Multifunctional in vitro bioactive properties: Antioxidant, antidiabetic, and antihypertensive of protein hydrolyzates from tarwi (Lupinus mutabilis Sweet) obtained by enzymatic biotransformation

Abstract

Background and objectives Tarwi is a legume that grows in the Andean region of Peru. This grain is characterized by having a high protein content (~42%). In order to generate added‐value products from this resource, the possibility of obtaining tarwi protein hydrolyzates (TPH) with in vitro bioactive properties was evaluated using Alcalase, Neutrase, and Flavourzyme enzymes, acting alone or in combination for up to 240 min. The in vitro evaluated properties were as follows: antioxidant (ABTS assay), antidiabetic (α‐amylase, α‐glucosidase and dipeptidyl peptidase IV (DPP‐IV) inhibition), and antihypertensive (angiotensin‐converting enzyme‐I (ACE) inhibition). Findings The TPH obtained from the different enzyme treatments exhibited important antioxidant, antidiabetic (specially for DPP‐IV inhibition), and antihypertensive properties. One‐stage treatment using Alcalase for 240 min and two sequential stage treatments with Alcalase–Neutrase for 180 min presented the highest ABTS antioxidant activity and lowest IC50 values for DPP‐IV and ACE corresponding to 2.0–1.95 µmol TE/mg, 2.14–2.61 and 0.16–0.11 mg/ml, respectively. Conclusions The results of this research demonstrate that TPH exhibit in vitro multifunctional bioactive properties. Significance and novelty TPH could potentially be used in the prevention or management of chronic diseases related to the development of oxidative processes, diabetes, and hypertension.

Antioxidant, antihypertensive and antidiabetic potential of peptidic fractions obtained from tarwi (Lupinus mutabilis) protein hydrolysate and identification of promising multifunctional bioactive peptides

“…The quantity of HA was calculated by chromatographic analysis (at 228 nm) according to Chirinos et al . (2021). ACE inhibition was expressed as percentage.…”

“…Despite the nutritional benefits of the seed, it has a high alkaloid content, so before use, it must be de‐bitterised by soaking with water and heat treatment. Thus, recently tarwi has been explored as a potential source for obtaining protein hydrolysates with multifunctional properties: antioxidant, antidiabetic and antihypertensive, resorting to hydrolysis with commercial enzymes of microbial origin, generating very encouraging results (Chirinos et al ., 2021). Research carried out on tarwi protein hydrolysates have confirmed the antioxidant and inhibition of hepatic gluconeogenesis effects (Intiquilla et al ., 2018; Muñoz et al ., 2018), but studies on the structure and nature (size, type and sequence of amino acids and hydrophobicity) of its bioactive peptides are very limited.…”

Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides

“…The higher ABTS •+ radical scavenging capacity of the hydrolyzates obtained after the combined action of three enzymes (pepsin, pancreatin, and Alcalase) in comparison with those obtained only by pepsin could be due to the higher efficiency of the hydrolytic process. Thus, Chirinos et al reported the higher antioxidant activity of Alcalase-Flavourzyme hydrolyzates from tarwi ( Lupinus mutabilis ) than that of Alcalase hydrolyzates [ 37 ]. Similarly, other works have found higher ABTS •+ radical scavenging capacity of soybean [ 38 ], cañihua ( Chenopodium pallidicaule ) [ 39 ], and kiwicha ( Amaranthus caudatus ) [ 40 ] protein hydrolyzates using Alcalase combinations with other enzymes compared with only Alcalase.…”

“…Although this value was higher than that measured for Captopril, used as standard in this assay (6.81 µg/mL), it was much lower than those reported for hydrolyzates from other plant proteins. As examples, Alcalase-hydrolyzates of Lupinus angustifolius protein showed IC 50 values ranged from 100–210 µg protein/mL [ 45 ], and the tarwi protein hydrolyzate by an Alcalase-Neutrase combination for 180 min showed an IC 50 value of 110 µg protein/mL [ 37 ].…”

Application of enzymes in the preparation of wheat germ polypeptides and their biological activities

“…The antihypertensive activity of wheat germ was due to the ACE inhibitory peptide produced after hydrolysis of protein ( 75 ), and the dominant peptide of ACE inhibitory peptide was Ile-Val-Tyr (Ivy) ( 76 ). The activity of ACE obtained by different proteolytic methods was various ( 77 , 78 ). The activity of ACE inhibitory peptide in wheat germ enzymatic hydrolysate obtained by Qu et al ( 19 ) was 65.9%, while the activity of ACE inhibitory peptide in wheat germ enzymatic hydrolysate pretreated by Jia et al ( 41 ) ultrasonic increased by 21.0-40.7%.…”