Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization

Enzyme and Microbial Technology

Volumn 49, Issue 4, 2011, Pages 326-346

  Cowan, Don A ^a   Fernandez Lafuente, Roberto ^b  

^a UNIVERSITY OF THE WESTERN CAPE   (South Africa)

^b INSTITUTO DE CATÁLISIS Y PETROLEOQUÍMICA   (Spain)

Author keywords

Chemical modification of enzymes; Enzyme immobilization; Enzyme stabilization; Modulation of enzyme properties; Thermophilic enzymes

Indexed keywords

BIOCATALYTIC PROCESS; COMPLEX MIXTURE; COVALENT LINKAGE; ENZYME INACTIVATION; ENZYME STABILIZATION; FUNCTIONAL PROPERTIES; PROTEIN STABILITY; SOLID SUPPORTS; SUBUNIT DISSOCIATION; THERMOPHILIC ENZYMES;

CATALYSTS; CHEMICAL MODIFICATION; CHEMICAL STABILITY; GENETIC ENGINEERING; INDUSTRIAL APPLICATIONS; PROTEINS; STABILIZATION;

ENZYME IMMOBILIZATION;

ALCOHOL DEHYDROGENASE; ALPHA GALACTOSIDASE; ALPHA GLUCOSIDASE; AMIDASE; AMINOACYLASE; AMYLASE; ASPARTATE CARBAMOYLTRANSFERASE; BETA GALACTOSIDASE; BETA GLUCOSIDASE; CALDOLYSIN; CATALASE; CATECHOL 2,3 DIOXYGENASE; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; CYTOCHROME P450; DIGUANYLATE CYCLASE; DIHYDROLIPOAMIDE DEHYDROGENASE; DNA BINDING PROTEIN; ESTERASE; FERREDOXIN; GLUCOKINASE; GLUCOSE DEHYDROGENASE; GLUTAMATE DEHYDROGENASE; GUANYLATE CYCLASE; IMMOBILIZED ENZYME; ISOMERASE; LEVO ARABINOSE ISOMERASE; MICROBIAL ENZYME; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROPIOLACTONE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

BACTERIAL STRAIN; BIOCATALYST; BIOSENSOR; CHEMICAL MODIFICATION; CROSS LINKING; ENZYME IMMOBILIZATION; ENZYME MODIFICATION; NONHUMAN; PHYSICAL CHEMISTRY; PROTEIN HYDROLYSIS; REVIEW; THERMOPHILE; THERMUS;

ENZYME STABILITY; ENZYMES, IMMOBILIZED; HOT TEMPERATURE; PROTEIN ENGINEERING; PROTEINS;

EID: 80051793850     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.06.023     Document Type: Review

References (268)

