BENISEED PROTEIN HYDROLYSATES DEMONSTRATE ANTIOXIDANT POTENTIALS AND INHIBIT ALBUMIN GLYCATION IN-VITRO
Abstract
The search for natural bioactive peptides with health-promoting properties has gained increasing attention due to the limitations of synthetic antioxidants and antiglycation agents. This study investigated the protein yield, degree of hydrolysis, antioxidant, and antiglycation activities of beniseed (Sesamum indicum) protein hydrolysates produced by enzymatic digestion with trypsin and chymotrypsin. Protein isolates were prepared using alkaline extraction and isoelectric precipitation, after which they were subjected to enzymatic hydrolysis. The resulting hydrolysates were analyzed for peptide yield, degree of hydrolysis, antioxidant properties using DPPH radical scavenging and FRAP assays, and antiglycation activity using bovine serum albumin glycation models. The protein yield obtained from beniseed seeds was 24.31%, confirming the seed as a rich source of plant proteins. Chymotrypsin hydrolysis produced a higher peptide yield and degree of hydrolysis compared to trypsin. However, trypsin hydrolysates demonstrated stronger antioxidant activity, with a DPPH scavenging capacity of 46.09 ± 0.56% at 2.5 mg/mL, surpassing chymotrypsin digests (p
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