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ORIGINAL ARTICLE

Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions

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Pages 407-414 | Received 21 Apr 2005, Published online: 11 Jul 2009

References

  • Ambler RP, Auffret AD, Clarke PH. The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa. FEBS Lett 1987; 215: 285–290
  • Baek DH, Sing JJ, Lee S-G, Kwon SJ, Asano Y, Sung M-H. New thermostable D-methioninamidase from Brevibacillus borstelensis BCS-1 and its application for D-phenylalanine production. Enzym Microb Technol 2003; 32: 131–139
  • Berne BJ, Pecora R. Dynamic light scattering. John Wiley & Sons, New York 1976
  • Bohidar HB, Behboudina M. Characterization of reverse micelles by dynamic light scattering. Colloids and Surfaces A: Physicochem Eng Aspects 2001; 178: 313–323
  • Brammar RWJ, Clarke PHJ. Induction and repression of Pseudomonas aeruginosa amidase. J Gen Microbiol 1964; 37: 307–319
  • Brammar WJ, Charles IG, Matfield M, Cheng-Pin L, Drew RE, Clarke PH. The nucleotide sequence of the amiE gene of Pseudomonas aeruginosa. FEBS Lett 1987; 215: 291–294
  • Brenner C. Catalysis in the nitrilase superfamily. Curr Opin Struct Biol 2002; 12: 775–782
  • Brown W. Dynamic light scattering: The method and some applications. Oxford University Press, New York 1993
  • Brown PR, Smyth MJ, Clarke PH, Rosemeyer MA. The subunit structure of the aliphatic amidase from Pseudomonas aeruginosa. Eur J Biochem 1973; 34: 177–187
  • Carvalho CML, Cabral JMS. Reverse micelles as reaction media for lipases. Biochime 2000; 82: 1063–1085
  • Cazabat AM, Langerin DJ. Diffusion of interacting particles: Light scattering study of microemulsions. Chem Phys 1981; 74: 3148
  • Chebrou H, Bigey F, Arnaud A, Galzy P. Study of the amidase signature group. Biochim Biophys Acta 1996; 1298: 285–293
  • Chen D-H, Liao M-H. Effects of mixed reverse micellar structure on stability and activity of yeast alcohol dehydrogenase. J Mol Catal B: Enzym 2002; 18: 155–162
  • Chen Y-X, Zhang X-Z, Chen S-M, You D-L, Wu X-X, Yang X-C, Guan W-Z. Kinetically controlled synthesis catalysed by proteases in reverse micelles and separation of precursor dipeptides of RGD. Enzym Microb Technol 1999; 25: 310–315
  • CRC Handbook. 1999. Boca Raton, FL: CRC Press.
  • Denning SN, Morgan SL. Approximating a region of a multifactor response surface. Experimental Design: A Chemometric Approach. Data handling in science and technology. Elsevier Science Publishers, Amsterdam 1987; 3: 181–218
  • Farkas E, Enydy EA, Csoka H. A comparison between the chelating properties of some dihydroxamic acids, desferrioxamine B acetohydroxamic acid. Polyhedron 1998; 18: 2301–2398
  • Farnaud S, Tata R, Sohi MK, Wan T, Brown PR, Sutton BJ. Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme. Biochem J 1999; 340: 711–714
  • Feliciano AS, Dias AI, Prazeres DMF. The effect of stirring and seeding on the AcPheLeuNH2 synthesis and crystallization in reversed micellar system. Enzym Microb Technol 2000; 27: 264–269
  • Fernandes MLM, Krieger N, Baron AM, Zamora PP, Ramos LP, Mitchell DA. Hydrolysis and synthesis reactions catalysed by Thermomyces lanuginosa lipase in the AOT/isooctane reversed micellar system. J Mol Catal B: Enzym 2004; 30: 43–49
  • Fessner W-D, Jones JB. Biocatalysis and biotransformation: from discovery to application. Curr Opin Chem Biol 2001; 5: 103–105
  • Fournand D, Arnaud A, Galzy P. Study of the acyl transfer activity of a recombinant amidase overproduced in an Escherichia coli strain. Application for short-chain hydroxamic acid and acid hydrazide synthesis. J Mol Catal B: Enzym 1998a; 4: 77–90
  • Fournand D, Bigey F, Arnaud A. Acyl transfer activity of an amidase from Rhidicoccus sp. Strain R312: Formation of a wide range of hydroxamic acids. Appl Environ Microbiol 1998b; 64: 2844–2852
  • Fournand D, Bigey F, Ratomahenina R, Arnaud A, Galzy P. Biocatalyst improvement for the production of short-chain hydroxamic acids. Enzym Microb Technol 1997; 20: 424–431
  • Fournand D, Vaysse L, Dubreucq E, Arnaud A, Galzy P. Monohydroxamic acid biosynthesis. J Mol Catal B: Enzym 1998c; 5: 207–211
  • Hauer B, Roberts SM. Biocatalysis and Biotransformation: probing the potential usefulness and the mechanism of action of some novel biocatalysts. Curr Opin Chem Biol 2004; 8: 103–105
  • Kamei N, Tanaka T, Kawai K, Miyawaki K, Okuyama A, Murakami Y, Arakawa Y, Haino M, Harada T, Shimano M. Reverse hydroxamate-based selectice TACE inhibitors. Bioorg Med Chem Lett 2004; 14: 2897–2900
  • Karmali A, Pacheco R, Tata R, Brown P. Substitutions of Thr-103-Ile and Trp-138-gly in amidase from Psueodmonas aeruginosa are responsible for altered kinetic properties and enzyme instability. Mol Biotechnol 2001; 17: 201–212
