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Biotechnological Aspects of Cold-Adapted Enzymes

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Psychrophiles: from Biodiversity to Biotechnology

Beginning with the development of basic tools by our hominid predecessors, humanshave continually searched for and utilized novel materials from the natural environment to survive and thrive. Today, our knowledge of the surrounding world extends to themolecular scale as we enter the age of genomics and systems biology, enabling previously unimaginable insight into processes that promise application in the agricultural, energy, food, medical, structural material and textile industries. As environmental concerns arise, biological tools are increasingly replacing harsh chemical and physical means of processing materials and they even harbor promise for creating cost-effective sustainable energy sources. It is imperative that we continue investigating ways in which natural products can offer economical alternatives to traditional industrial processes. Due to the growing and wide-spread use of enzymes in a variety of industrial applications, this review aims to build on previous works (Brenchley 1996; Ohgiya et al. 1999; Gerday et al. 2000; Allen et al. 2001; Cavicchioli et al. 2002) by illustrating recent advances and potential opportunities for the biotechnological application of cold-adapted enzymes.

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References

  • Allen D, Huston AL, Wells LE, Deming JW (2001) Biotechnological use of psychrophiles. In Bitton G (ed) Encyclopedia of environmental microbiology. Wiley, New York, pp 1–17.

    Google Scholar 

  • Arnold FH, Wintrode PL, Miyazaki K, Gershenson A (2001) How enzymes adapt: lessons from directed evolution. Trends Biochem Sci 26:100–106.

    Article  CAS  PubMed  Google Scholar 

  • Asenjo JA, Andrews BA, Reyes F, Salamanca M, Burzio L (2006) Protein and nucleic acid sequence encoding a krill-derived cold adapted trypsin-like activity enzyme. Patent No. WO2006022947.

    Google Scholar 

  • Bansal V, Rautaray D, Ahmad A, Sastry M (2004) Biosynthesis of zirconia nanoparticles using the fungus Fusarium oxysporum. J Mater Chem 14:3303–3305.

    Article  CAS  Google Scholar 

  • Benesova E, Markova M, Kralova B (2005) B-glucosidase and–glucosidase from psychrotrophic strain Arthrobacter sp C2–2. Czech J Food Sci 23:116–120.

    CAS  Google Scholar 

  • Bentahir M, Feller G, Aittaleb M, Lamotte-Brasseur J, Himri T, Chessa J-P, Gerday C (2000) Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the Antarctic Pseudomonas sp. TACII18. J Biol Chem 275:11147–11153.

    Article  CAS  PubMed  Google Scholar 

  • Bjarnason JB, Benediktsson B (2001) Protein hydrolysates produced with the use of marine proteases. Patent No. WO0128353.

    Google Scholar 

  • Bordusa F (2002) Proteases in organic synthesis. Chem Rev 102:4817–4867.

    Article  CAS  PubMed  Google Scholar 

  • Brenchley JE (1996) Psychrophilic microorganisms and their cold-active enzymes. J Indust Microbiol 17:432–437.

    Article  CAS  Google Scholar 

  • Brenchley JE, Loveland-Curtze J, Gutshall K, Humphrey V (2001) Stain removing compositions containing particular isolated and pure proteolytic enzymes. Patent No. US6326346.

    Google Scholar 

  • Brutchey RL, Yoo ES, Morse DE (2006) Biocatalytic synthesis of a nanostructured and crystalline bimetallic perovskite-like barium oxofluorotitanate at low temperature. J Am Chem Soc 128:10288–10294.

    Article  CAS  PubMed  Google Scholar 

  • Cavicchioli R (2006) Cold-adapted archaea. Nat Rev Microbiol 4:331–343.

    Article  CAS  PubMed  Google Scholar 

  • Cavicchioli R, Siddiqui KS, Andrews D, Sowers KR (2002) Low-temperature extremophiles and their applications. Curr Opin Biotechnol 13:253–161.

    Article  CAS  PubMed  Google Scholar 

  • Cha JN, Shimizu K, Zhou Y, Christiansen SC, Chmelka BF, Stucky GD, Morse DE (1999) Silicatein filaments and subunits from a marine sponge direct the polymerization of silica and silicones in vitro. Proc Natl Acad Sci USA 96:361–365.

