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KINETICS OF BEAN PROTEIN THERMAL DENATURATION
Author(s) -
HOHLBERG A.I.,
STANLEY D.W.
Publication year - 1987
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/j.1745-4549.1987.tb00034.x
Subject(s) - denaturation (fissile materials) , activation energy , differential scanning calorimetry , chemistry , kinetics , enthalpy , kinetic energy , order of reaction , phaseolus , thermal analysis , chromatography , thermal , thermodynamics , analytical chemistry (journal) , reaction rate constant , nuclear chemistry , botany , physics , quantum mechanics , biology
A kinetic model for the thermal denaturation of the 7S protein of common black beans (Phaseolus vulgaris) was developed. Thermal analysis was performed on hydrated (9:1) solutions of the proteins with a differential scanning calorimeter (DSC). Kinetic parameters were obtained by analyzing peaks in the DSC thermogram using the Borchardt and Daniels method. Denaturation temperature for 10% solutions increased from 382 to 387°K when increasing the heating rate from 5 to 30°C/min, while the enthalpy was steady at about 0.4J/g solution. The reaction order for phaseolin denaturation was found to be close to 2.5, with an activation energy of 932 KJ/mol and a pre‐exponetial factor of 127 min −1 . A critical evaluation of the peak temperature versus heating rate method revealed that the former method was less appropriate and accurate for determining the activation energy of protein denaturation.