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

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

Journal Name: Protein & Peptide Letters

Volume 12 , Issue 6 , 2005

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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.

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

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Article Details

VOLUME: 12
ISSUE: 6
Year: 2005
Page: [597 - 599]
Pages: 3
DOI: 10.2174/0929866054395824
Price: $65

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