1. Pollard D.J., Woodley J.M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol 2007, 25:66-73.
2. Woodley J.M. New opportunities for biocatalysis: making pharmaceutical processes greener. Trends Biotechnol 2008, 26:321-327.
3. Schmid A., Dordick J.S., Hauer B., Kiener A., Wubbolts M., Witholt B. Industrial biocatalysis today and tomorrow. Nature 2001, 409:258-268.
4. Straathof A.J.J., Panke S., Schmid A. The production of fine chemicals by biotransformations. Curr Opin Biotechnol 2002, 13:548-556.
5. Egorova K., Antranikian G. Industrial relevance of thermophilic Archaea. Curr Opin Microbiol 2005, 8:649-655.
6. Cowan D.A., Kirby B.M., Meiring T.L., Ferrer M., Guazzaroni M.E., Golyshina O.V., et al. Enzymes from extreme environments. Manual of industrial microbiology and biotechnology 2010, 512-517. ASM Press. 3rd edition. R.H. Baltz, J.E. Davies, A.L. Demain (Eds.).
7. Cantone S., Hanefeld U., Basso A. Biocatalysis in non-conventional media-ionic liquids, supercritical fluids and the gas phase. Green Chem 2007, 9:954-971.
8. Sheldon R.A. Green solvents for sustainable organic synthesis: state of the art. Green Chem 2005, 7:267-278.
9. Durand J., Teuma E., Gómez M. Ionic liquids as a medium for enantioselective catalysis. C R Chim 2007, 10:152-177.
10. Schoemaker H.E., Mink D., WubboLts M.G. Dispelling the myths-biocatalysis in industrial synthesis. Science 2003, 299:1694-1697.
11. Meyer H.-P. Chemocatalysis biocatalysis (biotransformation): some thoughts of a chemist and of a biotechnologist. Org Process Res Dev 2006, 10:572-580.
12. Polizzi K.M., Bommarius A.S., Broering J.M., Chaparro-Riggers J.F. Stability of biocatalysts. Curr Opin Chem Biol 2007, 11:220-225.
13. Meiring T.L., Bauer R., Scheepers I., Ohloff C., Tuffin I.M., Cowan D.A. Metagenomics and beyond: current approaches and integration with complementary technologies. Metagenomics: current innovations and future trends 2011, 1-19. Horizon Press. D. Marco (Ed.).
14. Mutondo M, Huddy RJ, Bauer R, Tuffin IM, Cowan DA. Metagenomic gene discovery. In: Li RW, editor. Chapter 15 in metagenomics and its applications in agriculture, biomedicine and environmental studies; in press.
15. Samuelson J.C. Recent developments in difficult protein expression: a guide to E. coli strains, promoters, and relevant host mutations. Methods Mol Biol 2011, 705:195-209.
16. Smith D.W. Problems of translating heterologous genes in expression systems: the role of tRNA. Biotechnol Prog 1996, 12:417-422.
17. Kurtovic S., Mannervik B. Identification of emerging quasi-species in directed enzyme evolution. Biochemistry 2009, 48:9330-9339.
18. Schmidt M., Böttcher D., Bornscheuer U.T. Protein engineering of carboxyl esterases by rational design and directed evolution. Protein Pept Lett 2009, 16:1162-1171.
19. Reetz M.T. Controlling the selectivity and stability of proteins by new strategies in directed evolution: the case of organocatalytic enzymes. Ernst Schering Found Symp Proc 2007, 321-340.
20. Jäckel C., Kast P., Hilvert D. Protein design by directed evolution. Ann Rev Biophys 2008, 37:153-173.
21. Avnir D., Lev O., Livage J. Recent bio-applications of sol-gel materials. J Mater Chem 2006, 16:1013-1030.
22. Rusmini F., Zhong Z., Feijen J. Protein immobilization strategies for protein biochips. Biomacromolecules 2007, 8:1775-1789.
23. Betancor L., Luckarift H.R. Bioinspired enzyme encapsulation for biocatalysis. Trends Biotechnol 2008, 26:566-572.
24. Siqueira J.R., Caseli L., Crespilho F.N., Zucolotto V., Oliveira O.N. Immobilization of biomolecules on nanostructured films for biosensing. Biosens Bioelectron 2010, 25:1254-1263.
25. Zhang K., Diehl M.R., Tirrell D.A. Artificial polypeptide scaffold for protein immobilization. J Am Chem Soc 2005, 127:10136-10137.
26. Hernandez K., Fernandez-Lafuente R. Control of protein immobilization. Coupling immobilization and site directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme Microb Technol 2011, 48:107-122.
27. Richter O., Hoffmann H., Kraushaar-Czarnetzki B. Effect of the rotor shape on the mixing characteristics of a continuous flow Taylor-vortex reactor. Chem Eng Sci 2008, 63:3504-3513.
28. Cabana H., Jones J.P., Agathos S.N. Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals. Biotechnol Bioeng 2009, 102:1582-1592.
29. Sheelu G., Kavitha G., Fadnavis N.W. Efficient immobilization of Lecitase in Gelatin hydrogel and degumming of rice bran oil using a spinning basket reactor. J Am Oil Chem Soc 2008, 85:739-748.
30. Rodrigues RC, Berenguer-Murcia A, Fernandez-Lafuente R. Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Adv Synth Catal; in press, doi:10.1002/adsc.201100163.
31. Vallin M., Syrén P.-O., Hult K. Mutant lipase-catalyzed kinetic resolution of bulky phenyl alkyl sec-alcohols: a thermodynamic analysis of enantioselectivity. Chembiochem 2010, 11:411-416.
32. Ortiz-Soto M.E., Rudiño-Piñera E., Rodriguez-Alegria M.E., Munguia A.L. Evaluation of cross-linked aggregates from purified Bacillus subtilis levansucrase mutants for transfructosylation reactions. BMC Biotechnol 2009, 9:68.
33. Van Loo B., Kingma J., Heyman G., Wittenaar A., Lutje Spelberg J.H., Sonke T., et al. Improved enantioselective conversion of styrene epoxides and meso-epoxides through epoxide hydrolases with a mutated nucleophile-flanking residue. Enzyme Microb Technol 2009, 44:145-153.
34. Chiang C.-J., Chern J.-T., Wang J.-Y., Chao Y.-P. Facile immobilization of evolved Agrobacterium radiobacter carbamoylase with high thermal and oxidative stability. J Agric Food Chem 2008, 56:6348-6354.
35. Matsumoto K., Davis B.G., Jones J.B. Chemically modified " polar patch" mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: designing combinatorial biocatalysts. Chem Eur J 2002, 8:4129-4137.
36. Davis B.G., Shang X., DeSantis G., Bott R.R., Jones J.B. The controlled introduction of multiple negative charge at single amino acid sites in subtilisin Bacillus lentus. Bioorg Med Chem 1999, 7:2293-2301.
37. Gron H., Bech L.M., Branner S., Breddam K. A highly active and oxidation-resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modification. Eur J Biochem 1990, 194:897-901.
38. Forde J., Vakurov A., Gibson T.D., Millner P., Whelehan M., Marison I.W., et al. Chemical modification and immobilisation of lipase B from Candida antarctica onto mesoporous silicates. J Mol Catal B: Enzym 2010, 66:203-209.
39. Forde J., Tully E., Vakurov A., Gibson T.D., Millner P., Ó'Fágáin C. Chemical modification and immobilisation of laccase from Trametes hirsuta and from Myceliophthora thermophila. Enzyme Microb Technol 2010, 46:430-437.
40. Wilson L., Illanes A., Abián O., Pessela B.C.C., Fernández-Lafuente R., Guisán J.M. Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media. Biomacromolecules 2004, 5:852-857.
41. Abian O., Mateo C., Fernández-Lorente G., Palomo J.M., Fernández-Lafuente R., Guisán J.M. Stabilization of immobilized enzymes against water-soluble organic cosolvents and generation of hyperhydrophilic micro-environments surrounding enzyme molecules. Biocatal Biotransform 2001, 19:489-503.
42. Fernandez-Lafuente R., Rosell C.M., Caanan-Haden L., Rodes L., Guisan J.M. Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents. Enzyme Microb Technol 1999, 24:96-103.
43. Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb Technol 2009, 45:405-418.
