Abstract
Z-potential measurements of aqueous crayfish protein isolate (CFPI) dispersions were carried out to determinate isoelectric point. Gels were prepared by heating CFPI dispersions at 90 °C for 30 min. Solubility and electrophoresis of CFPI and CFPI gels, extracted using different extraction media, were studied. Gels were characterised by linear viscoelasticity, water-holding capacity and SEM techniques. Results confirm that myofibrillar proteins play an important role, where a matrix is stabilized mainly by disulfide bonds, hydrophobic interactions and hydrogen bonds. Similar pH profiles obtained for CFPI dispersions (solubility and Z-potential measurements) and CFPI gels (solubility, linear viscoelasticity and water holding capacity) were obtained. SEM images provide information consistent with those pH profiles.
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