Background:
The animal blood that is produced in a slaughterhouse is a potential source
of inexpensive proteins used in the food industry around the world. However, 60% of it is surplus,
and it ends with a negative environmental impact.
Introduction:
The enzymatic hydrolysis of proteins represents a good way to produce peptides with
different biological activities.
Methods:
Enzymatic hydrolysis of bovine plasma with subtilisin at an alkaline pH and 61.5°C was
performed using the pH-stat method. Experiments were conducted considering the effects of a high
initial substrate concentration (So) and the enzyme/substrate ratio (E/S) minimizing the processing
time necessary to obtain a specific degree of hydrolysis (DH).
Results:
The best conditions obtained were 42 g/L of So and 0.89 AU/g substrate of E/S until a DH
of 20% in 11,1 ± 1,1 min was achieved to the tested conditions, which result in a fitted empirical
polynomial equation of degree 3.
Conclusion:
A kinetic equation is established to relate the DH and the reaction time to a relative error
of less than 5% in the fit, to obtain a good antioxidant product in an industrially interesting time.
Additionally, the results suggest a good adjustment of the data with a determination coefficient (R2)
of 0.9745 in validation.
Iron deficiencies continue to cause significant health problems in vulnerable populations. A good strategy to combat mineral deficiency includes fortification with iron-binding peptides. This research aims to determine the optimal conditions to hydrolyze red tilapia viscera (RTV) using Alcalase 2.4 L and recovery of iron-binding protein hydrolysate. The result showed that under the optimal hydrolysis condition including pH 10, 60 °C, E/S ratio of 0.306 U/g protein, and substrate concentration of 8 g protein/L, the obtained hydrolysate with 42.5% degree of hydrolysis (RTVH-B), displayed the maximal iron-binding capacity of 67.1 ± 1.9%. Peptide fractionation was performed using ultrafiltration and the <1 kDa fraction (FRTVH-V) expressed the highest iron-binding capacity of 95.8 ± 1.5%. Iron content of RTVH-B and its fraction was assessed, whereas iron uptake was measured indirectly as ferritin synthesis in a Caco-2 cell model and the result showed that bioavailability of bound minerals from protein complexes was significantly higher (p < 0.05) than iron salt in its free form, increased 4.7 times for the Fe2+–RTVH-B complex. This research suggests a potential application of RTVH-B as dietary supplements to improve iron absorption.
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