Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0304-4165(98)00077-4
Title: Protein stability in the amorphous carbohydrate matrix: relevance to anhydrobiosis
Authors: Sun, W.Q. 
Davidson, P.
Chan, H.S.O. 
Keywords: Anhydrobiosis
Carbohydrate
Desiccation tolerance
Glass transition
Protein stability
Seed longevity
Vigna radiata
Issue Date: 16-Sep-1998
Citation: Sun, W.Q., Davidson, P., Chan, H.S.O. (1998-09-16). Protein stability in the amorphous carbohydrate matrix: relevance to anhydrobiosis. Biochimica et Biophysica Acta - General Subjects 1425 (1) : 245-254. ScholarBank@NUS Repository. https://doi.org/10.1016/S0304-4165(98)00077-4
Abstract: The formation of intracellular glass is proposed to be relevant to protein stabilization and survival of anhydrobiotic organisms in the dry state. The stability of proteins in the amorphous carbohydrate matrix and its relevance to seed survival have been investigated in the present study. Glucose-6-phosphate dehydrogenase (G6PDH) was preserved in the amorphous glucose/sucrose (1:10, w/w) matrix by freeze-drying. The stability of freeze-dried G6PDH was examined at temperatures above and below the glass transition temperature (T(g)). The rate of G6PDH inactivation in the amorphous carbohydrate matrix deviated significantly from the Arrhenius kinetics, and conformed to the Williams-Landel-Ferry (WLF) relationship. The temperature dependence of G6PDH inactivation in two sets of samples with different T(g) values was compared. Identical temperature dependence of G6PDH inactivation was observed after temperature normalization by (T-T(g)). Seed survival of Vigna radiata Wilczek (mung bean) showed a similar WLF kinetics at storage temperatures T≥T(g). In situ protein stability in mung bean embryonic axes was studied using differential scanning calorimetry (DSC). Thermal stability of seed proteins exhibited a strong dependence on the T(g) of intracellular glass. These results indicate an important role of the glassy state in protein stabilization. Our data suggest an association between protein stability in intracellular glass and seed survival during storage. Copyright (C) 1998 Elsevier Science B.V.
Source Title: Biochimica et Biophysica Acta - General Subjects
URI: http://scholarbank.nus.edu.sg/handle/10635/76833
ISSN: 03044165
DOI: 10.1016/S0304-4165(98)00077-4
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