Hydrolyzing behaviors of endogenous proteases on proteins in sesame milk and application for producing low-phytate sesame protein hydrolysate

•Hydrolysis behaviors of endogenous proteases on sesame milk proteins were examined.•Endogenous proteases randomly cleaved the cleavable peptide bonds on 11S globulins.•Cleavage specificity of serine carboxypeptidases on sesame proteins was clarified.•Lipids and proteins in hydrolyzed sesame milk were easily separated by centrifugation.•Low-phytate sesame protein hydrolysate with good solubility was obtained. Endogenous proteases with high activity have been identified in sesame seeds. However, the hydrolyzing behaviors of endogenous proteases on proteins in sesame milk are not well understood. In this study, the endogenous proteases optimally hydrolyzed proteins at pH 4.5 and 50 °C for 6 h. Tricine–sodium dodecyl sulphate–polyacrylamide gel electrophoresis and liquid chromatography tandem mass spectrometry analyses revealed that endogenous proteases randomly cleaved the cleavable peptide bonds on 11S globulins, and amino acid analysis indicated that serine carboxypeptidases preferentially cleaved tryptophan, phenylalanine, methionine, tyrosine, and leucine. The hydrolyzed sesame milk was separated into cream, transparent skim, and precipitate fractions by centrifugation (3000g, 5 min). The major protein components in skim were 42% peptides (