About this Journal Submit a Manuscript Table of Contents
Scientifica
Volume 2013 (2013), Article ID 512840, 28 pages
http://dx.doi.org/10.1155/2013/512840
Review Article

Psychrophilic Enzymes: From Folding to Function and Biotechnology

Laboratory of Biochemistry, Centre for Protein Engineering, Institute of Chemistry, University of Liège, B6a, 4000 Liège, Belgium

Received 18 October 2012; Accepted 6 November 2012

Academic Editors: S. Bottomley and A. P. Malykhina

Copyright © 2013 Georges Feller. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Citations to this Article [22 citations]

The following is the list of published articles that have cited the current article.

  • L. E. Petrovskaya, K. A. Novototskaya-Vlasova, E. A. Kryukova, E. M. Rivkina, D. A. Dolgikh, and M. P. Kirpichnikov, “Cell surface display of cold-active esterase EstPc with the use of a new autotransporter from Psychrobacter cryohalolentis K5T,” Extremophiles, 2014. View at Publisher · View at Google Scholar
  • Kalpana Hiteshi, and Reena Gupta, “Thermal adaptation of α-amylases: a review,” Extremophiles, 2014. View at Publisher · View at Google Scholar
  • Jan Kjølhede Vester, Mikkel Andreas Glaring, and Peter Stougaard, “An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment,” Applied Microbiology and Biotechnology, 2014. View at Publisher · View at Google Scholar
  • Nor Hafizah Ahmad Kamarudin, Raja Noor Zaliha Raja Abd. Rahman, Mohd Shukuri Mohamad Ali, Thean Chor Leow, Mahiran Basri, and Abu Bakar Salleh, “A New Cold-Adapted, Organic Solvent Stable Lipase from Mesophilic Staphylococcus epidermidis AT2,” The Protein Journal, vol. 33, no. 3, pp. 296–307, 2014. View at Publisher · View at Google Scholar
  • Virender Kumar, Poornima Yedavalli, Vishal Gupta, and Nalam Madhusudhana Rao, “Engineering lipase A from mesophilic Bacillus subtilis for activity at low temperatures,” Protein Engineering Design & Selection, vol. 27, no. 3, pp. 73–82, 2014. View at Publisher · View at Google Scholar
  • Daisuke Mitsuya, Shun-ichi Tanaka, Hiroyoshi Matsumura, Naoto Urano, Kazufumi Takano, Kyoko Ogasahara, Michiyo Takehira, Katsuhide Yutani, and Masami Ishida, “Strategy for cold adaptation of the tryptophan synthase alpha subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties,” Journal of Biochemistry, vol. 155, no. 2, pp. 73–82, 2014. View at Publisher · View at Google Scholar
  • Maria Giuliani, Ermenegilda Parrilli, Filomena Sannino, Gennaro Antonio Apuzzo, Gennaro Marino, and Maria Luisa Tutino, “Recombinant production of a single-chain antibody fragment in Pseudoalteromonas haloplanktis TAC125,” Applied Microbiology and Biotechnology, vol. 98, no. 11, pp. 4887–4895, 2014. View at Publisher · View at Google Scholar
  • Jonathan Maiangwa, Mohd Shukuri Mohamad Ali, Abu Bakar Salleh, Raja Noor Zaliha Raja Abd Rahman, Fairolniza Mohd Shariff, and Thean Chor Leow, “Adaptational properties and applications of cold-active lipases from psychrophilic bacteria,” Extremophiles, 2014. View at Publisher · View at Google Scholar
  • L. N. Ramya, and K. K. Pulicherla, “Molecular insights into cold active polygalacturonase enzyme for its potential application in food processing,” Journal of Food Science and Technology, 2014. View at Publisher · View at Google Scholar
  • Sebastiana Angelaccio, Martino Luigi di Salvo, Alessia Parroni, Angela Di Bello, Roberto Contestabile, and Stefano Pascarella., “STRUCTURAL STABILITY OF COLD-ADAPTED SERINE HYDROXYMETHYLTRANSFERASE, A TOOL FOR β-HYDROXY-α-AMINO ACID BIOSYNTHESIS,” Journal of Molecular Catalysis B: Enzymatic, 2014. View at Publisher · View at Google Scholar
