Amsterdam, 65-84.
|
[24]
|
Klibanov, A.M. (2001) Improving enzymes by using them in organic solvent. Nature, 409, 241-246.
doi:10.1038/35051719
|
[25]
|
Klibanov, A.M. (1997) Why are enzymes less active in organic solvents than in water? Trends in Biotechnology, 15, 77-83. doi:10.1016/S0167-7799(97)01013-5
|
[26]
|
Dandavate, V., Jinjala, J., Keharia, H. and Madamwar, D. (2009) Production, partial purification and characterization of organic solvent tolerant lipase from Burkholderia multivorans V2 and its application for ester synthesis. Bioresource Technology, 100, 3374-3381.
doi:10.1016/j.biortech.2009.02.011
|
[27]
|
Tanford, C. (1961) Physical chemistry of macromolecules. John Wiley and Sons, New York.
|
[28]
|
Valstar, A. (2000) Protein-surfactant interactions. Ph.D. Thesis, Uppsala University, Uppsala.
|
[29]
|
Schmidt-Dannert, C., Rua, M.L., Atomi, H. and Schmid, R.D. (1996) Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning nucleotide sequence, purification and some properties. Biochimie and Biophysica Acta, 1301, 105-114.
|
[30]
|
Eltaweel, M.A., Rahman, R.N.Z., Basri, M. and Salleh, A.B. (2005) An organic-solvent stable lipase from Bacillus sp. strain 42. Analytical Biochemistry, 53, 187-192.
|
[31]
|
Leow, T.C. (2005) Molecular studies, characterization and structure elucidation of a thermostable lipase from Geobacillus sp. Ph.D. Thesis, Universiti Putra Malaysia, Serdang.
|
[32]
|
Hermoso J., Pignolo, D., Kerfelec, B. and Crenon, I. (1996) Lipase activation by non-ionic detergents. The crystal structure of porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. Journal of Biological Chemistry, 271, 18007-18016.
doi:10.1074/jbc.271.30.18007
|
[33]
|
Ruiz-Pena, M., Oropesa-Nuriez, R., Pons, T., Louro, S.R. and Perez-Gamatges, A. (2010) Physico-chemical studies of molecular interactions between nonionic surfactants and bovine serum albumin. Colloids and Surfaces B: Bio- interfaces, 75, 282-289.
doi:10.1016/j.colsurfb.2009.08.046
|
[34]
|
Glusker, J.P., Katz, A.K. and Bock, C.W. (1999) Metal ions in biological systems. Rigaku Journal, 16, 8-16.
|
[35]
|
Rahman, R.N.Z., Baharum, S.N., Basri, M. and Salleh, A.B. (2005) High yield purification of an organic solvent-tolerant lipase from Pseudomonas sp. strain S5. Analytical Biochemistry, 341, 267-274.
doi:10.1016/j.ab.2005.03.006
|
[36]
|
Don, H., Ga, S., Han, S.P. and Cao, S.G. (1999) Purification and characterization of a Pseudomonas sp. lipase and its properties in non-aqueous media. Biotechnology and Applied Biochemistry, 30, 251-156.
|