Literature DB >> 17195087

Cold-adapted enzymes from marine Antarctic microorganisms.

J-C Marx1, T Collins, S D'Amico, G Feller, C Gerday.   

Abstract

The Antarctic marine environment is characterized by challenging conditions for the survival of native microorganisms. Indeed, next to the temperature effect represented by the Arrhenius law, the viscosity of the medium, which is also significantly enhanced by low temperatures, contributes to slow down reaction rates. This review analyses the different challenges and focuses on a key element of life at low temperatures: cold-adapted enzymes. The molecular characteristics of these enzymes are discussed as well as the adaptation strategies which can be inferred from the comparison of their properties and three-dimensional structures with those of their mesophilic counterparts. As these enzymes display a high specific activity at low and moderate temperatures associated with a relatively high thermosensitivity, the interest in these properties is discussed with regard to their current and possible applications in biotechnology.

Mesh:

Year:  2006        PMID: 17195087     DOI: 10.1007/s10126-006-6103-8

Source DB:  PubMed          Journal:  Mar Biotechnol (NY)        ISSN: 1436-2228            Impact factor:   3.619


  66 in total

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Review 4.  Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.

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  36 in total

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5.  Activity and community structures of sulfate-reducing microorganisms in polar, temperate and tropical marine sediments.

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7.  Is cold the new hot? Elevated ubiquitin-conjugated protein levels in tissues of Antarctic fish as evidence for cold-denaturation of proteins in vivo.

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10.  Influence of production process design on inclusion bodies protein: the case of an Antarctic flavohemoglobin.

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