TY - JOUR
T1 - Antioxidant, antihypertensive and antidiabetic potential of peptidic fractions obtained from tarwi (Lupinus mutabilis) protein hydrolysate and identification of promising multifunctional bioactive peptides
AU - Chirinos, Rosana
AU - Villasante-Bravo, Naysha
AU - Aguilar-Galvez, Ana
AU - Figueroa-Merma, Andrés
AU - Carpentier, Sebastien
AU - Pedreschi, Romina
AU - Campos, David
N1 - Publisher Copyright:
© 2022 Institute of Food, Science and Technology (IFSTTF).
PY - 2022/11
Y1 - 2022/11
N2 - Tarwi is an Andean grain, belonging to the legume group and is characterised by its high protein content, exceeding that reported in soybeans being an interesting resource for obtaining bioactive peptides. The tarwi protein hydrolysate (TPH) obtained by enzymatic hydrolysis with Alcalase (60 min) followed by Neutrase (120 min) presented important multifunctional properties to cope with oxidative stress, hypertension and diabetes. After concentration and purification process the most active fraction containing the highest antioxidant, antihypertensive (inhibition of angiotensin-converting enzyme I, ACE) and antidiabetic (inhibition of dipeptidyl peptidase IV, DPP IV) properties were found in the low-molecular weight peptide fraction. Thus, this last fraction was subjected to a de novo sequencing LC–MS/MS analysis yielding the identification of 25 peptides, with potential activities as ACE and DPP IV inhibitors and antioxidative according to BIOPEP database. Of these, four novel peptides: AVPFWM, YSGWLGL, AHAGFGMLY and FFSMKVM, stood out for their relatively high scores in bioactivity predicted by Peptide Ranker, additionally the structure–activity evaluation performed on them, supported the predicted antioxidant, antihypertensive and antidiabetic properties. These results demonstrated that TPH might be considered a potential source of peptides with multifunctional bioactive properties with possibilities of application in the food and nutraceutical sectors.
AB - Tarwi is an Andean grain, belonging to the legume group and is characterised by its high protein content, exceeding that reported in soybeans being an interesting resource for obtaining bioactive peptides. The tarwi protein hydrolysate (TPH) obtained by enzymatic hydrolysis with Alcalase (60 min) followed by Neutrase (120 min) presented important multifunctional properties to cope with oxidative stress, hypertension and diabetes. After concentration and purification process the most active fraction containing the highest antioxidant, antihypertensive (inhibition of angiotensin-converting enzyme I, ACE) and antidiabetic (inhibition of dipeptidyl peptidase IV, DPP IV) properties were found in the low-molecular weight peptide fraction. Thus, this last fraction was subjected to a de novo sequencing LC–MS/MS analysis yielding the identification of 25 peptides, with potential activities as ACE and DPP IV inhibitors and antioxidative according to BIOPEP database. Of these, four novel peptides: AVPFWM, YSGWLGL, AHAGFGMLY and FFSMKVM, stood out for their relatively high scores in bioactivity predicted by Peptide Ranker, additionally the structure–activity evaluation performed on them, supported the predicted antioxidant, antihypertensive and antidiabetic properties. These results demonstrated that TPH might be considered a potential source of peptides with multifunctional bioactive properties with possibilities of application in the food and nutraceutical sectors.
KW - Antidiabetic
KW - Lupinus mutabilis
KW - antihypertensive
KW - antioxidant
KW - bioactive peptides
KW - de novo sequencing
UR - http://www.scopus.com/inward/record.url?scp=85139009139&partnerID=8YFLogxK
U2 - 10.1111/ijfs.16100
DO - 10.1111/ijfs.16100
M3 - Article
AN - SCOPUS:85139009139
SN - 0950-5423
VL - 57
SP - 7402
EP - 7411
JO - International Journal of Food Science and Technology
JF - International Journal of Food Science and Technology
IS - 11
ER -