Effects of Trehalose on Pressure-Induced Inactivation of Yeast Alcohol Dehydrogenase

Title: Effects of Trehalose on Pressure-Induced Inactivation of Yeast Alcohol Dehydrogenase

Volume: 12 Issue: 6

Author(s): Hyun Park, Gene Kidman and Dexter B. Northrop

Affiliation:

Keywords: yeast alcohol dehydrogenase, trehalose, hydrostatic pressure, protein denaturation, barostability, thermostability, surface tension

Abstract: Isozymes of yeast alcohol dehydrogenase are slowly denatured at moderate hydrostatic pressures ( < 3 kbar). The time courses for inactivation are biphasic and both phases of both isozymes are protected by trehalose. ADH-I is slightly more barostable than ADH-II which is opposite to their thermostabilities. Trehalose at 1M extends their halflives about 6-fold at 2 kbar, pH 7.5 and 25°C. In contrast, 1M sucrose provides only 4.4-fold protection under identical conditions, a finding consistent with the superior protein stabilization of trehalose to other denaturants.

Cite this article as:

Park Hyun, Kidman Gene and Northrop B. Dexter, Effects of Trehalose on Pressure-Induced Inactivation of Yeast Alcohol Dehydrogenase, Protein & Peptide Letters 2005; 12 (6) . https://dx.doi.org/10.2174/0929866054395824

DOI https://dx.doi.org/10.2174/0929866054395824	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305