Papain Hydrolysates of Lupin Proteins with Antioxidant, Antimicrobial, and Acetylcholinesterase Inhibitory Activities

Dietary proteins are no longer just nutritional ingredients in our food. During hydrolysis, some of the released peptides may possess properties that favor health human body. In study enzymatic hydrolysis lupin was performed using papain. Three enzyme-to-substrate ratios were set for three different duration times. The SDS-PAGE samples performed. Each hydrolysate studied degree (DH), acetylcholinesterase (AChE) inhibitory, antimicrobial, and antioxidant activities (AOA, according to four spectrophotometric methods). DH varied from 9.06 ± 0.20 27.97 0.37%. According results, best AOA measured by ABTS method (from 0.76 0.03 1.15 0.46 M TE/100 g protein). All hydrolysates displayed AChE inhibitory activity (IC50), which between 155.58 1.87 199.63 0.41 mg/g protein. To knowledge, this is first report protein hydrolysates. conclusion, prove have a high potential serve as source bioactive peptides.