Bibliographic citations
Villasante, N., (2022). Purificación de péptidos bioactivos, con actividades antioxidante, antihipertensiva e hipoglucemiante in vitro, a partir del Tarwi (Lupinus mutabilis) [Universidad Nacional Agraria La Molina]. https://hdl.handle.net/20.500.12996/5561
Villasante, N., Purificación de péptidos bioactivos, con actividades antioxidante, antihipertensiva e hipoglucemiante in vitro, a partir del Tarwi (Lupinus mutabilis) []. PE: Universidad Nacional Agraria La Molina; 2022. https://hdl.handle.net/20.500.12996/5561
@mastersthesis{renati/248428,
title = "Purificación de péptidos bioactivos, con actividades antioxidante, antihipertensiva e hipoglucemiante in vitro, a partir del Tarwi (Lupinus mutabilis)",
author = "Villasante Bravo, Naysha",
publisher = "Universidad Nacional Agraria La Molina",
year = "2022"
}
The objective of this research was to concentrate and purify the peptides of a tarwi protein hydrolyzate (HPT), employing ultrafiltration techniques and gel filtration chromatography, based on their antioxidant activity (AA) and antihypertensive properties (inhibition of the enzyme converting angiotensin I, ACE) and hypoglycemic (inhibition of the enzyme dipeptidyl peptidase IV, DPP-IV) through the measurement of its IC50 value, as well as its characterization at the molecular weight level employing SDS-PAGE electrophoresis. The hydrolyzate was obtained from the hydrolysis in two stages of the tarwi protein with the enzymes Alcalase (60 min) followed by Neutrase (180 min) at 50 ºC. HPT after ultrafiltration using 10 and 3 kDa cut-off membranes, resulted in a permeate < 3 kDa with AA values of 1.89 μmol TE/mg protein and IC50 values for ACE and DPP IV of 0.11 mg/ mL and 3.71 mg/mL, respectively. The permeate passing through gel filtration chromatography, using Biogel P-2, was divided into a total of four fractions (F I - F IV), where the last fraction (F IV) exhibited the highest AA (6.41 μmol TE/ g protein) and low IC50 value for ACE and DPP-IV (0.06 and 0.32 mg/mL, respectively). After electrophoresis, the peptides that make up the last two fractions; F III and F IV, showed molecular weight ranges, which ranged from the lowest, from ~ 15 kDa to < 1kDa, which would justify the best values achieved in the antioxidant, antihypertensive and hypoglycemic properties, evaluated, highlighting fraction IV. The results obtained indicate that the evaluated tarwi protein hydrolyzate has multifunctional peptides, and can be considered in its whole or purified form as a potential natural ingredient in the production of functional foods and/or nutraceuticals.
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