Abstract

The antioxidant activity of bioactive peptides obtained from hydrolyzed mung bean (Vidna radiata) grown in Espinal Tolima was evaluated. Alkaline hydrolysis was performed with 1 N NaOH. Mung bean protein concentrate obtained was 82%. The enzymatic hydrolysis was performed using a randomized block design, with commercial enzymes: Alcalase®, trypsin® and Flavourzyme®. The kinetics of the hydrolysis degree (DH) was measured based on time. The factor evaluated was the reaction time in minutes and the response variable was the degree of hydrolysis (DH), which was 43.21% for Alcalase, 41.20% for Trypsin and 38.41% for Flavourzyme. Two experiments used for measuring the antiradical activity in vitro were positive for the three types of enzymes. The optimal antiradical capacity was obtained at 30 min for Alcalase and Trypsin, and 45 min, respectively for Flavourzyme. Antioxidant activity in vitro such as, ABTS, DPPH, ORAC and FRAC correlated with the in vivo assays. Mung bean hydrolysates could have antioxidant effects, a good alternative when incorporated into diet, as a dietary supplement or added to a food matrix. Key words: Antioxidant, bioactive peptides, hydrolyses, mung bean.

Highlights

  • Enzymatic protein hydrolysates have been used to improve the functional properties of food products, formulate pharmaceuticals in specific clinical application, and obtain bioactive peptides (Torruco-Uco et al, 2008)

  • Some researchers suggested an intake between 3.0 to 5.0 Oxygen radical absorbance capacity (ORAC)/day, in order to promote oxidative balance in blood plasma and body tissues (Prior et al, 2003; Rojano et al, 2012).mung bean hydrolysates could be a good alternative when incorporated into diet, either in the form of encapsulation or added to food matrix

  • The degree of enzymatic hydrolysis (%degree of hydrolysis (DH)) of protein concentrates mung beans grown in the municipality of Espinal Tolima was more efficient with Alcalase and trypsin at 30 min with values of 43.21 and 41.29%, compared to 45 min used for Flavourzyme enzyme where a value of 38.45% was obtained

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Summary

INTRODUCTION

Enzymatic protein hydrolysates have been used to improve the functional properties of food products, formulate pharmaceuticals in specific clinical application, and obtain bioactive peptides (Torruco-Uco et al, 2008). Where: %ABTS is ABTS radical stabilizing activity, expressed as a percentage; AABTS is absorbance of ABTS+ before adding the sample; A6min is absorbance of the reaction mixture at 6 min. 50 50 μL of sample was added to 900 μL of a solution of FRAP (acetic acid –sodium acetate, pH 3.4 Buffer acid, TPTZ, FeCl3, in 10:1: 1), after 30 min of reaction the absorbance was determined at a wavelength of 593 nm. This value was compared with the reference curve constructed with ascorbic acid as a primary standard, and the results were expressed as ascorbic acid equivalents (AEAC). Ab control is absorbance of control in this case ascorbic acid is used; hydrolyzed Ab is absorbance of the sample, in this case the hydrolysates

RESULTS AND DISCUSSION
Evaluation of antioxidant activity in vitro
Conclusion
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