Friedmann, E.I. Endolithic microorganisms in the Antarctic cold desert. Science 1982, 215, 1045-1053
Cary, S.C.; McDonald, I.R.; Barrett, J.E.; Cowan, D.A. On the rocks: The microbiology of Antarctic Dry Valley soils. Nat. Rev. Microbiol. 2010, 8, 129-138
Cowan, D.A.; Casanueva, A.; Stafford, W. Ecology and Biodiversity of Cold-adapted Microorganisms. In Physiology and Biochemistry of Extremophiles; Gerday, C., Glansdorff, N., Eds.; ASM Press: Washington, DC, USA, 2007; pp. 119-132
Margesin, R.; Schinner, F.; Marx, J.C.; Gerday, C. Psychrophiles, from Biodiversity to Biotechnology; Springer-Verlag: Berlin/Heidelberg, Germany, 2008
Feller, G.; Gerday, C. Psychrophilic enzymes: Hot topics in cold adaptation. Nat. Rev. Microbiol. 2003, 1, 200-208
Feller, G. Protein stability and enzyme activity at extreme biological temperatures. J. Phys. Condens. Mat. 2010, 22, doi 10.1088/0953-8984/1022/1032/323101
Feller, G.; Lonhienne, T.; Deroanne, C.; Libioulle, C.; Van Beeumen, J.; Gerday, C. Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23. J. Biol. Chem. 1992, 267, 5217-5221
D'Amico, S.; Collins, T.; Marx, J.C.; Feller, G.; Gerday, C. Psychrophilic microorganisms: Challenges for life. EMBO Rep. 2006, 7, 385-389
Collins, T.; Meuwis, M.A.; Gerday, C.; Feller, G. Activity, stability and flexibility in glycosidases adapted to extreme thermal environments. J. Mol. Biol. 2003, 328, 419-428
D'Amico, S.; Marx, J.C.; Gerday, C.; Feller, G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 2003, 278, 7891-7896
Georlette, D.; Damien, B.; Blaise, V.; Depiereux, E.; Uversky, V.N.; Gerday, C.; Feller, G. Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases. J. Biol. Chem. 2003, 278, 37015-37023
Siddiqui, K.S.; Feller, G.; D'Amico, S.; Gerday, C.; Giaquinto, L.; Cavicchioli, R. The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase. J. Bacteriol. 2005, 187, 6197-6205
Fields, P.A.; Somero, G.N. Hot spots in cold adaptation: Localized increases in conformational flexibility in lactate dehydrogenase A(4) orthologs of Antarctic notothenioid fishes. Proc. Natl. Acad. Sci. USA 1998, 95, 11476-11481
Chiuri, R.; Maiorano, G.; Rizzello, A.; del Mercato, L.L.; Cingolani, R.; Rinaldi, R.; Maffia, M.; Pompa, P.P. Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases. Biophys. J. 2009, 96, 1586-1596
Fedoy, A.E.; Yang, N.; Martinez, A.; Leiros, H.K.; Steen, I.H. Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability. J. Mol. Biol. 2007, 372, 130-149
Tosco, A.; Birolo, L.; Madonna, S.; Lolli, G.; Sannia, G.; Marino, G. GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: Molecular characterization and gene cloning. Extremophiles 2003, 7, 17-28
Piette, F.; D'Amico, S.; Struvay, C.; Mazzucchelli, G.; Renaut, J.; Tutino, M.L.; Danchin, A.; Leprince, P.; Feller, G. Proteomics of life at low temperatures: Trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. Mol. Microbiol. 2010, 76, 120-132
Falasca, P.; Evangelista, G.; Cotugno, R.; Marco, S.; Masullo, M.; De Vendittis, E.; Raimo, G. Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125. Extremophiles 2012, 16, 539-552
Aghajari, N.; Feller, G.; Gerday, C.; Haser, R. Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 1998, 7, 564-572
Aghajari, N.; Feller, G.; Gerday, C.; Haser, R. Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 1998, 6, 1503-1516
