Wq. Sun et al., PROTEIN STABILITY IN THE AMORPHOUS CARBOHYDRATE MATRIX - RELEVANCE TOANHYDROBIOSIS, Biochimica et biophysica acta (G). General subjects, 1425(1), 1998, pp. 245-254
The formation of intracellular glass is proposed to be relevant to pro
tein 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 prese
nt study. Glucose-6-phosphate dehydrogenase (G6PDH) was preserved in t
he 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 inact
ivation in the amorphous carbohydrate matrix deviated significantly fr
om the Arrhenius kinetics, and conformed to the Williams-Landel-Ferry
(WLF) relationship. The temperature dependence of G6PDH inactivation i
n two sets of samples with different T-g values was compared. Identica
l temperature dependence of G6PDH inactivation was observed after temp
erature normalization by (T-T-g). Seed survival of Vigna radiata Wilcz
ek (mung bean) showed a similar WLF kinetics at storage temperatures T
greater than or equal to T-g. In situ protein stability in mung bean
embryonic axes was studied using differential scanning calorimetry (DS
C), Thermal stability of seed proteins exhibited a strong dependence o
n 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. (C) 1998 Elsevier Science B.V. All rights re
served.