44. Betancor L., Hidalgo A., Fernández-Lorente G., Mateo C., Fernández-Lafuente R., Guisan J.M. Preparation of a stable biocatalyst of bovine liver catalase using immobilization and postimmobilization techniques. Biotechnol Prog 2003, 19:763-767.
45. Fernandez-Lafuente R., Rosell C.M., Rodriguez V., Guisan J.M. Strategies for enzyme stabilization by intramolecular crosslinking with bifunctional reagents. Enzyme Microb Technol 1995, 17:517-523.
46. Mansfeld J., Vriendl G., Veltman O.R., Van Den Burg B., Venema G., Eijsink V.G.H., et al. Site-directed mutagenesis and immobilization for probing a new model of protein stabilization. FASEB J 1997, 11:1309.
47. Ulbrich-Hofmann R., Arnold U., Mansfeld J. The concept of the unfolding region for approaching the mechanisms of enzyme stabilization. J Mol Catal B: Enzym 1999, 7:125-131.
48. Mansfeld J., Vriend G., Van Den Burg B., Eijsink V.G.H., Ulbrich-Hofmann R. Probing the unfolding region in a thermolysin-like protease by site-specific immobilization. Biochemistry 1999, 38:8240-8245.
49. Wynn R., Richards F.M. Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques. Protein Sci 1993, 2:395-403.
50. DeSantis G., Berglund P., Stabile M.R., Gold M., Jones J.B. Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus. Biochemistry 1998, 37:5968-5973.
51. Abian O., Grazú V., Hermoso J., González R., García J.L., Fernández-Lafuente R., et al. Stabilization of Penicillin G Acylase from Escherichia coli: Site-Directed Mutagenesis of the Protein Surface to Increase Multipoint Covalent Attachment. Appl Environ Microbiol 2004, 70:1249-1251.
52. Montes T., Grazú V., López-Gallego F., Hermoso J.A., García J.L., Manso I., et al. Genetic modification of the penicillin G acylase surface to improve its reversible immobilization on ionic exchangers. Appl Environ Microbiol 2007, 73:312-319.
53. López-Gallego F., Montes T., Fuentes M., Alonso N., Grazu V., Betancor, et al. R. Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl supports. J Biotechnol 2005, 116:1-10.
54. Montes T., Grazu V., López-Gallego F., Hermoso J.A., Guisán J.M., Fernández-Lafuente R. Chemical modification of protein surfaces to improve their reversible enzyme immobilization on ionic exchangers. Biomacromolecules 2006, 7:3052-3058.
55. Montes T., Grazú V., Manso I., Galán B., López-Gallego F., González R., et al. Improved stabilization of genetically modified penicillin G acylase in the presence of organic cosolvents by co-immobilization of the enzyme with polyethyleneimine. Adv Synth Catal 2007, 349:459-464.
56. Rodrigues R.C., Godoy C.A., Volpato G., Ayub M.A.Z., Fernandez-Lafuente R., Guisan J.M. Immobilization-stabilization of the lipase from Thermomyces lanuginosus: critical role of chemical amination. Process Biochem 2009, 44:963-968.
57. Fernandez-Lorente G., Godoy C.A., Mendes A.A., Lopez-Gallego F., Grazu V., de las Rivas B., et al. Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose. Biomacromolecules 2008, 9:2553-2561.
58. Baker-Austin C., Dopson M. Life in acid: pH homeostasis in acidophiles. Trends Microbiol 2007, 15:165-171.
59. van de Vossenberg J.L.C.M., Driessen A.J., Zillig W., Konings W.N. Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae. Extremophiles 1998, 2:67-74.
60. Olsson K., Keis S., Morgan H.W., Dimroth P., Cook G.M. Bioenergetic properties of the thermoalkaliphilic Bacillus sp. strain TA2.A1. J Bacteriol 2003, 1852:461-465.
61. Demirjian D.C., Morís-Varas F., Cassidy C.S. Enzymes from extremophiles. Curr Opin Chem Biol 2001, 5:144-151.
62. Hough D.W., Danson M.J. Extremozymes. Curr Opin Chem Biol 1999, 3:39-46.
63. Segerer A.H., Burggraf S., Fiala G., Huber G., Huber R., Pley U., et al. Life in hot springs and hydrothermal vents. Orig Life Evol Biosph 1993, 23:77-90.
64. Kristjannson J.K., Stetter K.O. Thermophilic bacteria, in thermophilic bacteria 1991, CRC Press, Boca Raton, p. 2-13.
65. Cowan D.A. Life in extreme thermal environments: implications for exobiology, in life on mars. British interplanet 1999, Soc Special Publication, p. 37-48.
66. Razvi A., Scholtz J.M. Lessons in stability from thermophilic proteins. Protein Sci 2006, 15:1569-1578.
67. Bischof J.C., He X. Thermal stability of proteins. Ann N Y Acad Sci 2005, 1066:12-33.
68. Van Mierlo C.P.M., Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J Biotechnol 2000, 79:281-298.
69. Cowan D.A. Thermophilic proteins: stability and function in aqueous and organic solvents. Comp Biochem Physiol A Physiol 1997, 118:429-438.
70. Scandurra R., Consalvi V., Chiaraluce R., Politi L., Engel P.C. Protein thermostability in extremophiles. Biochimie 1998, 80:933-941.
71. Daniel R.M., Cowan D.A. Biomolecular stability and life at high temperatures. Cell Mol Life Sci 2000, 57:250-264.
72. Ladenstein R., Antranikian G. Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water. Adv Biochem Eng Biotechnol 1998, 61:37-85.
73. Daniel R.M., Danson M.J., Hough D.W., Lee C.K., Peterson M.E., Cowan D.A. Enzyme stability and activity at high temperatures in anatomy and physiology of extremophilic proteins. Nova Science, Sidiqui 2008, S1-S34. T. Thomas (Ed.).
74. Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M. Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface. J Mol Biol 1999, 289:357-369.
75. Cowan D.A. Relationships between enzyme stability, activity and conformational mobility in organic solvents. Comp Physiol Biochem 1997, 118:429-438.
76. Liang X., Arunima A., Zhao Y., Bhaskaran R., Shende A., Byrne T.S., et al. Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3. Biophys J 2010, 99:273-283.
77. Walters J., Swartz P., Mattos C., Clark A.C. Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3. Arch Biochem Biophys 2011, 508:31-38.
78. Tian J., Wang P., Gao S., Chu X., Wu N., Fan Y. Enhanced thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 by rational engineering of a glycine to proline mutation. FEBS J 2010, 277:4901-4908.
79. Tyagi R., Gupta M.N. Chemical modification and chemical cross-linking for protein/enzyme stabilization. Biochemistry (Moscow) 1998, 63:334-344.
80. Ó'Fágáin C. Enzyme stabilization-recent experimental progress. Enzyme Microb Technol 2003, 33:137-149.
81. Davis B.G. Chemical modification of biocatalysts. Curr Opin Biotechnol 2003, 14:379-386.
82. Palomo J.M. Diels-alder cycloaddition in protein chemistry. Eur J Org Chem 2010, 6303-6314.
83. Chalker J.M., Bernardes G.J.L., Lin Y.A., Davis B.G. Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chem Asian J 2009, 4:630-640.
84. Baslé E., Joubert N., Pucheault M. Protein chemical modification on endogenous amino acids. Chem Biol 2010, 17:213-227.
85. Fernandez-Lafuente R., Rosell C.M., Alvaro G., Guisan J.M. Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde. Enzyme Microb Technol 1992, 14:489-495.
86. Khajeh K., Naderi-Manesh H., Ranjbar B., Moosavi-Movahedi A.A., Nemat-Gorgani M. Chemical modification of lysine residues in Bacillus α-amylases: effect on activity and stability. Enzyme Microb Technol 2001, 28:543-549.
87. Gupta M.N., Roy I. Enzymes in organic media: forms, functions and applications. Eur J Biochem 2004, 271:2575-2583.
88. Cabrera Z., Fernandez-Lorente G., Fernandez-Lafuente R., Palomo J.M., Guisan J.M. Enhancement of Novozym-435 catalytic properties by physical or chemical modification. Process Biochem 2009, 44:226-231.
89. Fernández-Lorente G., Palomo J.M., Mateo C., Munilla R., Ortiz C., Cabrera Z.G., et al. Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance. Biomacromolecules 2006, 7:2610-2615.
