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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 [8 citations]

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  • 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
  • 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