  • Pik Mun Foong, Roghayeh Abedi Karjiban, Yahaya M. Normi, Abu Bakar Salleh, and Mohd Basyaruddin Abdul Rahman, “Bioinformatics survey of the metal usage by psychrophilic yeast Glaciozyma antarctica PI12,” Metallomics, vol. 7, no. 1, pp. 156–164, 2014. View at Publisher · View at Google Scholar
  • Emanuele Bosi, Marco Fondi, Isabel Maida, Elena Perrin, Donatella de Pascale, Maria Luisa Tutino, Ermenegilda Parrilli, Angelina Lo Giudice, Alain Filloux, and Renato Fani, “Genome-scale phylogenetic and DNA composition analyses of Antarctic Pseudoalteromonas bacteria reveal inconsistencies in current taxonomic affiliation,” Hydrobiologia, 2015. View at Publisher · View at Google Scholar
  • Mikyoung Ji, Callie V. Barnwell, and Amy M. Grunden, “Characterization of recombinant glutathione reductase from the psychrophilic Antarctic bacterium Colwellia psychrerythraea,” Extremophiles, 2015. View at Publisher · View at Google Scholar
  • Swati Bajaj, and Dileep K. Singh, “Biodegradation of persistent organic pollutants in soil, water and pristine sites by cold-adapted microorganisms: Mini review,” International Biodeterioration & Biodegradation, vol. 100, pp. 98–105, 2015. View at Publisher · View at Google Scholar
  • Euiyoung Bae, Sojin Moon, and George N. Phillips, “Molecular dynamics simulation of a psychrophilic adenylate kinase,” Journal Of The Korean Society For Applied Biological Chemistry, vol. 58, no. 2, pp. 209–212, 2015. View at Publisher · View at Google Scholar
  • Skander Elleuche, Farah M. Qoura, Ute Lorenz, Torben Rehn, Thomas Brück, and Garabed Antranikian, “Cloning, expression and characterization of the recombinant cold-active type-I pullulanase from Shewanella arctica,” Journal of Molecular Catalysis B: Enzymatic, 2015. View at Publisher · View at Google Scholar
  • Anna Bujacz, Maria Rutkiewicz-Krotewicz, Karolina Nowakowska-Sapota, and Marianna Turkiewicz, “Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychroba,” Acta Crystallographica Section D-Biological Crystallography, vol. 71, pp. 632–645, 2015. View at Publisher · View at Google Scholar
  • Kjersti Lian, Hanna-Kirsti S. Leiros, and Elin Moe, “MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability,” FEBS Open Bio, 2015. View at Publisher · View at Google Scholar
  • Sepideh Parvizpour, Jafar Razmara, Ashraf Fadhil Jomah, Mohd Shahir Shamsir, and Rosli Mohd Illias, “Structural prediction of a novel laminarinase from the psychrophilic Glaciozyma antarctica PI12 and its temperature adaptation analysis,” Journal of Molecular Modeling, vol. 21, no. 3, 2015. View at Publisher · View at Google Scholar
  • Laura J. Raiger Iustman, Paula M. Tribelli, Jose G. Ibarra, Mariela V. Catone, Esmeralda C. Solar Venero, and Nancy I. Lopez, “Genome sequence analysis of Pseudomonas extremaustralis provides new insights into environmental adaptability and extreme conditions resistance,” Extremophiles, vol. 19, no. 1, pp. 207–220, 2015. View at Publisher · View at Google Scholar
  • Jan Kjolhede Vester, Mikkel Andreas Glaring, and Peter Stougaard, “Improved cultivation and metagenomics as new tools for bioprospecting in cold environments,” Extremophiles, vol. 19, no. 1, pp. 17–29, 2015. View at Publisher · View at Google Scholar
  • Gabriel Zamith Leal Dalmaso, Davis Ferreira, and Alane Beatriz Vermelho, “Marine Extremophiles: A Source of Hydrolases for Biotechnological Applications,” Marine Drugs, vol. 13, no. 4, pp. 1925–1965, 2015. View at Publisher · View at Google Scholar