90. Torchilin V.P., Maksimenko A.V., Smirnov V.N., Berezin I.V., Klibanov A.M., Martinek K. The principles of enzyme stabilization IV. Modification of 'key' functional groups in the tertiary structure of proteins. Biochem Biophys Acta 1979, 567:1-11.
91. Wong S.S., Wong L.-J.C. Chemical crosslinking and the stabilization of proteins and enzymes. Enzyme Microb Technol 1992, 14:866-874.
92. Torchilin V.P., Maksimenko A.V., Smirnov V.N., Berezin I.V., Martinek K. Principles of enzyme stabilization V. The possibility of enzyme selfstabilization under the action of potentially reversible intramolecular cross-linkages of different length. Biochim Biophys Acta 1979, 568:1-10.
93. Betancor L., López-Gallego F., Hidalgo A., Alonso-Morales N., Fuentes M., Fernández-Lafuente R., et al. Prevention of interfacial inactivation of enzymes by coating the enzyme surface with dextran-aldehyde. J Biotechnol 2004, 110:201-207.
94. Cao L. Immobilised enzymes: science or art?. Curr Opin Chem Biol 2005, 9:217-226.
95. Cao L., van Langen L., Sheldon R.A. Immobilised enzymes: carrier-bound or carrier-free?. Curr Opin Biotechnol 2003, 14:387-394.
96. Hartmeier W. Immobilized biocatalysts-from simple to complex systems. Trends Biotechnol 1985, 3:149-153.
97. Katchalski-Katzir E. Immobilized enzymes-learning from past successes and failures. Trends Biotechnol 1993, 11:471-478.
98. Cheetham P.S.J. The use of biotransformations for the production of flavours and fragrances. Trends Biotechnol 1993, 11:478-488.
99. Iyer P.V., Ananthanarayan L. Enzyme stability and stabilization-aqueous and non-aqueous environment. Process Biochem 2008, 43:1019-1032.
100. Mateo C., Palomo J.M., Fernandez-Lorente G., Guisan J.M., Fernandez-Lafuente R. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol 2007, 40:1451-1463.
101. Bes M.T., Gomez-Moreno C., Guisan J.M., Fernandez-Lafuente R. Selective oxidation: stabilisation by multipoint attachment of ferredoxin NADP+ reductase, an interesting cofactor recycling enzyme. J Mol Catal A: Chem 1995, 98:161-169.
102. Bayramoglu G., Karakişla M., Altintaş B., Metin A.U., Saçak M., Arica M.Y. Polyaniline grafted polyacylonitrile conductive composite fibers for reversible immobilization of enzymes: stability and catalytic properties of invertase. Process Biochem 2009, 44:880-885.
103. Mateo C., Abian O., Fernandez-Lafuente R., Guisan J.M. Reversible enzyme immobilization via a very strong and nondistorting ionic adsorption on support-polyethylenimine composites. Biotechnol Bioeng 2000, 68:98-105.
104. Martinek K., Klibanov A.M., Goldmacher V.S. The principles of enzyme stabilization. II. Increase in the thermostability of enzymes as a result of multipoint noncovalent interaction with a polymeric support. Biochem Biophys Acta 1977, 485:13-28.
105. Martinek K., Klibanov A.M., Goldmacher V.S., Berezin I.V. The principles of enzyme stabilization: I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochem Biophys Acta 1977, 485:1-12.
106. Mateo C., Palomo J.M., Fuentes M., Betancor L., Grazu V., López-Gallego F., et al. Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins. Enzyme Microb Technol 2006, 39:274-280.
107. Mateo C., Grazú V., Pessela B.C.C., Montes T., Palomo J.M., Torres R., et al. Advances in the design of new epoxy supports for enzyme immobilization-stabilization. Biochem Soc Transform 2007, 35:1593-1601.
108. Betancor L., López-Gallego F., Hidalgo A., Alonso-Morales N., Mateo C., Dellamore-Ortiz G., et al. Different mechanisms of protein immobilization on glutaraldehyde activated supports: effect of support activation and immobilization conditions. Enzyme Microb Technol 2006, 39:877-882.
109. López-Gallego F., Betancor L., Mateo C., Hidalgo A., Alonso-Morales N., Dellamora-Ortiz G., et al. Enzyme stabilization by glutaraldehyde crosslinking of adsorbed proteins on aminated supports. J Biotechnol 2005, 119:70-75.
110. Pedroche J., del Mar Yust M., Mateo C., Fernández-Lafuente R., Girón-Calle J., Alaiz M., et al. Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability. Enzyme Microb Technol 2007, 40:1160-1166.
111. Margolin A.L. Novel crystalline catalysts. Trends Biotechnol 1996, 14:223-230.
112. Cao L., Van Rantwijk F., Sheldon R.A. Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org Lett 2000, 2:1361-1364.
113. Wilson L., Betancor L., Fernández-Lorente G., Fuentes M., Hidalgo A., Guisán, et al. Cross-linked aggregates of multimeric enzymes: a simple and efficient methodology to stabilize their quaternary structure. Biomacromolecules 2004, 5:814-817.
114. Mateo C., Fernandes B., Van Rantwijk F., Stolz A., Sheldon R.A. Stabilisation of oxygen-labile nitrilases via co-aggregation with poly(ethyleneimine). J Mol Catal B: Enzymol 2006, 38:154-157.
115. Ostendorp R., Auerbach G., Jaenicke R. Extremely thermostable L(+)-lactate dehydrogenase from Thermotoga maritima: cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state. Protein Sci 1996, 5:862-873.
116. Purcarea C., Ahuja A., Lu T., Kovari L., Guy H.I., Evans D.R. Aquifex aeolicus aspartate transcarbamoylase, an enzyme specialized for the efficient utilization of unstable carbamoyl phosphate at elevated temperature. J Biol Chem 2003, 278:52924-52934.
117. Pavlov N.A., Cherny D.I., Nazimov I.V., Slesarev A.I., Subramaniam V. Identification, cloning and characterization of a new DNA-binding protein from the hyperthermophilic methanogen Methanopyrus kandleri. Nucleic Acids Res 2002, 30:685-694.
118. Clarke D.J., Coulson J., Baillie R., Campopiano D.J. Biotinylation in the hyperthermophile Aquifex aeolicus: isolation of a cross-linked BPL:BCCP complex. Eur J Biochem 2003, 270:1277-1287.
119. Tanaka T., Inoue M., Sakamoto J., Sone N. Intra- and inter-complex cross-linking of subunits in the quinol oxidase super-complex from thermophilic Bacillus PS3. J Biochem 1996, 119:482-486.
120. Yamazaki T., Tsugawa W., Sode K. Increased thermal stability of glucose dehydrogenase by cross-linking chemical modification. Biotechnol Lett 1999, 21:199-202.
121. Piller K., Daniel R.M., Petach H.H. Properties and stabilization of an extracellular α-glucosidase from the extremely thermophilic archaebacteria Thermococcus strain AN1: enzyme activity at 130°C. Biochem Biophys Acta 1996, 1292:197-205.
122. Bolivar J.M., Rocha-Martin J., Mateo C., Cava F., Berenguer J., Fernandez-Lafuente R., et al. Coating of soluble and immobilized enzymes with ionic polymers: full stabilization of the quaternary structure of multimeric enzymes. Biomacromolecules 2009, 10:742-747.
123. Cheon Y.-H., Kim G.-J., Kim H.-S. Stabilization of d-hydantoinase by intersubunit cross-linking. J Mol Catal B: Enzymol 2000, 11:29-35.
124. Botting C.H., Talbot P., Paytubi S., White M.F. Extensive lysine methylation in hyperthermophilic crenarchaea: potential implications for protein stability and recombinant enzymes. Archaea 2010, [art. no. 106341].
125. Maras B., Consalvi V., Chiaraluce R., Politi L., De Rosa M., Bossa F., et al. The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-e{open}-methyllysine related to thermostability?. Eur J Biochem 1992, 20:81-87.
126. Kai K., Noguchi S., Sone N. Over-expression and post-translational modification of thermophilic Bacillus cytochrome c-551 in Bacillus subtilis. J Ferment Bioeng 1997, 84:190-194.
127. Kotwal S.M., Khire J.M., Khan M.I. Chemical modification of α-galactosidase from the thermophilic fungus Humicola sp. J Biochem Mol Biol Biophys 2000, 4:65-72.
