Literature DB >> 9634802

Extremozymes: expanding the limits of biocatalysis.

M W Adams1, F B Perler, R M Kelly.   

Abstract

The study of enzymes isolated from organisms inhabiting unconventional ecosystems has led to the realization that biocatalysis need not be constrained to mild conditions and can be considered at pH's, temperatures, pressures, ionic and solvent environments long thought to be destructive to biomolecules. Parallel to this, it has been demonstrated that even conventional enzymes will catalyze reactions in solvents other than water. However, the intrinsic basis for biological function under extreme conditions is only starting to be addressed, as are associated applications. This was the focus of a recent NSF/NIST-sponsored workshop on extremozymes. Given the information acquired from the study of extremozymes, modification of enzymes to improve their ranges of stability and activity remains a possibility. Ultimately, by expanding the range of conditions suitable for enzyme function, new opportunities to use biocatalysis will be created.

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Year:  1995        PMID: 9634802     DOI: 10.1038/nbt0795-662

Source DB:  PubMed          Journal:  Biotechnology (N Y)        ISSN: 0733-222X


  31 in total

1.  Biochemical and phylogenetic analyses of a cold-active beta-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA.

Authors:  J M Coombs; J E Brenchley
Journal:  Appl Environ Microbiol       Date:  1999-12       Impact factor: 4.792

2.  Genetic diversity of archaea in deep-sea hydrothermal vent environments.

Authors:  K Takai; K Horikoshi
Journal:  Genetics       Date:  1999-08       Impact factor: 4.562

Review 3.  Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.

Authors:  C Vieille; G J Zeikus
Journal:  Microbiol Mol Biol Rev       Date:  2001-03       Impact factor: 11.056

4.  Extrinsic factors potassium chloride and glycerol induce thermostability in recombinant anthranilate synthase from Archaeoglobus fulgidus.

Authors:  W Malcolm Byrnes; Vincent L Vilker
Journal:  Extremophiles       Date:  2004-07-02       Impact factor: 2.395

5.  Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea.

Authors:  Leanne M Timpson; Diya Alsafadi; Cillín Mac Donnchadha; Susan Liddell; Michael A Sharkey; Francesca Paradisi
Journal:  Extremophiles       Date:  2011-10-21       Impact factor: 2.395

6.  Site-directed mutagenesis of a family 42 β-galactosidase from an antarctic bacterium.

Authors:  Matthew V Shumway; Peter P Sheridan
Journal:  Int J Biochem Mol Biol       Date:  2012-05-18

7.  Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.

Authors:  T C Cheng; V Ramakrishnan; S I Chan
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

8.  Proteolysin, a novel highly thermostable and cosolvent-compatible protease from the thermophilic bacterium Coprothermobacter proteolyticus.

Authors:  Ana Toplak; Bian Wu; Fabrizia Fusetti; Peter J L M Quaedflieg; Dick B Janssen
Journal:  Appl Environ Microbiol       Date:  2013-07-12       Impact factor: 4.792

Review 9.  Life in hot acid: pathway analyses in extremely thermoacidophilic archaea.

Authors:  Kathryne S Auernik; Charlotte R Cooper; Robert M Kelly
Journal:  Curr Opin Biotechnol       Date:  2008-09-11       Impact factor: 9.740

10.  Characterization of Di-myo-Inositol-1,1(prm1)-Phosphate in the Hyperthermophilic Bacterium Thermotoga maritima.

Authors:  V Ramakrishnan; M Verhagen; M Adams
Journal:  Appl Environ Microbiol       Date:  1997-01       Impact factor: 4.792

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