    Article  CAS  PubMed  Google Scholar 

  • Cherry JR, Fidanstef AL (2003) Directed evolution of industrial enzymes: an update. Curr Opin Biotechnol 14:438–443.

    Article  CAS  PubMed  Google Scholar 

  • Coker JA, Brenchley JE (2006) Protein engineering of a cold-active ß-galactosidase from Arthrobacter sp. SB to increase lactose hydrolysis reveals new sites affecting low temperature activity. Extremophiles 10:515–524.

    Article  CAS  PubMed  Google Scholar 

  • Collins T, Hoyoux A, Dutron A, Georis J, Genot B, Dauvrin T, Arnaut F, Gerday C, Feller G (2006) Use of glycoside family 8 xylanases in baking. J Cereal Sci 43:79–84.

    Article  CAS  Google Scholar 

  • D’Amico S, Gerday C, Feller G (2001) Structural determinants of cold adaptation and stability in a large protein. J Biol Chem 276:25791–25796.

    Article  PubMed  Google Scholar 

  • D’Amico S, Marx J-C, Gerday C, Feller G (2003a) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278:7891–7896.

    Article  PubMed  Google Scholar 

  • D’Amico S, Gerday C, Feller G (2003b) Temperature adaptation of proteins: Engineering mesophilic-like activity and stability in a cold-adapted i-amylase. J Mol Biol 332:981–988.

    Article  PubMed  Google Scholar 

  • D’Amico S, Collins T, Marx J-C, Feller G, Gerday C (2006) Psychrophilic microorganisms: challenges for life. EMBO Reports 7:385–389.

    Article  PubMed  Google Scholar 

  • Deming JW (2002) Psychrophiles and polar regions. Curr Opin Microbiol 3:301–309.

    Article  Google Scholar 

  • DeVries R, Visser J (2001) Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol Mol Biol Rev 65:497–522.

    Article  CAS  Google Scholar 

  • Dutron A, Georis J, Dauvrin T, Collins T, Hoyoux A, Feller G (2005) Use of family 8 enzymes with xylanolytic activity in baking. Patent No. MXPA05002751.

    Google Scholar 

  • Felby C, Larsen D, Joergensen H, Vibe-Pederson J (2006) Enzymatic hydrolysis of biomasses having a high dry matter (DM) content. Patent No. WO2006056838.

    Google Scholar 

  • Feller G, Gerday C (2003) Psychrophilic enzymes: Hot topics in cold adaptation. Nat Rev Microbiol 1:200–208.

    Article  CAS  PubMed  Google Scholar 

  • Georlette D, Jonsson ZO, Van Petegem F, Chessa J-P, Van Beeumen J, Hubscher U, Gerday C (2000) A DNA ligase from psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur J Biochem 267:3502–3512.

    Article  CAS  PubMed  Google Scholar 

  • Gerday C, Aittaleb M, Arpigny JL, Baise E, Chessa J-P, Garsoux G, Perescu I, Feller G (1997) Psychrophilic enzymes: a thermodynamic challenge. Biochim Biophys Acta 1342:119–131.

    CAS  PubMed  Google Scholar 

  • Gerday C, Aittaleb M, Benhatir M, Chessa J-P, Claverie P, Collins T, D’Amico S, Dumont, J, Garsoux G, Georlette D, Hoyoux A, Lonhienne T, Meuwis M-A, Feller G (2000) Cold-adapted enzymes: from fundamentals to biotechnology. TIBTECH 18:103–107.

    CAS  Google Scholar 

  • Gerday C, Hoyoux A, Francois J-M, Dubois P, Baise E, Jennes I, Genicot S (2005) Cold-active ß-galactosidase, the process for its preparation and the use thereof. Patent No. US2005196835.

    Google Scholar 

  • Gerike U, Danson MJ, Hough DW (2001) Cold-active citrate synthase: mutagenesis of active-site residues. Protein Eng 14:655–661.