Aghajari, N.; Roth, M.; Haser, R. Crystallographic evidence of a transglycosylation reaction: Ternary complexes of a psychrophilic alpha-amylase. Biochemistry 2002, 41, 4273-4280
Qian, M.; Haser, R.; Buisson, G.; Duee, E.; Payan, F. The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution. Biochemistry 1994, 33, 6284-6294
Feller, G. Enzyme Function at Low Temperatures in Psychrophiles. In Protein Adaptation in Extremophiles; Siddiqui, K.S., Thomas, T., Eds.; Nova Science Publishers: New York, NY, USA, 2008; pp. 35-69
Russell, R.J.; Gerike, U.; Danson, M.J.; Hough, D.W.; Taylor, G.L. Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 1998, 6, 351-361
Aghajari, N.; van Petegem, F.; Villeret, V.; Chessa, J.P.; Gerday, C.; Haser, R.; Van Beeumen, J. Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins 2003, 50, 636-647
Kim, S.Y.; Hwang, K.Y.; Kim, S.H.; Sung, H.C.; Han, Y.S.; Cho, Y.J. Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 1999, 274, 11761-11767
Leiros, I.; Moe, E.; Lanes, O.; Smalas, A.O.; Willassen, N.P. The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features. Acta Crystallogr. D Biol. Crystallogr. 2003, 59, 1357-1365
Gorfe, A.A.; Brandsdal, B.O.; Leiros, H.K.; Helland, R.; Smalas, A.O. Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: Qualitative evaluation of electrostatic differences at the substrate binding site. Proteins 2000, 40, 207-217
Brandsdal, B.O.; Smalas, A.O.; Aqvist, J. Electrostatic effects play a central role in cold adaptation of trypsin. FEBS Lett. 2001, 499, 171-175
Tsigos, I.; Velonia, K.; Smonou, I.; Bouriotis, V. Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123. Eur. J. Biochem. 1998, 254, 356-362
Merlino, A.; Russo Krauss, I.; Castellano, I.; de Vendittis, E.; Rossi, B.; Conte, M.; Vergara, A.; Sica, F. Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis. J. Struct. Biol. 2010, 172, 343-352
Aurilia, V.; Rioux-Dube, J.F.; Marabotti, A.; Pezolet, M.; D'Auria, S. Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. The case of an esterase from Pseudoalteromonas haloplanktis. J. Phys. Chem. B 2009, 113, 7753-7761
Mereghetti, P.; Riccardi, L.; Brandsdal, B.O.; Fantucci, P.; de Gioia, L.; Papaleo, E. Near native-state conformational landscape of psychrophilic and mesophilic enzymes: Probing the folding funnel model. J. Phys. Chem. B 2010, 114, 7609-7619
Spiwok, V.; Lipovova, P.; Skalova, T.; Duskova, J.; Dohnalek, J.; Hasek, J.; Russell, N.J.; Kralova, B. Cold-active enzymes studied by comparative molecular dynamics simulation. J. Mol. Model. 2007, 13, 485-497
Tiberti, M.; Papaleo, E. Dynamic properties of extremophilic subtilisin-like serine-proteases. J. Struct. Biol. 2011, 174, 69-83
D'Amico, S.; Sohier, J.S.; Feller, G. Kinetics and energetics of ligand binding determined by microcalorimetry: Insights into active site mobility in a psychrophilic alpha-amylase. J. Mol. Biol. 2006, 358, 1296-1304
Sun, K.; Camardella, L.; Di Prisco, G.; Herve, G. Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica. FEMS Microbiol. Lett. 1998, 164, 375-382
Xu, Y.; Zhang, Y.; Liang, Z.; van de Casteele, M.; Legrain, C.; Glansdorff, N. Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: Properties of the enzyme, genetic organization and synthesis in Escherichia coli. Microbiology 1998, 144, 1435-1441
