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Volume 2013 (2013), Article ID 512840, 28 pages
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 [11 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.
- Kalpana Hiteshi, and Reena Gupta, “Thermal adaptation of α-amylases: a review,” Extremophiles, 2014.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.