    Article  CAS  PubMed  Google Scholar 

  • Giovannoni SJ, Britschgi TB, Moyer CL, Field KG (1990) Genetic diversity in Sargasso sea bacterioplankton. Nature 345:60–63.

    Article  CAS  PubMed  Google Scholar 

  • Hasan AKMQ, Tamiya E (1997) Cold-active protease CP-58 and psychrotrophic bacteria. Patent No. WO9730172.

    Google Scholar 

  • Hasan AKMQ, Tamiya E (1998) Cold-active protease CP70. Patent No. US6200793.

    Google Scholar 

  • He H, Chen XL, Li JW, Zhang YZ, Gao PJ (2004) Taste improvement of refrigerated meat treated with cold-adapted protease. Food Chem 84:307–311.

    Article  CAS  Google Scholar 

  • Karasova-Lipovova P, Strnad H, Spiwok V, Mala S, Kralova B, Russell NJ (2003) The cloning, purification and characterization of a cold-active t-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2–2. Enzyme Microb Technol 33:836–844.

    Article  CAS  Google Scholar 

  • Kisailus D, Choi JH, Weaver JC, Yang W, Morse DE (2005) Enzymatic synthesis and nanostructural control of gallium oxide at low temperature. Adv Mater 17:314–318.

    Article  CAS  Google Scholar 

  • Kisailus D, Truong Q, Amemiya Y, Weaver JC, Morse DE (2006) Self-assembled bifunctional surface mimics an enzymatic and templating protein for the synthesis of a metal oxide semiconductor. Proc Natl Acad Sci USA 103:5652–5657.

    Article  CAS  PubMed  Google Scholar 

  • Krishna, SH (2002) Developments and trends in enzyme catalysis in nonconventional media. Biotech Adv 20:239–267.

    Article  Google Scholar 

  • Kulakova L, Galkin A, Nakayama T, Nishino T, Esaki N (2003) Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. Strain Ac10 by rational mutagenesis. J Mol Catal B Enzymatic 22:113–117.

    Article  CAS  Google Scholar 

  • Li JK, Lee TC (1995) Bacterial ice nucleation and its potential application in the food industry. Trends Food Sci Technol 6:259–265.

    Article  CAS  Google Scholar 

  • Lin Y, Tanaka S (2006) Ethanol fermentation from biomass resources; current state and prospects. Appl Microbiol Biotechnol 69:627–642.

    Article  CAS  PubMed  Google Scholar 

  • Lonhienne T, Gerday C, Feller G (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim Biophys Acta 1543:1–10.

    CAS  PubMed  Google Scholar 

  • Lonhienne T, Zoidakis J, Vorgias CE, Feller G, Gerday C, Bouriotis V (2001) Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium. J Mol Biol 310:291–297.

    Article  CAS  PubMed  Google Scholar 

  • Lorenz P, Liebeton K, Niehaus F, Eck J (2002) Screening for novel enzymes for biocatalytic processes: accessing the metagenome as a resource of novel functional sequence space. Curr Opin Biotechnol 13:572–577.

    Article  CAS  PubMed  Google Scholar 

  • Margesin R, Feller G, Gerday C, Russell N (2002) Cold-adapted microorganisms: adaptation strategies and biotechnological potential. In Bitton G (ed) The encyclopedia of environmental microbiology. Wiley, New York, pp 871–885.

    Google Scholar 

  • Mavromatis K, Feller G, Kokkinidis M, Bouriotis V (2003) Cold adaptation of a psychrophilic chitinase: a mutagenesis study. Protein Eng 16:497–503.

    Article  CAS  PubMed  Google Scholar 

  • Michel V, Lehoux I, Depret G, Anglade P, Labadie J, Hebraud M (1997) The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid binding proteins. J Bacteriol 23:7331–7342.

    Google Scholar 

  • Miyazaki K, Wintrode PL, Grayling RA, Rubingh DN, Arnold FH (2000) Directed evolution study of temperature adaptation in a psychrophilic enzyme. J Mol Biol 297:1015–1026.