Alvarez, M.; Zeelen, J.P.; Mainfroid, V.; Rentier-Delrue, F.; Martial, J.A.; Wyns, L.; Wierenga, R.K.; Maes, D. Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. J.Biol. Chem. 1998, 273, 2199-2206
Narinx, E.; Baise, E.; Gerday, C. Subtilisin from psychrophilic Antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng. 1997, 10, 1271-1279
Coquelle, N.; Fioravanti, E.; Weik, M.; Vellieux, F.; Madern, D. Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments. J. Mol. Biol. 2007, 374, 547-562
Georlette, D.; Jonsson, Z.O.; van Petegem, F.; Chessa, J.; van Beeumen, J.; Hubscher, U.; Gerday, C. A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur. J. Biochem. 2000, 267, 3502-3512
Masullo, M.; Arcari, P.; de Paola, B.; Parmeggiani, A.; Bocchini, V. Psychrophilic elongation factor Tu from the antarctic Moraxella sp. Tac II 25: Biochemical characterization and cloning of the encoding gene. Biochemistry 2000, 39, 15531-15539
Ruggiero, I.; Raimo, G.; Palma, M.; Arcari, P.; Masullo, M. Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125. Extremophiles 2007, 11, 699-709
Ciardiello, M.A.; Camardella, L.; Carratore, V.; di Prisco, G. L-Glutamate dehydrogenase from the antarctic fish Chaenocephalus aceratus. Primary structure, function and thermodynamic characterisation: Relationship with cold adaptation. Biochim. Biophys. Acta 2000, 1543, 11-23
Di Fraia, R.; Wilquet, V.; Ciardiello, M.A.; Carratore, V.; Antignani, A.; Camardella, L.; Glansdorff, N.; Di Prisco, G. NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases. Eur. J. Biochem. 2000, 267, 121-131
D'Amico, S.; Gerday, C.; Feller, G. Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 2001, 276, 25791-25796
Xu, Y.; Feller, G.; Gerday, C.; Glansdorff, N. Moritella cold-active dihydrofolate reductase: Are there natural limits to optimization of catalytic efficiency at low temperature? J. Bacteriol. 2003, 185, 5519-5526
Garsoux, G.; Lamotte, J.; Gerday, C.; Feller, G. Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis. Biochem. J. 2004, 384, 247-253
Altermark, B.; Niiranen, L.; Willassen, N.P.; Smalas, A.O.; Moe, E. Comparative studies of endonuclease I from cold-adapted Vibrio salmonicida and mesophilic Vibrio cholerae. FEBS J. 2007, 274, 252-263
Birolo, L.; Tutino, M.L.; Fontanella, B.; Gerday, C.; Mainolfi, K.; Pascarella, S.; Sannia, G.; Vinci, F.; Marino, G. Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling. Eur. J. Biochem. 2000, 267, 2790-2802
Watanabe, S.; Yasutake, Y.; Tanaka, I.; Takada, Y. Elucidation of stability determinants of cold-adapted monomeric isocitrate dehydrogenase from a psychrophilic bacterium, Colwellia maris, by construction of chimeric enzymes. Microbiology 2005, 151, 1083-1094
Collins, T.; Meuwis, M.A.; Stals, I.; Claeyssens, M.; Feller, G.; Gerday, C. A novel family 8 xylanase, functional and physicochemical characterization. J. Biol. Chem. 2002, 277, 35133-35139
Xu, Y.; Feller, G.; Gerday, C.; Glansdorff, N. Metabolic enzymes from psychrophilic bacteria: Challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi. J. Bacteriol. 2003, 185, 2161-2168
Gerike, U.; Danson, M.J.; Russell, N.J.; Hough, D.W. Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R. Eur. J. Biochem. 1997, 248, 49-57
Li, X.; Jiang, X.; Li, H.; Ren, D. Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: Molecular cloning, gene expression and characterization of the recombinant protein. Extremophiles 2008, 12, 325-333
