Abstract
Dietary proteins are no longer just nutritional ingredients in our food. During hydrolysis, some of the released peptides may possess properties that favor the health of the human body. In our study enzymatic hydrolysis of lupin proteins was performed using papain. Three enzyme-to-substrate ratios were set for three different duration times. The SDS-PAGE of the samples was performed. Each hydrolysate was studied for the degree of hydrolysis (DH), acetylcholinesterase (AChE) inhibitory, antimicrobial, and antioxidant activities (AOA, according to four spectrophotometric methods). The DH varied from 9.06 ± 0.20 to 27.97 ± 0.37%. According to the results, the best AOA was measured by the ABTS method (from 0.76 ± 0.03 to 1.15 ± 0.46 M TE/100 g protein). All the hydrolysates displayed AChE inhibitory activity (IC50), which varied between 155.58 ± 1.87 and 199.63 ± 0.41 mg/g protein. To the best of our knowledge, this is the first report of the acetylcholinesterase inhibitory activity of lupin protein hydrolysates. In conclusion, lupin proteins prove to have a high potential to serve as a source of bioactive peptides.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