    Article  CAS  PubMed  Google Scholar 

  • Muryoi N, Sato M, Kaneko S, Kawahara H, Obata h, Yaish MW, Griffith M, Glick BR (2004) Cloning and expression of afpA, a gene encoding an antifreeze protein from the arctic plant growth-promoting rhizobacterium Pseudomonas putida GF12–2. J Bacteriol 186:5661–5671.

    Article  CAS  PubMed  Google Scholar 

  • Nakagawa T, Nagaoka T, Taniguchi S, Miyaji T, Tomizuka N (2004) Isolation and characterization of psychrophilic yeasts producing cold-adapted pectinolytic enzymes. Lett Appl Microbiol 38:383–387.

    Article  CAS  PubMed  Google Scholar 

  • Narinx E, Baise E, Gerday C (1997) Subtilisin from psychrophilic Antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng 10:1271–1279.

    Article  CAS  PubMed  Google Scholar 

  • Nichols CM, Lardiere SG, Bowman JP, Nichols PD, Gibson JAE, Guezennec J (2005) Chemical characterization of exopolysaccharides from Antarctic marine bacteria. Microb Ecol 49:578–589.

    Article  CAS  PubMed  Google Scholar 

  • Novozymes (2005) Presentation from the ninth chemical industry finance and investments conference. URL: http://www.novozymes.com/NR/rdonlyres/64054ABC-F525–4B62–A1EB-5BBE6A55468E/0/Chemicals_Conference_ML_2005.pdf.

  • Ohgiya S, Hoshino T, Okuyama H, Tanaka S, Ishizaki K (1999) Biotechnology of enzymes from cold-adapted microorganisms. In: Margesin R, Schinner F (eds) Biotechnological applications of cold-adapted organisms. Springer, Berlin, pp 17–34.

    Google Scholar 

  • Ohtani N, Haruki M, Morikawa M, Kanaya S (2001) Heat labile ribonuclease HI from a psychrotrophic bacterium: gene cloning, characterization and site-directed mutagenesis. Protein Eng 14:975–982.

    Article  CAS  PubMed  Google Scholar 

  • Owusu-Apenten RK (1999) Low temperature organic phase biocatalysis using cold-adapted enzymes. In: Margesin R, Schinner F (eds) Biotechnological applications of cold-adapted organisms. Springer, Berlin, pp 35–48.

    Google Scholar 

  • Panasik N (2002) Structural basis for thermostability and thermal dependence of activity in P// barrel glycosyl hydrolases. PhD Thesis, Pennsylvania State University, USA.

    Google Scholar 

  • Peck LS (2002) Ecophysiology of Antarctic marine ectotherms: limits to life. Polar Biol 25:31–40.

    Article  Google Scholar 

  • Pomeroy LR, Wiebe WJ (2001) Temperature and substrates as interactive limiting factors for marine heterotrophic bactera. Aquat Microb Ecol 23:187–204.

    Article  Google Scholar 

  • Rasmussen BF, Stock AM, Rings D, Petsko GA (1992) Crystallin ribonuclease A loses function below the dynamical transition at 220 K. Nature 357:423–424.

    Article  CAS  PubMed  Google Scholar 

  • Rina M, Pozidis C, Mavromatis K, Tzanodaskalaki M, Kokkinidis M, Bouriotis V (2000) Alkaline phosphatase from the Antarctic strain TAB5. Eur J Biochem 267:1230–1238.

    Article  CAS  PubMed  Google Scholar 

  • Robertson GH, Wong DWS, Lee CC, Wagschal K, Smith MR, Orts WJ (2006) Native or raw starch digestion: a key step in energy efficient biorefining of grain. J Agric Food Chem 54: 353–365.

    Article  CAS  PubMed  Google Scholar 

  • Russell NJ (1997) Psychrophilic bacteria-molecular adaptations of membrane lipids. Comp Biochem Physiol Physiol 118:489–493.

    Article  CAS  Google Scholar 

  • Schoemaker HE, Mink E, Wubbolts MG (2003) Dispelling the myths—biocatalysis in industrial synthesis. Science 299:1694–1697.

    Article  CAS  PubMed  Google Scholar 

  • Sellek GA, Chaudhuri JB (1999) Biocatalysis in organic media using enzymes from extremophiles. Enzyme Microb Technol 25:471–482.

