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- W2023182192 abstract "Arachin forms a heat-reversible gel under certain experimental conditions. The minimal gelling concentration for this system is 7.25%. Above minimal gelling concentration calculation of thermodynamic parameters for gelation of arachin revealed a constant delta Hbonding (-1220 cal.mol-1) where delta Sbonding values varied with an increase in protein concentration (ranging from -4.01 e.u. at 7.5% to -3.48 e.u. at 10.0%). The main steps involved in the gelation phenomenon include thermal denaturation of arachin, partial aggregation of heat-denatured protein molecules, setting of protein solution and maturation of the gel formed. Gel maturation process follows first order kinetics and is characterized by a large positive delta G+(+) (22,030 cal.mol-1). Determination of delta H+(+) and delta S+(+) for this process revealed that mostly delta S+(+) (-62.9 e.u.) contributes to the large positive delta G+(+), thus decreasing the overall rate of gel maturation process. This large negative delta S+(+) value probably arises from a loss of entropy of protein molecules because of their increased involvement in gel network formation. The polymer gel network seems to be primarily contributed by a part of both arachin dodecameric and hexameric species." @default.
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- W2023182192 date "1989-04-01" @default.
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- W2023182192 title "Heat-induced reversible gelation of arachin: kinetics, thermodynamics and protein species involved in the process" @default.
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- W2023182192 doi "https://doi.org/10.1016/0141-8130(89)90051-2" @default.
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