Cartier, G.; Lorieux, F.; Allemand, F.; Dreyfus, M.; Bizebard, T. Cold adaptation in DEAD-box proteins. Biochemistry 2010, 49, 2636-2646
Tang, M.A.; Motoshima, H.; Watanabe, K. Fluorescence studies on the stability, flexibility and substrate-induced conformational changes of acetate kinases from psychrophilic and mesophilic bacteria. Protein J. 2012, 31, 337-344
D'Amico, S.; Gerday, C.; Feller, G. Temperature adaptation of proteins: Engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase. J. Mol. Biol. 2003, 332, 981-988
Cipolla, A.; D'Amico, S.; Barumandzadeh, R.; Matagne, A.; Feller, G. Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic alpha-amylase from Antarctic Bacterium. J. Biol. Chem. 2011, 286, 38348-38355
Asgeirsson, B.; Cekan, P. Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod. FEBS Lett. 2006, 580, 4639-4644
Lonhienne, T.; Gerday, C.; Feller, G. Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 2000, 1543, 1-10
Bjelic, S.; Brandsdal, B.O.; Aqvist, J. Cold adaptation of enzyme reaction rates. Biochemistry 2008, 47, 10049-10057
Tehei, M.; Franzetti, B.; Madern, D.; Ginzburg, M.; Ginzburg, B.Z.; Giudici-Orticoni, M.T.; Bruschi, M.; Zaccai, G. Adaptation to extreme environments: Macromolecular dynamics in bacteria compared in vivo by neutron scattering. EMBO Rep. 2004, 5, 66-70
Russell, N.J. Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 2000, 4, 83-90
Gianese, G.; Bossa, F.; Pascarella, S. Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. Proteins 2002, 47, 236-249
Goldstein, R.A. Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation. Protein Sci. 2007, 16, 1887-1895
Kulakova, L.; Galkin, A.; Nakayama, T.; Nishino, T.; Esaki, N. Cold-active esterase from Psychrobacter sp. Ant300: Gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability. Biochim. Biophys. Acta 2004, 1696, 59-65
Mavromatis, K.; Tsigos, I.; Tzanodaskalaki, M.; Kokkinidis, M.; Bouriotis, V. Exploring the role of a glycine cluster in cold adaptation of an alkaline phosphatase. Eur. J. Biochem. 2002, 269, 2330-2335
Sakaguchi, M.; Matsuzaki, M.; Niimiya, K.; Seino, J.; Sugahara, Y.; Kawakita, M. Role of proline residues in conferring thermostability on aqualysin I. J. Biochem. 2007, 141, 213-220
Paredes, D.I.; Watters, K.; Pitman, D.J.; Bystroff, C.; Dordick, J.S. Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility. BMC Struct. Biol. 2011, 11, 42
Feller, G.; D'Amico, D.; Gerday, C. Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis. Biochemistry 1999, 38, 4613-4619
Yip, K.S.; Stillman, T.J.; Britton, K.L.; Artymiuk, P.J.; Baker, P.J.; Sedelnikova, S.E.; Engel, P.C.; Pasquo, A.; Chiaraluce, R.; Consalvi, V. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 1995, 3, 1147-1158
Vetriani, C.; Maeder, D.L.; Tolliday, N.; Yip, K.S.; Stillman, T.J.; Britton, K.L.; Rice, D.W.; Klump, H.H.; Robb, F.T. Protein thermostability above 100 degrees C: A key role for ionic interactions. Proc. Natl. Acad. Sci. USA 1998, 95, 12300-12305
Papaleo, E.; Tiberti, M.; Invernizzi, G.; Pasi, M.; Ranzani, V. Molecular determinants of enzyme cold adaptation: Comparative structural and computational studies of cold- and warm-adapted enzymes. Curr. Protein Pept. Sci. 2011, 12, 657-683