128. Burdette D.S., Vieille C., Zeikus J.G. Cloning and expression of the gene encoding the Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase and biochemical characterization of the enzyme. Biochem J 1996, 316:115-122.
129. Peretz M., Weiner L.M., Burstein Y. Cysteine reactivity in Thermoanaerobacter brockii alcohol dehydrogenase. Protein Sci 1997, 6:1074-1083.
130. Hedin E.M.K., Patkar S.A., Vind J., Svendsen A., Hult K., Berglund P. Selective reduction and chemical modification of oxidized lipase cysteine mutants. Can J Chem 2002, 80:529-539.
131. Holmquist M., Martinelle M., Berglund P., Clausen I.G., Patkar S., Svendsen A., et al. Lipases from Rhizomucor miehei and Humicola lanuginosa: modification of the lid covering the active site alters enantioselectivity. J Protein Chem 1993, 12:749-757.
132. Fernandez-Lafuente R. Lipase from Thermomyces lanuginosus: uses and prospects as an industrial biocatalyst. J Mol Catal B: Enzymol 2010, 62:197-212.
133. Khajeh K., Ranjbar B., Naderi-Manesh H., Ebrahim Habibi A., Nemat-Gorgani M. Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calcium. Biochem Biophys Acta 2001, 1548:229-237.
134. Matsumura H., Wiwatchaiwong S., Nakamura N., Yohda M., Ohno H. A novel method for direct electrochemistry of a thermoacidophilic cytochrome P450. Electrochem Commun 2006, 8:1245-1249.
135. Georlette D., Blaise V., Bouillenne F., Damien B., Thorbjarnardóttir S.H., Depiereux E., et al. Adenylation-dependent conformation and unfolding pathways of the NAD +-dependent DNA ligase from the thermophile Thermus scotoductus. Biophys J 2004, 86:1089-1104.
136. Georlette D., Blaise V., Dohmen C., Bouillenne F., Damien B., Depiereux E., et al. Cofactor binding modulates the conformational stabilities and unfolding patterns of NAD+-dependent DNA ligases from Escherichia coli and Thermus scotoductus. J Biol Chem 2003, 27:49945-49953.
137. Alcalde M., Plou F.J., Andersen C., Martín M.T., Pedersen S., Ballesteros A. Chemical modification of lysine side chains of cyclodextrin glycosyltransferase from Thermoanaerobacter causes a shift from cyclodextrin glycosyltransferase to α-amylase specificity. FEBS Lett 1999, 445:333-337.
138. Cowan D.A., Daniel R.M., Morgan H.W. Some observations on the inhibition and activation of a thermophilic protease. Int J Biochem 1987, 19:483-486.
139. Taguchi H., Matsuzawa H., Ohta T. l-lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence. Eur J Biochem 1984, 145:283-290.
140. Kumar D., Savitri, Thakur N., Verma R., Bhalla T.C. Microbial proteases and application as laundry detergent additive. Res J Microbiol 2008, 3:661-672.
141. Wong C.-H. Engineering enzymes for chemoenzymatic synthesis. Part 2: Modifying proteases for peptide synthesis. Trends Biotechnol 1992, 10:378-381.
142. Gusek T.W., Kinsella J.E. Properties of the soluble and immobilized serine protease from Thermomonospora fusca YX. Ann N Y Acad Sci 1990, 613:415-420.
143. Cowan D.A., Daniel R.M. Properties of immobilized caldolysin, a thermostable protease from an extreme thermophile. Biotechnol Bioeng 1982, 24:2053-2061.
144. Mozhaev V.V. Immobilization provides additional stabilization of an initially stable protease from Thermoactinomyces vulgaris (thermitase). Biotechnol Technol 1990, 4:255-256.
145. Wilson S.-A., Peek K., Daniel R.M. Immobilization of a proteinase from the extremely thermophilic organism Thermus Rt41A. Biotechnol Bioeng 1994, 43:225-231.
146. Wilson S.A., Daniel R.M., Peek K. Peptide synthesis with a proteinase from the extremely thermophilic organism Thermus Rt41A. Biotechnol Bioeng 1994, 44:337-346.
147. Prakash O., Jaiswal N. α-Amylase: an ideal representative of thermostable enzymes. Appl Biochem Biotechnol 2010, 160:2401-2414.
148. Collins T., Gerday C., Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 2005, 29:3-23.
149. Paolucci-Jeanjean D., Belleville M.-P., Zakhia N., Rios G.M. Kinetics of cassava starch hydrolysis with Termamyl® enzyme. Biotechnol Bioeng 2000, 6871-6877.
150. Ulbrich R. A comparison of the chemical and thermal stability of soluble and immobilized α-amylases from B. licheniformis and A. oryzae. Biomed Biochem Acta 1988, 47:821-830.
151. Simpson H.D., Haufler U.R., Daniel R.M. An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga. Biochem J 1991, 277:413-417.
152. Edward V.A., Pillay V.L., Swart P., Singh S. Immobilization of xylanase from Thermomyces lanuginosus SSBP using Eudragit S-100. S Afr J Sci 2002, 98:553-554.
153. Maalej-Achouri I., Guerfali M., Gargouri A., Belghith H. Production of xylo-oligosaccharides from agro-industrial residues using immobilized Talaromyces thermophilus xylanase. J Mol Catal B: Enzymol 2009, 59:145-152.
154. Lehmacher A., Bisswanger H. Isolation and characterization of an extremely thermostable d-xylose isomerase from Thermus aquaticus HB8. J Gen Microbiol 1990, 136:679-686.
155. Bandlish R.K., Hess J.M., Epting K.L., Vieille C., Kelly R.M. Glucose-to-fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species. Biotechnol Bioeng 2002, 80:185-194.
156. Jørgensen F., Hansen O.C., Stougaard P. Enzymatic conversion of d-galactose to d-tagatose: Heterologous expression and characterisation of a thermostable l-arabinose isomerase from Thermoanaerobacter mathranii. Appl Microbiol Biotechnol 2004, 64:816-822.
157. Berenguer-Murcia A., Fernandez-Lafuente R. New trends in the recycling of NAD(P)H for the design of sustainable asymmetric reductions catalyzed by dehydrogenases. Curr Org Chem 2010, 14:1000-1021.
158. Raia C.A., D'Auria S., Guagliardi A., Bartolucci S., De Rosa M., Rossi M. Characterization of redox proteins from extreme thermophilic archaehacteria: studies on alcohol dehydrogenase and thioredoxins. Biosens Bioelectron 1995, 10:135-140.
159. Greiner L., Schroder I., Muller D.H., Liese A. Utilization of adsorption effects for the continuous reduction of NADP+ with molecular hydrogen by Pyrococcus furiosus hydrogenase. Green Chem 2003, 5:697-700.
160. Miroliaei M. Studies on the activity and stability of immobilized thermophilic alcohol dehydrogenase. Sci Iran 2007, 14:112-117.
161. Rocha-Martin J., Vega D.E., Cabrera Z., Bolivar J.M., Fernandez-Lafuente R., Berenguer J., et al. Purification, immobilization and stabilization of a highly enantioselective alcohol dehydrogenase from Thermus thermophilus HB27 cloned in E. coli. Process Biochem 2009, 44:1004-1012.
162. Bolivar J.M., Cava F., Mateo C., Rocha-Martín J., Guisán J.M., Berenguer J., et al. Immobilization-stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus. Appl Microbiol Biotechnol 2008, 80:49-58.
163. Mateo C., Abian O., Bernedo M., Cuenca E., Fuentes M., Fernandez-Lorente G., et al. Some special features of glyoxyl supports to immobilize proteins. Enzyme Microb Technol 2005, 37:456-462.
164. Pessela B.C.C., Torres R., Fuentes M., Mateo C., Munilla R., Vian A., et al. Selective and mild adsorption of large proteins on lowly activated immobilized metal ion affinity chromatography matrices: purification of multimeric thermophilic enzymes overexpressed in Escherichia coli. J Chromatogr A 2004, 1055:93-98.
165. Bolivar J.M., Rocha-Martin J., Mateo C., Cava F., Berenguer J., Vega D., et al. Purification and stabilization of a glutamate dehygrogenase from Thermus thermophilus via oriented multisubunit plus multipoint covalent immobilization. J Mol Catal B: Enzymol 2009, 58:158-163.
