Abstract
Abstract The limited enzymatic hydrolysis gelation method was investigated using peanut protein isolate (PPI) without any coagulators. A peanut protein gel could be formed by enzyme treatment with Alcalase at low temperature (50–70 °C). The influence of enzymatic hydrolysis on the rheological and physicochemical properties was investigated. Structural changes in the PPI were characterized by analyzing the subunits, chemical forces, surface hydrophobicity, fluorescence spectra, and circular dichroism (CD) spectra. The results revealed that enzymatic hydrolysis significantly affected the conarachin II protein of PPI, and had little influence on conarachin I and the basic subunits of arachin. Hydrophobic interaction was the main chemical force active in the peanut protein gel. An increase in the surface hydrophobicity coupled with red-shifts of the fluorescence spectra indicated that inner hydrophobic regions were exposed after hydrolysis, resulting in gel formation via hydrophobic interactions. The CD spectra showed that significant changes occurred in the secondary structure of PPI, where the ordered PPI structure formed a more open structure after enzymatic hydrolysis.
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