  • Klyachko N L, Levashov AV. Bioorganic synthesis in reverse micelles and related systems. Curr Opin Colloid Interface Sci 2003; 8: 179–186
  • Komeda H, Ishikawa N, Asano Y. Enhancement of the thermal stability and catalytic activity of D-stereospecific amino-acid amidase from Ochrobacterium anthropi SV3 by directed evolution. J Mol Catal B: Enzym 2003; 21: 283–290
  • Lang J, Lalem N, Zana R. Quaternary water in oil microemulsions. 1: Effect of alcohol chain length and concentration on droplet size and exchange of material between droplets. J Phys Chem 1991; 95: 9533–9541
  • Leung J, Shah DO. Solubilization and phase equilibria of water-in-oil microemulsions. I: Effects of spontaneous curvature and elasticity of interfacial films. J Colloid Interface Sci 1987; 120: 330–344
  • Lopez F, Cinelli G, Ambrosone L, Colafemmina G, Ceglie A, Palazzo G. Role of cosurfactant in water-in-oil microemulsion: interfacial properties tune the enzymatic activity of liapse. Colloids and Surfaces A: Physicochem Eng Aspects 2004; 237: 49–59
  • Martinek K, Klyachko Kabanov AVN, Khmelnitsky YL, Levashov AV. Micellar enzymology: its relation to membranology. Biochem Biophys Acta 1989; 981: 161–172
  • Martins S, Farnaud S, Pacheco V, Pacheco R, Karmali A, Tata R, Brown PR. Differential behaviour of recombinant wild-type and altered amidases on immobilized metal-ion affinity chromatography. Int J Biochromatography 2000; 5: 111–129
  • Melo EP, Aires-Barros MR, Cabral JMS. Reverse micelles and protein biotechnology. Biotechnol Ann Rev 2001; 7: 87–129
  • Melo EP, Costa SMB, Cabral JMS, Fojan P, Petersen SB. Cutinase-AOT interactions in reverse micelles: the effect of 1-hexanol. Chem Phys Lipids 2003; 124: 37–47
  • Novo C, Farnaud S, Tata R, Clemente A, Brown PR. Support for a three dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity. Biochem J 2002; 365: 731–738
  • Novo C, Tata R, Clemente A, Brown PR. Pseudomonas aeruginosa aliphatic amidase is related to the nitrilase/cyanide hydratase enzyme family and Cys166 is predicted to be the active site nucleophile of the catalytic mechanism. FEBS Lett 1995; 367: 275–279
  • Pace, HC, Brenner, C. 2001. The nitrilase superfamily: classification, structure and function. Available: http://genomebiology.com/2001/2/1reviews/0001.1.
  • Pacheco R, Serralheiro MLM, Karmali A, Haris PI. Measuring enzymatic activity of a recombinant amidase using Fourier transform infrared spectroscopy. Anal Biochem 2003; 322: 208–214
  • Pedro AJE, Fevereiro PS, Serralheiro ML, Aires-Barros MR. Study of the stability of Vaccinium myrtillus peroxidase in reverse micellar systems. Biocatal Biotrans 2002; 20: 129–135
  • Rahaman RS, Hatton AT. Structural characterization of α-chymotrypsin containing AOT reversed micelles. J Phys Chem 1991; 95: 1799–1811
  • Robinson LA, Wilson DM, Delaet NGJ, Bradley EK, Dankwardt SM, Campbell JA, Martin RL, Van Wart HE, Walker KAM, Sullivan RW. Novel inhibitors of procollagen C-proteinase. Part 2: glutamic acid hydroxamates. Bioorg Med Chem Lett 2003; 13: 2381–2384
  • Sambrook J, Fritsch E, Maniatis T. A Laboratory Manual. Molecular Cloning. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 1989
  • Serralheiro MLM, Cabral JMS. Irreversible thermoinactivation of α-chymotrypsin in buffer and water miscible organic solvent. Comparison with a reverse micellar system. J Mol Catal B: Enzym 1999a; 7: 191–205
  • Serralheiro MLM, Prazeres DMF, Cabral JMS. Dipeptide synthesis and separation in a reversed micellar membrane reactor. Enzym Microb Technol 1994; 16: 1064–1073
  • Serralheiro MLM, Prazeres DMF, Cabral JMS. Continuous production and simultaneous precipitation of a dipeptide in a reversed micellar membrane reactor. Enzym Microb Technol 1999b; 24: 507–513
  • Shah C, Sellappan S, Madamwar D. Entrapment of enzyme in water-restricted microenvironment-amyloglucosidase in reverse micelles. Process Biochem 2000; 35: 971–975
  • Shah DO, Hou M-J. Effects of the Molecular Structure of the Interface and Continuous Phase on Solubilization of Water in Water/Oil Microemulsions. Langmuir 1987; 3: 1086
  • Shaw NM, Naughton AB. The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca. Tetrahedron 2004; 60: 747–752
  • Tata R, Marsh P, Brown PR. Arg-188 and Trp-144 are implicated in the binding of urea and acetamide to the active site of the amidase from Pseudomonas aeruginosa. Biochim Biophys Acta 1994; 1205: 139–145
  • Taybjee MH, Nadar SK, MacFadyen RJ. Tissue inhibitor of metalloproteinase-1 and matrix metalloproteinase-9 levels in patients with hypertension. Am J Hypertens 1994; 17: 770–774
  • Vieira E, Seoud OA. Effect of a positively charged water-in-oil microemulsion on the apparent pKa of a hydrophilic indicator. J Colloid Interface Sci 1991; 141: 295–298

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