Thermal gelation of globulin from Phaseolus angularis (red bean)

Abstract

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°C, and both the storage modulus (G′) and loss modulus (G″) increased rapidly during cooling. The addition of NaCl at lower concentrations led to increases in G′ and G″ values, with decreased creep compliance, suggesting higher viscoelasticity. At higher salt concentrations, viscoelasticity was decreased, and the optimum NaCl concentration to produce maximum gel rigidity was 0.2 M. Sodium dodecyl sulfate and urea caused more pronounced reduction of the gel moduli than dithiothreitol and N-ethylmaleimide. The data suggest that hydrophobic interactions and hydrogen bonding play an important role in heat-induced gelation, while electrostatic interactions and a balance of attractive-repulsive forces are also important. The gels formed at 95°C exhibited a homogenous microstructure with extensive cross-links and sheet-like network structures. © 2002 Elsevier Science Ltd. All rights reserved.