166. Pessela B.C.C., Munilla R., Betancor L., Fuentes M., Carrascosa A.V., Vian A., et al. Ion exchange using poorly activated supports, an easy way for purification of large proteins. J Chromatogr A 2004, 1034:155-159.
167. Bolivar J.M., Mateo C., Rocha-Martin J., Cava F., Berenguer J., Fernandez-Lafuente R., et al. The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports. Enzyme Microb Technol 2009, 44:139-144.
168. Bolivar J.M., Rocha-Martin J., Godoy C., Rodrigues R.C., Guisan J.M. Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus. Process Biochem 2010, 45:107-113.
169. Grosová Z., Rosenberg M., Rebroš M. Perspectives and applications of immobilised β-galactosidase in food industry-a review. Czech J Food Sci 2008, 26:1-14.
170. Mlichová Z., Rosenberg M. Current trends of β-galactosidase application in food technology. J Food Nutr. Res 2006, 45:47-54.
171. Lu L., Li Z., Xiao M. Recent progress on galacto-oligosaccharides synthesis by microbial beta-galactosidase-a review. Acta Microbiol Sin 2008, 48:980-985.
172. Volkov I.Yu., Lunina N.A., Berezina O.V., Velikodvorskaya G.A., Zverlov V.V. Thermoanaerobacter ethanolicus gene cluster containing the α- and β-galactosidase genes melA and lacA and properties of recombinant LacA. Mol Biol 2005, 39:799-805.
173. Saito T., Yoshida Y., Kawashima K., Lin K.H., Maeda S., Kobayashi T. Immobilization and characterization of a thermostable β-galactosidase from a thermophilic anaerobe on a porous ceramic support. Appl Microbiol Biotechnol 1994, 40:618-621.
174. Saito T., Yoshida Y., Kawashima K., Lin K.H., Inagaki H., Maeda S., et al. Influence of aldehyde groups on the thermostability of an immobilized enzyme on an inorganic support. Mater Sci Eng C 1997, 5:149-152.
175. Nakkharat P., Haltrich D. Lactose hydrolysis and formation of galactooligosaccharides by a novel immobilized β-galactosidase from the thermophilic fungus Talaromyces thermophilus. Appl Biochem Biotechnol 2006, 129:215-225.
176. D'Auria S., Pellino F., La Cara F., Barone R., Rossi M., Nucci R. Immobilization on chitosan of a thermophilic β-glycosidase expressed in Saccharomyces cerevisiae. Appl Biochem Biotechnol 1996, 61:157-166.
177. Febbraio F., Portaccio M., Stellato S., Rossi S., Bencivenga U., Nucci R., et al. Advantages in using immobilized thermophilic β-glycosidase in nonisothermal bioreactors. Biotechnol Bioeng 1998, 59:108-115.
178. Bruins M.E., Thewessen A.J.H., Janssen A.E.M., Boom R.M. Enzyme inactivation due to Maillard reactions during oligosaccharide synthesis by a hyperthermophilic glycosidase: influence of enzyme immobilisation. J Mol Catal B: Enzymol 2003, 21:31-34.
179. Thomsen M.S., Nidetzky B. Microfluidic reactor for continuous flow biotransformations with immobilized enzymes: the example of lactose hydrolysis by a hyperthermophilic β-glycoside hydrolase. Eng Life Sci 2008, 8:40-48.
180. Thomsen M.S., Nidetzky B. Coated-wall microreactor for continuous biocatalytic transformations using immobilized enzymes. Biotechnol J 2009, 4:98-107.
181. Ladero M., Ruiz G., Pessela B.C.C., Vian A., Santos A., Garcia-Ochoa F. Thermal and pH inactivation of an immobilized thermostable β-galactosidase from Thermus sp. strain T2: comparison to the free enzyme. Biochem Eng J 2006, 31:14-24.
182. Pessela B.C.C., Mateo C., Fuentes M., Vian A., García J.L., Carrasosa A.V., et al. Stabilization of a multimeric β-galactosidase from Thermus sp. Strain T2 by immobilization on novel heterofunctional epoxy supports plus aldehyde-dextran cross-linking. Biotechnol Prog 2004, 20:388-392.
183. Pessela B.C.C., Fernández-Lafuente R., Fuentes M., Vián A., García J.L., Carrascosa A.V., et al. Reversible immobilization of a thermophilic β-galactosidase via ionic adsorption on PEI-coated Sepabeads. Enzyme Microb Technol 2003, 32:369-374.
184. Fuentes M., Maquiese J.V., Pessela B.C.C., Abian O., Fernández-Lafuente R., Mateo C., et al. New cationic exchanger support for reversible immobilization of proteins. Biotechnol Prog 2004, 20:284-288.
185. Fuentes M., Pessela B.C.C., Maquiese J.V., Ortiz C., Segura R.L., Palomo J.M., et al. Reversible and strong immobilization of proteins by ionic exchange on supports coated with sulfate-dextran. Biotechnol Prog 2004, 20:1134-1139.
186. Pessela B.C.C., Mateo C., Filho M., Carrascosa A., Fernández-Lafuente R., Guisan J.M. Selective adsorption of large proteins on highly activated IMAC supports in the presence of high imidazole concentrations: Purification, reversible immobilization and stabilization of thermophilic α- and β-galactosidases. Enzyme Microb Technol 2007, 40:242-248.
187. Pessela B.C.C., Fuentes M., Mateo C., Munilla R., Carrascosa A.V., Fernandez-Lafuente R., et al. Purification and very strong reversible immobilization of large proteins on anionic exchangers by controlling the support and the immobilization conditions. Enzyme Microb Technol 2006, 39:909-915.
188. Pessela B.C.C., Mateo C., Carrascosa A.V., Vian A., García J.L., Rivas G., et al. One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-His-tagged β-galactosidase from Thermus sp. strain T2 by using novel heterofunctional chelate-epoxy Sepabeads. Biomacromolecules 2003, 4:107-113.
189. Pessela B.C.C., Vian A., Mateo C., Fernández-Lafuente R., García J.L., Guisán J.M., et al. Overproduction of Thermus sp. strain T2 β-galactosidase in Escherichia coli and preparation by using tailor-made metal chelate supports. Appl Environ Microbiol 2003, 69:1967-1972.
190. Bolivar J.M., Mateo C., Godoy C., Pessela B.C.C., Rodrigues D.S., Giordano R.L.C., et al. The co-operative effect of physical and covalent protein adsorption on heterofunctional supports. Process Biochem 2009, 44:757-763.
191. Bolivar J.M., Mateo C., Grazu V., Carrascosa A.V., Pessela B.C., Guisan J.M. Heterofunctional supports for the one-step purification, immobilization and stabilization of large multimeric enzymes: amino-glyoxyl versus amino-epoxy supports. Process Biochem 2010, 45:1692-1698.
192. Ladero M., Perez M.T., Santos A., Garcia-Ochoa F. Hydrolysis of lactose by free and immobilized β-galactosidase from Thermus sp. strain T2. Biotechnol Bioeng 2003, 81:241-252.
193. Pessela B.C.C., Mateo C., Fuentes M., Vian A., García J.L., Carrascosa A.V., et al. The immobilization of a thermophilic β-galactosidase on Sepabeads supports decreases product inhibition: complete hydrolysis of lactose in dairy products. Enzyme Microb Technol 2003, 33:199-205.
194. Mulimani V.H., Ramalingam V.H. Enzymic hydrolysis of raffinose and stachyose in soymilk by alpha-galactosidase from Gibberella fujikuroi. Biochem Mol Biol Int 1995, 36:897-905.
195. Filho M., Pessela B.C., Mateo C., Carrascosa A.V., Fernandez-Lafuente R., Guisán J.M. Immobilization-stabilization of an α-galactosidase from Thermus sp. strain T2 by covalent immobilization on highly activated supports: selection of the optimal immobilization strategy. Enzyme Microb Technol 2008, 42:265-271.
196. Filho M., Pessela B.C., Mateo C., Carrascosa A.V., Fernandez-Lafuente R., Guisán J.M. Reversible immobilization of a hexameric α-galactosidase from Thermus sp. strain T2 on polymeric ionic exchangers. Process Biochem 2008, 43:1142-1146.
197. Fischer L., Bromann R., Serve W.M., KengerT, De Vos W.M., Wagner F. Catalytical potency of β-glucosidase from the extremophile Pyrococus furiosus in glucoconjugate synthesis. Biotechnology 1996, 14:88-91.
