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Title: Protein inactivation in amorphous sucrose and trehalose matrices: Effects of phase separation and crystallization
Authors: Sun, W.Q. 
Davidson, P.
Keywords: Crystallization
Desiccation tolerance
Glass transition
Phase separation
Protein preservation
Issue Date: 16-Sep-1998
Citation: Sun, W.Q., Davidson, P. (1998-09-16). Protein inactivation in amorphous sucrose and trehalose matrices: Effects of phase separation and crystallization. Biochimica et Biophysica Acta - General Subjects 1425 (1) : 235-244. ScholarBank@NUS Repository.
Abstract: Trehalose is the most effective carbohydrate in preserving the structure and function of biological systems during dehydration and subsequent storage. We have studied the kinetics of protein inactivation in amorphous glucose/sucrose (1:10, w/w) and glucose/trehalose (1:10, w/w) systems, and examined the relationship between protein preservation, phase separation and crystallization during dry storage. The glucose/trehalose system preserved glucose-6-phosphate dehydrogenase better than did the glucose/sucrose system with the same glass transition temperature (T(g)). The Williams-Landel-Ferry kinetic analysis indicated that the superiority of the glucose/trehalose system over the glucose/sucrose system was possibly associated with a low free volume and a low free volume expansion at temperatures above the T(g). Phase separation and crystallization during storage were studied using differential scanning calorimetry, and three separate domains were identified in stored samples (i.e., sugar crystals, glucose-rich and disaccharide-rich amorphous domains). Phase separation and crystallization were significantly retarded in the glucose/trehalose system. Our data suggest that the superior stability of the trehalose system is associated with several properties of the trehalose glass, including low free volume, restricted molecular mobility and the ability to resist phase separation and crystallization during storage. Copyright (C) 1998 Elsevier Science B.V.
Source Title: Biochimica et Biophysica Acta - General Subjects
ISSN: 03044165
DOI: 10.1016/S0304-4165(98)00076-2
Appears in Collections:Staff Publications

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