    Article  CAS  Google Scholar 

  • Senapati S, Ahmad A, Khan MI, Sastry M, Kumar R (2005) Extracellular biosynthesis of bimetallic Au-Ag alloy nanoparticles. Small 5:517–520.

    Article  Google Scholar 

  • Shahidi F, Kamil YVAJ (2001) Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol 12:435–464.

    Article  Google Scholar 

  • Shetty JK, Lantero OJ, Dunn-Colemen N (2005) Technological advances in ethanol production. Int Sugar J 107:605.

    CAS  Google Scholar 

  • Shimizu K, Cha J, Stucky GD, Morse DE (1998) Silicatein h: Cathespin L-like protein in sponge biosilica. Proc Natl Acad Sci USA 95:6234–6238.

    Article  CAS  PubMed  Google Scholar 

  • Stinson SC (1998) Counting on chiral drugs. Chem Eng News 76:83–96.

    Google Scholar 

  • Suen W-C, Zhang N, Xiao L, Madison V, Zaks A (2004) Improved activity and thermostability of Candida antarctica lipase B by DNA family shuffling. PEDS 17:133–140.

    CAS  PubMed  Google Scholar 

  • Sumerel JL, Yang W, Kisailus D, Weaver JC, Choi JH, Morse DE (2003) Biocatalytically templated synthesis of titanium oxide. Chem Mater 15:4804–4809.

    Article  CAS  Google Scholar 

  • Tahir MN, Eberhardt M, Therese HA, Kolb U, Theato P, Muller WEG, S H-C, Tremel W (2006) From single molecules to nanoscopically structured functional materials: Au nanocrystal growth on TiO2 nanowires controlled by surface-bound silicatein. Angew Chem Int Ed 45:4803–4809.

    Article  CAS  Google Scholar 

  • Takaiwa M, Saeki K, Okuda M, Kobayashi T, Ito S, Kubota H, Ota Y, Fujimori N (1997) Cold alkaline protease, microorganism producing the same, process for producing the same, and detergent compositions and food processing enzyme preparations containing the same. Patent No. WO9743406.

    Google Scholar 

  • Trytek M, Fiedurek J (2005) A novel psychrotrophic fungus, Mortierella minutissima, for D-limonene biotransformation. Biotechnol Lett 27:149–153.

    Article  CAS  PubMed  Google Scholar 

  • van den Burg B (2003) Extremophiles as a source for novel enzymes. Current Opin Microbiol 6:213–218.

    Article  Google Scholar 

  • Wells LE, Deming JW (2006) Characterization of a cold-active bacteriophage on two psychrophilic marine hosts. Aquat Microb Ecol 45:15–29.

    Article  Google Scholar 

  • Wyman CE (2003) Potential synergies and challenges in refining cellulosic biomass to fuels, chemicals, and power. Biotechnol Prog 19:254–262.

    Article  CAS  PubMed  Google Scholar 

  • Zecchinon L, Oriol A, Netzel U, Svennberg J, Gerardin-Otthiers N, Feller G (2005) Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphyglycerate kinase—A microcalorimetric study. J Biol Chem 280:41307–41314.

    Article  CAS  PubMed  Google Scholar 

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  1. 2006–2007 AAAS Science and Technology Policy Fellow, American Association for the Advancement of Science (AAAS), 1200 New York Avenue NW, Washington, DC 20005, USA

    Adrienne L. Huston

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  1. Institute of Microbiology, University of Innsbruck, Technikerstrasse 25, 6020, Innsbruck, Austria

    Rosa Margesin  & Franz Schinner  & 

  2. Laboratory of Biochemistry, University of Liège, Institute of Chemistry B6, 4000, Liège, Belgium

    Jean-Claude Marx  & Charles Gerday  & 

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Huston, A.L. (2008). Biotechnological Aspects of Cold-Adapted Enzymes. In: Margesin, R., Schinner, F., Marx, JC., Gerday, C. (eds) Psychrophiles: from Biodiversity to Biotechnology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-74335-4_20

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