198. Guncheva M., Zhiryakova D. Catalytic properties and potential applications of Bacillus lipases. J Mol Catal B: Enzymol 2011, 68:1-21.
199. Contesini F.J., Lopes D.B., MacEdo G.A., Nascimento M.D.G., Carvalho P.D.O. Aspergillus sp. lipase: potential biocatalyst for industrial use. J Mol Catal B: Enzymol 2010, 67:163-171.
200. Fan Y., Qian J. Lipase catalysis in ionic liquids/supercritical carbon dioxide and its applications. J Mol Catal B: Enzymol 2010, 66:1-7.
201. Rodrigues R.C., Fernandez-Lafuente R. Lipase from Rhizomucor miehei as a biocatalyst in fats and oils modification. J Mol Catal B: Enzymol 2010, 66:15-32.
202. Li N., Zong M.-H. Lipases from the genus Penicillium: production, purification, characterization and applications. J Mol Catal B: Enzymol 2010, 66:43-54.
203. Rodrigues R.C., Fernandez-Lafuente R. Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process. J Mol Catal B: Enzymol 2010, 64:1-22.
204. Bajaj A., Lohan P., Jha P.N., Mehrotra R. Biodiesel production through lipase catalyzed transesterification: an overview. J Mol Catal B: Enzymol 2010, 62:9-14.
205. Shu Z.-Y., Jiang H., Lin R.-F., Jiang Y.-M., Lin L., Huang J.-Z. Technical methods to improve yield, activity and stability in the development of microbial lipases. J Mol Catal B: Enzymol 2010, 62:1-8.
206. Tan T., Lu J., Nie K., Deng L., Wang F. Biodiesel production with immobilized lipase: a review. Biotechnol Adv 2010, 28:628-634.
207. Sánchez-Otero M.G., Valerio-Alfaro G., García-Galindo H.S., Oliart-Ros R.M. Immobilization in the presence of Triton X-100: Modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase. J Ind Microbiol Biotechnol 2008, 35:1687-1693.
208. Nawani N., Singh R., Kaur J. Immobilization and stability studies of a lipase from thermophilic Bacillus sp: the effect of process parameters on immobilization of enzyme. Electr J Biotechnol 2006, 9:559-565.
209. Kumar S., Pahujani S., Ola R.P., Kanwar S.S., Gupta R. Enhanced thermostability of silica-immobilized lipase from Bacillus coagulans BTS-3 and synthesis of ethyl propionate. Acta Microbiol Immunol Hung 2006, 53:219-231.
210. Wood A.N.P., Fernandez-Lafuente R., Cowan D.A. Purification and partial characterization of a novel thermophilic carboxylesterase with high mesophilic specific activity. Enzyme Microb Technol 1995, 17:816-825.
211. Fernandez-Lafuente R., Wood A.N.P., Cowan D.A. Hyperstabilization of a thermophilic esterase by multipoint covalent attachment. Enzyme Microb Technol 1995, 17:366-372.
212. Fernandez-Lafuente R., Wood A.N., Cowan D.A. Reducing enzyme conformational flexibility by multi-point covalent immobilisation. Biotechnol Tech 1995, 9:1-6.
213. Kambourova M., Kirilova N., Mandeva R., Derekova A. Purification and properties of thermostable lipase from a thermophilic Bacillus stearothermophilus MC 7. J Mol Catal B: Enzymol 2003, 22:307-313.
214. Schmidt-Dannert C., Sztajer H., Stocklein W., Menge U., Schmid R.D. Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochem Biophys Acta 1994, 1214:43-53.
215. Carrasco-López C., Godoy C., de las Rivas B., Fernández-Lorente G., Palomo J.M., Guisán J.M., et al. Activation of bacterial thermo alkalophilic lipases is spurred by dramatic structural rearrangements. J Biol Chem 2009, 284:4365-4372.
216. Palomo J.M., Fernández-Lorente G., Rúa M.L., Guisán J.M., Fernández-Lafuente R. Evaluation of the lipase from Bacillus thermocatenulatus as an enantioselective biocatalyst. Tetrahedron Asymmetry 2003, 14:3679-3687.
217. Palomo J.M., Ortiz C., Fuentes M., Fernandez-Lorente G., Guisan J.M., Fernandez-Lafuente R. Use of immobilized lipases for lipase purification via specific lipase-lipase interactions. J Chromatogr A 2004, 1038:267-273.
218. Palomo J.M., Segura R.L., Fernández-Lorente G., Pernas M., Rua M.L., Guisán J.M., et al. Purification, immobilization, and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports. Biotechnol Prog 2004, 20:630-635.
219. Fernandez-Lorente G., Cabrera Z., Godoy C., Fernandez-Lafuente R., Palomo J.M., Guisan J.M. Interfacially activated lipases against hydrophobic supports: effect of the support nature on the biocatalytic properties. Process Biochem 2008, 43:1061-1067.
220. Bolivar J.M., López-Gallego F., Godoy C., Rodrigues D.S., Rodrigues R.C., Batalla P., et al. The presence of thiolated compounds allows the immobilization of enzymes on glyoxyl agarose at mild pH values: new strategies of stabilization by multipoint covalent attachment. Enzyme Microb Technol 2009, 45:477-483.
221. Hiol A., Jonzo M.D., Rugani N., Druet D., Sarda L., Comeau L.C. Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit. Enzyme Microb Technol 2000, 26:421-430.
222. Palomo J.M., Segura R.L., Mateo C., Fernandez-Lafuente R., Guisan J.M. Improving the activity of lipases from thermophilic organisms at mesophilic temperatures for biotechnology applications. Biomacromolecules 2004, 5:249-254.
223. Lee D.-C., Lee S.-G., Kim H.-S. Production of D-p-hydroxyphenylglycine from D. l-5-(4-hydroxyphenyl)hydantoin using immobilized thermostable d-hydantoinase from Bacillus stearothermophilus SD-1. Enzyme Microb Technol 1996, 18:35-40.
224. Nam K.Y., Struck D.K., Holtzapple M.T. ATP regeneration by thermostable ATP synthase. Biotechnol Bioeng 1996, 51:305-316.
225. Bartsch K., Schneider R., Schulz A. Stereospecific production of the herbicide phosphinothricin (Glufosinate): Purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process. Appl Environ Microbiol 1996, 62:3794-3799.
226. Fernandez-Lafuente R., Guisan J.M., Ali S., Cowan D. Immobilization of functionally unstable catechol-2,3-dioxygenase greatly improves operational stability. Enzyme Microb Technol 2000, 26:568-573.
227. Martín M.T., Plou F.J., Alcalde M., Ballesteros A. Immobilization on Eupergit C of cyclodextrin glucosyltransferase (CGTase) and properties of the immobilized biocatalyst. J Mol Catal B: Enzymol 2003, 21:299-308.
228. Martín M.T., Cruces M.A., Alcalde M., Plou F.J., Bernabé M., Ballesteros A. Synthesis of maltooligosyl fructofuranosides catalyzed by immobilized cyclodextrin glucosyltransferase using starch as donor. Tetrahedron 2004, 60:529-534.
229. Tardioli P.W., Zanin G.M., de Moraes F.F. Characterization of Thermoanaerobacter cyclomaltodextrin glucanotransferase immobilized on glyoxyl-agarose. Enzyme Microb Technol 2006, 39:1270-1278.
230. Amud A.E., Da Silva G.R.P., Tardioli P.W., Soares C.M.F., Moraes F.F., Zanin G.M. Methods and supports for immobilization and stabilization of cyclomaltodextrin glucanotransferase from Thermoanaerobacter. Appl Biochem Biotechnol 2008, 146:189-201.
231. Moldes C., García J.L., García P. Contruction of a chimeric thermostable pyrophosphatase to facilitate its purification and immobilization by using the choline-binding tag. Appl Environ Microbiol 2004, 70:4642-4647.
232. Kim H.-J., Kim A.-R., Jeon S.-J. Immobilization on chitosan of a thermophilic trehalose synthase from Thermus thermophilus HJ6. J Microb Biotechnol 2010, 20:513-517.
233. Makhongela H.S., Glowacka A.E., Agarkar V.B., Sewell B.T., Weber B., Cameron R.A., et al. A novel thermostable nitrilase superfamily amidase from Geobacillus pallidus showing acyl transfer activity. Appl Microbiol Biotechnol 2007, 75:801-811.
234. Chiyanzu I., Cowan D.A., Burton S.G. Immobilization of Geobacillus pallidus RAPc8 nitrile hydratase (NHase) reduces substrate inhibition and enhances thermostability. J Mol Catal B: Enzymol 2010, 63:109-115.
