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The thermal aggregation behavior of red bean (Phaseolus angularis) globulin (RBG) was studied at ~1% (w/v) protein concentration in 0.01 M phosphate buffer, pH 7.4. The percentage of protein precipitated was affected by heating temperature, heating time and salt concentration. The influences of several salts of the chaotropic series and protein structure-modifying agents on thermal coagulation of...
The heat-induced gelation properties of red bean globulin (RBG) were studied under the influence of salts and several protein structure perturbants. The viscoelastic properties of the gels were evaluated by small amplitude oscillatory tests and creep experiments. Gel structure developed progressively when a protein dispersion (~10% w/v) was heated from 25 to 95<space> o C, and both the...
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