Literature DB >> 1445404

Enzymes from thermophilic archaebacteria: current and future applications in biotechnology.

D A Cowan1.   

Abstract

The one guaranteed property of enzymes isolated from extremely thermophilic micro-organisms is their thermostability. Most significantly, almost any such enzyme will be more thermostable than the functionally similar enzyme from a lower temperature source. Thermostability is not an isolated property: resistance to heat denaturation imparts stability to a number of other denaturing influences (detergents, organic solvents, etc). These characteristics of hyperthermophilic enzymes are the most likely basis for the development of new biotechnological applications. A limited number of hyperthermophilic enzymes have found application in specialist biotechnological applications; others have visible potential in growing areas of biotechnology. Existing and potential applications are discussed using DNA manipulation enzymes, dehydrogenases, and esterases as examples.

Mesh:

Year:  1992        PMID: 1445404

Source DB:  PubMed          Journal:  Biochem Soc Symp        ISSN: 0067-8694


  7 in total

1.  The thermophilic esterase from Archaeoglobus fulgidus: structure and conformational dynamics at high temperature.

Authors:  S D'Auria; P Herman; J R Lakowicz; E Bertoli; F Tanfani; M Rossi; G Manco
Journal:  Proteins       Date:  2000-03-01

Review 2.  Proteins from extremophiles as stable tools for advanced biotechnological applications of high social interest.

Authors:  Marcella de Champdoré; Maria Staiano; Mosè Rossi; Sabato D'Auria
Journal:  J R Soc Interface       Date:  2007-04-22       Impact factor: 4.118

3.  Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents.

Authors:  C Kujo; T Ohshima
Journal:  Appl Environ Microbiol       Date:  1998-06       Impact factor: 4.792

4.  The esterase from the thermophilic eubacterium Bacillus acidocaldarius: structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus fulgidus.

Authors:  S D'Auria; P Herman; J R Lakowicz; F Tanfani; E Bertoli; G Manco; M Rossi
Journal:  Proteins       Date:  2000-08-15

5.  Characterization and Low-Resolution Structure of an Extremely Thermostable Esterase of Potential Biotechnological Interest from Pyrococcus furiosus.

Authors:  F Mandelli; T A Gonçalves; C A Gandin; A C P Oliveira; M Oliveira Neto; F M Squina
Journal:  Mol Biotechnol       Date:  2016-11       Impact factor: 2.695

6.  An autonomously replicating transforming vector for Sulfolobus solfataricus.

Authors:  R Cannio; P Contursi; M Rossi; S Bartolucci
Journal:  J Bacteriol       Date:  1998-06       Impact factor: 3.490

7.  Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.

Authors:  R M Alldread; D M Halsall; A R Clarke; T K Sundaram; T Atkinson; M D Scawen; D J Nicholls
Journal:  Biochem J       Date:  1995-01-15       Impact factor: 3.857

  7 in total

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