235. Pasunooti S., Surya W., Tan S.N., Liang Z.-X. Sol-gel immobilization of a thermophilic diguanylate cyclase for enzymatic production of cyclic-di-GMP. J Mol Catal B: Enzymol 2010, 67:98-103.
236. Beneyton T., El Harrak A., Griffiths A.D., Hellwig P., Taly V. Immobilization of CotA, an extremophilic laccase from Bacillus subtilis, on glassy carbon electrodes for biofuel cell applications. Electrochem Commun 2011, 13:24-27.
237. Hidalgo A., Betancor L., Lopez-Gallego F., Moreno R., Berenguer J., Fernández-Lafuente R., et al. Design of an immobilized preparation of catalase from Thermus thermophilus to be used in a wide range of conditions. Structural stabilization of a multimeric enzyme. Enzyme Microb Technol 2003, 33:278-285.
238. Hickey A.M., Marle L., McCreedy T., Watts P., Greenway G.M., Littlechild J.A. Immobilization of thermophilic enzymes in miniaturized flow reactors. Biochem Soc Transform 2007, 35:1621-1623.
239. Hickey A.M., Ngamsom B., Wiles C., Greenway G.M., Watts P., Littlechild J.A. A microreactor for the study of biotransformations by enzyme. Biotechnol J 2009, 4:510-516.
240. Ngamsom B., Hickey A.M., Greenway G.M., Littlechild J.A., Watts P., Wiles C. Development of a high throughput screening tool for biotransformations utilising a thermophilic l-aminoacylase enzyme. J Mol Catal B: Enzymol 2010, 63:81-86.
241. Sakihama N., Nagai K., Ohmori H., Tomizawa H., Tsujita M., Shin M. Immobilized ferredoxins for affinity chromatography of ferredoxin-dependent enzymes. J Chromatogr 1992, 597:147-153.
242. Kohda J., Kawanishi H., Suehara K.-I., Nakano Y., Yano T. Stabilization of free and immobilized enzymes using hyperthermophilic chaperonin. J Biosci Bioeng 2006, 101:131-136.
243. Bergeron L.M., Gomez L., Whitehead T.A., Clark D.S. Self-renaturing enzymes: design of an enzyme-chaperone chimera as a new approach to enzyme stabilization. Biotechnol Bioeng 2009, 102:1316-1322.
244. Tikhonova G.A., Tikhonova T.V., Gurvits I.D., Karyagina A.S., Lavrova N.V., Sergienko O.V., et al. Chimeric lactase capable of spontaneous and strong immobilization on cellulose and development of a continuous-flow system for lactose hydrolysis at high temperatures. Appl Environ Microbiol 2010, 76:8071-8075.
245. Nahálka J., Gemeiner P. Thermoswitched immobilization-A novel approach in reversible immobilization. J Biotechnol 2006, 123:478-482.
246. Staiano M., Baldassarre M., Esposito M., Apicella E., Vitale R., Aurilia V., et al. New trends in bio/nanotechnology: stable proteins as advanced molecular tools for health and environment. Environ Technol 2010, 31:935-942.
247. Irwin J.A. Extremophiles and their application to veterinary medicine. Environ Technol 2010, 31:857-869.
248. Aoki K., Ishimaru Y., Iida T. Characteristics of ISFET-type β-glucosidic glucoside sensor using thermophilic enzymes β-glucosidase and glucokinase. Chem Ind Chem J 1999, 767-768.
249. Aoki K., Suzuki H., Ishimaru Y., Toyama S., Ikariyama Y., Iida T. Thermophilic glucokinase-based sensors for the detection of various saccharides and glycosides. Sens Actuators B 2005, 108:727-732.
250. Jeffries C., Pasco N., Baronian K., Gorton L. Evaluation of a thermophile enzyme for a carbon paste amperometric biosensor: l-glutamate dehydrogenase. Biosens Bioelectron 1997, 12:225-232.
251. Lehn C., Schmidt H.-L. Stability and stabilization of enzymes from mesophilic and thermophilic organisms in respect to their use in FIA-systems for the determination of l-lactate and acetate. J Chem Technol Biotechnol 1997, 69:161-166.
252. Antiochia R., Cass A.E.G., Palleschia G. Purification and sensor applications of an oxygen insensitive, thermophilic diaphorase. Anal Chem Acta 1997, 345:17-28.
253. Halliwell C.M., Simon E., Toh C.-S., Bartlett P.N., Cass A.E.G. Immobilisation of lactate dehydrogenase on poly(aniline)-poly(acrylate) and poly(aniline)-poly-(vinyl sulphonate) films for use in a lactate biosensor. Anal Chem Acta 2002, 453:191-200.
254. Maly J., Masojidek J., Masci A., Ilie M., Cianci E., Foglietti V., et al. Direct mediatorless electron transport between the monolayer of photosystem II and poly(mercapto-p-benzoquinone) modified gold electrode-new design of biosensor for herbicide detection. Biosens Bioelectron 2005, 21:923-932.
255. Koblizek M., Masojidek J., Komenda J., Kucera T., Pilloton R., Mattoo A.K., et al. A sensitive photosystem II-based biosensor for detection of a class of herbicides. Biotechnol Bioeng 1998, 60:664-669.
256. Banat I.M., Nigam, Koblížek M., Malý J., Masojídek J., Komenda J.K., et al. A biosensor for the detection of triazine and phenylurea herbicides designed using Photosystem II coupled to a screen-printed electrode. Biotechnol Bioeng 2002, 78:110-116.
257. Bachas-Daunert P.G., Sellers Z.P., Wei Y. Detection of halogenated organic compounds using immobilized thermophilic dehalogenase. Anal Bioanal Chem 2009, 395:1173-1178.
258. Zheng H., Zhou J., Okezaki Y., Suye S.-I. Construction of l-lysine sensor by layer-by-layer adsorption of l-lysine 6-dehydrogenase and ferrocene-labeled high molecular weight coenzyme derivative on gold electrode. Electroanalysis 2008, 20:2685-2691.
259. Palomo J.M., Fernández-Lorente G., Guisán J.M., Fernández-Lafuente R. Modulation of immobilized lipase enantioselectivity via chemical amination. Adv Synth Catal 2007, 349:1119-1127.
260. Godoy C.A., de las Rivas B., Filice M., Fernández-Lorente G., Guisan J.M., Palomo J.M. Enhanced activity of an immobilized lipase promoted by site-directed chemical modification with polymers. Process Biochem 2010, 45:534-541.
261. Rodrigues R.C., Ayub M.A.Z. Effects of the combined use of Thermomyces lanuginosus and Rhizomucor miehei lipases for the transesterification and hydrolysis of soybean oil. Process Biochem 2011, 46:682-688.
262. Rodrigues R.C., Pessela B.C.C., Volpato G., Fernandez-Lafuente R., Guisan J.M., Ayub M.A.Z. Two step ethanolysis: a simple and efficient way to improve the enzymatic biodiesel synthesis catalyzed by an immobilized-stabilized lipase from Thermomyces lanuginosus. Process Biochem 2010, 45:1268-1273.
263. Rodrigues R.C., Bolivar J.M., Volpato G., Filice M., Godoy C., Fernandez-Lafuente R., et al. Improved reactivation of immobilized-stabilized lipase from Thermomyces lanuginosus by its coating with highly hydrophilic polymers. J Biotechnol 2009, 144:113-119.
264. Rodrigues R.C., Bolivar J.M., Palau-Ors A., Volpato G., Ayub M.A.Z., Fernandez-Lafuente R., et al. Positive effects of the multipoint covalent immobilization in the reactivation of partially inactivated derivatives of lipase from Thermomyces lanuginosus. Enzyme Microb Technol 2009, 44:386-393.
265. Rodrigues R.C., Godoy C.A., Filice M., Bolivar J.M., Palau-Ors A., Garcia-Vargas J.M., et al. Reactivation of covalently immobilized lipase from Thermomyces lanuginosus. Process Biochem 2009, 44:641-646.
266. Godoy C.A., Rivas B.D.L., Grazú V., Montes T., Guisàn J.M., López-Gallego F. Glyoxyl-disulfide agarose: a tailor-made support for site-directed rigidification of proteins. Biomacromolecules 2011, 12:1800-1809.
267. Grazú V., López-Gallego F., Montes T., Abian O., González R., Hermoso J.A., et al. Promotion of multipoint covalent immobilization through different regions of genetically modified penicillin G acylase from E. coli. Process Biochem 2010, 45:390-398.
268. Díaz-Rodríguez A., Davis B.G. Chemical modification in the creation of novel biocatalysts. Curr Opin Chem Biol 2011, 15:211-219.