Bibliographic citations
Ochoa, K., (2017). Hidrólisis enzimática en una y dos etapas de la proteína de la cañihua Chenopodium pallidicaule Aellen., para obtener péptidos bioactivos [Tesis, Universidad Nacional Agraria La Molina]. https://hdl.handle.net/20.500.12996/3055
Ochoa, K., Hidrólisis enzimática en una y dos etapas de la proteína de la cañihua Chenopodium pallidicaule Aellen., para obtener péptidos bioactivos [Tesis]. : Universidad Nacional Agraria La Molina; 2017. https://hdl.handle.net/20.500.12996/3055
@mastersthesis{renati/248679,
title = "Hidrólisis enzimática en una y dos etapas de la proteína de la cañihua Chenopodium pallidicaule Aellen., para obtener péptidos bioactivos",
author = "Ochoa Pachas, Karina Guadalupe",
publisher = "Universidad Nacional Agraria La Molina",
year = "2017"
}
In this study, protein hydrolysates with bioactive potential antihypertensive and antioxidant capacity were extracted from cañihua flour (79.38 %, p/p) by enzymatic hydrolysis using commercial enzymes Alcalase® (endoprotease), Neutrasa® (endoprotease) and Flavourzyme® (protease/peptidase complex) in one and two stages. The highest degrees of hydrolysis (DH) were obtained 240 minutes for reactions in one step with Alcalase and Neutrase with 42.82 and 35.96 values percent, respectively; whereas Flavourzyme’s values were low (9.63 percent). A significant increase in DH was obtained combining enzymes (two stage reactors) Alcalase/Flavourzyme and Alcalase/Neutrase with 46.76 and 60.28 values percent respectively combined. The antioxidant capacity (CAOX) ABTS+ in vitro increased with GH protein, yielding the highest values with two stage reactor method, where combinations Alcalase/Neutrase and Alcalase/Flavourzyme gave values ABTS+ in the range of 3 and 3.50 mol equivalent trolox (TE)/mg protein, respectively. IC50 values depended mainly on the type of enzyme or the mixture of enzymes used, with the DH directly related to the CAOX. The best results were obtained with the combination of Neutrase/Alcalase enzymes (180 min) reaching an IC50 of 0.12 mg of protein/ml, to this condition a DH of 42.19 percent and an ABTS+ value of 2.46 μmol TE/mg protein was obtained. When assessing the stability of the hydrolyzate against gastrointestinal conditions using an in vitro model (sequential hydrolysis with pepsin and pancreatin), an IC50 of 0.07 mg / ml protein was obtained, indicating that the peptides show stability in the assay conditions
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