Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant alpha-amylase

Article Abstract:

The genuine properties of a psychrophilic enzyme are retained when expressed in a mesophilic host, as long as the culture temperature is low enough to allow correct folding and to prevent irreversible denaturation. This was gleaned from a study of the folding state of a recombinant alpha-amylase, where the heat-labile alpha-amylase from the antarctic psychrophile Alteromonas haloplanktis was expressed in Escherichia coli at various temperatures. The heat-labile alpha-amylase folds correctly when overexpressed in E. coli.

Gene expression, Protein folding, Amylases

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The beta-lactamase secreted by the antarctic psychrophile Psychrobacter immobilis A8

Article Abstract:

The antarctic bacteria Psychrobacter immobilis produces a beta-lactamase that has a low level of thermal stability and is active at low temperatures. At temperatures less than 10 degrees celsius, the activity of the beta-lactamase is similar to that of mesophilic class C beta-lactamases. The secretion of the enzyme is probably an ancestral protective method against bacteriolytic microorganisms that produce metabolites from beta-lactam.

Natural history, Antarctic regions, Beta lactamases

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Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis

Article Abstract:

Researchers describe a beta-galactosidase from an Antarctic bacterium that is similar to the E. coli enzyme but can operate at lower temperatures. This enzyme can outperform beta-galactosidase from Kluyveromyces marxianus var. lactis and could be used to process dairy products in refrigerated plants.

Microbial enzymes, Psychrotrophic organisms, Psychrotrophic microorganisms

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