Thermal aggregation and gelation of kidney bean (Phaseolus vulgaris L.) protein isolate at pH 2.0: Influence of ionic strength

Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels

“…The width of flexible fibrils was nearly 10 nm, and the contour length was 650 nm or more after heating for 2 h. Intermolecular electrostatic repulsion plays a dominant role in the fibril formation process caused by a large decrease in fibril flexibility. The successive growth of fibrils caused changes in morphology (12). In a previous study, kidney bean protein (phaseolin) fibrils were observed to exhibit similar phenomena (16), perhaps as an indication of conformational changes during fibril formation.…”

“…Under conditions of low salt and a high protein charge density, gels are transparent or semitransparent. Microscopy shows that these gels consist of thin branched strands or aggregated proteins (12,13). When the net charge density is close to neutral, or at a high salt concentration, turbid coarse gels are formed consisting of dense protein domains (13).…”

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

“…It could be found that the kinetics of collagen self-assembly could be modulated by NaCl concentration. The diameter of collagen fibril formed in 60 mM of NaCl concentration was larger than that in others, different from the result that particle size of the formed aggregates in heated kidney bean protein isolate increased with the increase in ionic strength from 0 to 300 mM (Zhang et al, 2010). On increasing NaCl concentration, there was an increase of the nucleation time, as revealed in Fig.…”

Functional and physicochemical properties of pulse proteins

“…Based on data obtained by applying oscillatory rheometry, these workers concluded that the gel elasticity and strength parameters depend on NaCl or CaCl 2 content. Zhang et al (2010) investigated the thermal gelation at an acidic pH of a protein isolate obtained from kidney bean, as influenced by ionic strength. According to these investigators, the gelation behavior of kidney bean proteins is influenced to a marked extent by the ionic strength, with the extent of protein aggregation and storage moduli increasing and the LGC decreasing as the ionic strength is increased from 0 to 300 mM (Fig.…”