Bell, G.S.; Russell, R.J.; Connaris, H.; Hough, D.W.; Danson, M.J.; Taylor, G.L. Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile. Eur. J. Biochem. 2002, 269, 6250-6260
Bae, E.; Phillips, G.N., Jr. Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J. Biol. Chem. 2004, 279, 28202-28208
Mandrich, L.; Pezzullo, M.; Del Vecchio, P.; Barone, G.; Rossi, M.; Manco, G. Analysis of thermal adaptation in the HSL enzyme family. J. Mol. Biol. 2004, 335, 357-369
Tronelli, D.; Maugini, E.; Bossa, F.; Pascarella, S. Structural adaptation to low temperatures-analysis of the subunit interface of oligomeric psychrophilic enzymes. FEBS J. 2007, 274, 4595-4608
Zheng, B.; Yang, W.; Zhao, X.; Wang, Y.; Lou, Z.; Rao, Z.; Feng, Y. Crystal structure of hyperthermophilic endo-beta-1,4-glucanase: Implications for catalytic mechanism and thermostability. J. Biol. Chem. 2012, 287, 8336-8346
De Vendittis, E.; Castellano, I.; Cotugno, R.; Ruocco, M.R.; Raimo, G.; Masullo, M. Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition. J. Theor. Biol. 2008, 250, 156-171
Saelensminde, G.; Halskau, O., Jr.; Helland, R.; Willassen, N.P.; Jonassen, I. Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins. Extremophiles 2007, 11, 585-596
Saunders, N.F.; Thomas, T.; Curmi, P.M.; Mattick, J.S.; Kuczek, E.; Slade, R.; Davis, J.; Franzmann, P.D.; Boone, D.; Rusterholtz, K.; et al. Mechanisms of thermal adaptation revealed from the genomes of the Antarctic Archaea Methanogenium frigidum and Methanococcoides burtonii. Genome Res. 2003, 13, 1580-1588
Jahandideh, M.; Barkooie, S.M.; Jahandideh, S.; Abdolmaleki, P.; Movahedi, M.M.; Hoseini, S.; Asadabadi, E.B.; Jouni, F.J.; Karami, Z.; Firoozabadi, N.H. Elucidating the protein cold-adaptation: Investigation of the parameters enhancing protein psychrophilicity. J. Theor. Biol. 2008, 255, 113-118
Metpally, R.P.; Reddy, B.V. Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins. BMC Genomics 2009, 10, doi:10.1186/1471-2164-10-11
Russell, N.J. Molecular adaptations in psychrophilic bacteria: Potential for biotechnological applications. Adv. Biochem. Eng. Biotechnol. 1998, 61, 1-21
Margesin, R.; Schinner, F. Biotechnological Applications of Cold-adapted Organisms; Springer-Verlag: Berlin/Heidelberg, Germany, 1999
Gerday, C.; Aittaleb, M.; Bentahier, M.; Chessa, J.P.; Claverie, P.; Collins, T.; D'Amico, S.; Dumont, J.; Garsoux, G.; Georlette, D.; et al. Cold-adapted enzymes: From fundamentals to biotechnology. Trends Biotechnol. 2000, 18, 103-107
Allen, D.; Huston, A.L.; Weels, L.E.; Deming, J.W. Biotechnological Use of Psychrophiles. In Encyclopedia of Environmental Microbiology; Bitton, G., Ed.; John Wiley and Soons: New York, NY, USA, 2002; pp. 1-17
Cavicchioli, R.; Siddiqui, K.S.; Andrews, D.; Sowers, K.R. Low-temperature extremophiles and their applications. Curr. Opin. Biotechnol. 2002, 13, 253-261
Marx, J.C.; Collins, T.; D'Amico, S.; Feller, G.; Gerday, C. Cold-adapted enzymes from marine Antarctic microorganisms. Mar. Biotechnol. 2007, 9, 293-304
Cavicchioli, R.; Charlton, T.; Ertan, H.; Mohd Omar, S.; Siddiqui, K.S.; Williams, T.J. Biotechnological uses of enzymes from psychrophiles. Microb. Biotechnol. 2011, 4, 449-460
Bioprospecting Information Resource, United Nations University: Tokyo, Japan. Available online: http://www.bioprospector.org/bioprospector/ (accessed on 14 September 2012).
