Heat-induced reversible gelation of arachin: kinetics, thermodynamics and protein species involved in the process.
IR@CSIR-CFTRI
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Relation |
http://ir.cftri.com/2357/
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Title |
Heat-induced reversible gelation of arachin: kinetics, thermodynamics and protein species involved in the process.
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Creator |
Kella, N. K. D.
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Subject |
03 Proteins
33 Nuts |
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Description |
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.
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Date |
1989
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Type |
Article
PeerReviewed |
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Format |
pdf
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Language |
en
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Identifier |
http://ir.cftri.com/2357/1/Int.%20J.%20Biol.%20Macromol.%2C%201989%2C%20Vol.%2011%2C%20April%20105.pdf
Kella, N. K. D. (1989) Heat-induced reversible gelation of arachin: kinetics, thermodynamics and protein species involved in the process. International Journal of Biological Macromolecules, 11 (2). pp. 105-12. ISSN 0141-8130 |
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