Kobori, H.; Sullivan, C.W.; Shizuya, H. Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5' end labelling of nucleic acids. Proc. Natl. Acad. Sci. USA 1984, 81, 6691-6695
Rina, M.; Pozidis, C.; Mavromatis, K.; Tzanodaskalaki, M.; Kokkinidis, M.; Bouriotis, V. Alkaline phosphatase from the Antarctic strain TAB5. Properties and psychrophilic adaptations. Eur. J. Biochem. 2000, 267, 1230-1238
Wang, E.; Koutsioulis, D.; Leiros, H.K.; Andersen, O.A.; Bouriotis, V.; Hough, E.; Heikinheimo, P. Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5. J. Mol. Biol. 2007, 366, 1318-1331
Koutsioulis, D.; Wang, E.; Tzanodaskalaki, M.; Nikiforaki, D.; Deli, A.; Feller, G.; Heikinheimo, P.; Bouriotis, V. Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase. Protein Eng. Des. Sel. 2008, 21, 319-327
Babu, J.; Ramteke, P.W.; Thomas, G. Cold active microbial lipases: Some hot issues and recent developments. Biotechnol. Adv. 2008, 26, 457-470
Lohan, D.; Johnston, S. UNU-IAS Report: Bioprospecting in Antarctica, 2005. Available online: http://www.ias.unu.edu/binaries2/antarctic_bioprospecting.pdf (accessed on 14 September 2014).
Davail, S.; Feller, G.; Narinx, E.; Gerday, C. Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41. J. Biol. Chem. 1994, 269, 17448-17453
Van Petegem, F.; Collins, T.; Meuwis, M.A.; Gerday, C.; Feller, G.; Van Beeumen, J. The structure of a cold-adapted family 8 xylanase at 1.3 Å resolution. Structural adaptations to cold and investigation of the active site. J. Biol. Chem. 2003, 278, 7531-7539
Collins, T.; de Vos, D.; Hoyoux, A.; Savvides, S.N.; Gerday, C.; Van Beeumen, J.; Feller, G. Study of the active site residues of a glycoside hydrolase family 8 xylanase. J. Mol. Biol. 2005, 354, 425-435
De Vos, D.; Collins, T.; Nerinckx, W.; Savvides, S.N.; Claeyssens, M.; Gerday, C.; Feller, G.; Van Beeumen, J. Oligosaccharide binding in family 8 glycosidases: Crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product. Biochemistry 2006, 45, 4797-4807
Collins, T.; Hoyoux, A.; Dutron, A.; Georis, J.; Genot, B.; Dauvrin, T.; Arnaut, F.; Gerday, C.; Feller, G. Use of glycoside hydrolase family 8 xylanases in baking. J. Cereal Sci. 2006, 43, 79-84
Wintrode, P.L.; Arnold, F.H. Temperature adaptation of enzymes: Lessons from laboratory evolution. Adv. Protein Chem. 2000, 55, 161-225
Siddiqui, K.S.; Cavicchioli, R. Improved thermal stability and activity in the cold-adapted lipase B from Candida antarctica following chemical modification with oxidized polysaccharides. Extremophiles 2005, 9, 471-476
Siddiqui, K.S.; Parkin, D.M.; Curmi, P.M.; de Francisci, D.; Poljak, A.; Barrow, K.; Noble, M.H.; Trewhella, J.; Cavicchioli, R. A novel approach for enhancing the catalytic efficiency of a protease at low temperature: Reduction in substrate inhibition by chemical modification. Biotechnol. Bioeng. 2009, 103, 676-686
Siddiqui, K.S.; Poljak, A.; Cavicchioli, R. Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives. Cell. Mol. Biol. 2004, 50, 657-667.