Improving antioxidant activity of black bean protein by hydrolysis with protease combinations

Abstract

This study explored the use of a simplex centroid design to produce protein hydrolysates with antioxidant properties using Alcalase Ò 2.4L, Flavourzyme Ò 500L and Neutrase Ò 0.8L. Proteases kinetic parameters and the ultrafiltration of protein hydrolysates were also investigated. The highest antioxidant activity, in the studied conditions, was reached when the mixture of Alcalase Ò 2.4L and Flavourzyme Ò 500L was used in the hydrolysates production. The antioxidant power of the black bean proteins, measured by the total antioxidant capacity and reducing power assay, increased after hydrolysis by 31% and 70%, respectively. The black bean proteins hydrolysates fractions (3-30 kDa) showed an antioxidant activity decrease along with a reduction in molecular weight, demonstrating that a set of varied molecular weight peptides was responsible for the antioxidant characteristics of black bean protein hydrolysates.

Enzymatic hydrolysis of black cricket (Gryllus assimilis) proteins positively affects their antioxidant properties

“…Alcalase TM 2.4L is a B. licheniformis serine protease that contains subtilisin endoproteinase activity and high specificity for cleavage of aromatic amino acids (Pimentel, Alves, Harnedy, FitzGerald, & Oliveira, 2019; Waglay & Karboune, 2016). Neutrase TM 0.8L is an endoprotease that has high affinity for hydrophobic amino acids (Aguilar et al., 2019), and can promote (as well as Alcalase TM 2.4L) an increase in the number of target sites available for the Flavourzyme TM 500L action, which justifies the synergistic effect of the ternary combination of the applied proteases (Nchienzia, Morawicki, & Gadang, 2010).…”

“…Aguilar et al. (2019) studied the effects of the addition of the substrate (black bean protein concentrate) to the enzyme Neutrase TM 0.8L and observed that the half‐life time of the enzyme was reduced from 100.46 to 87.74 min, which may affect the formation of bioactive peptides.…”

“…The protease activity was determined according to the method proposed by Charney and Tomarelli (1947) and described by Aguilar, Cason, and De Castro (2019). A reaction mixture containing 0.25 mL of 1% azocasein, 0.25 mL of 0.1 mol/L phosphate buffer (pH 7), and 0.5 mL of enzyme solution was incubated for 40 min at 50 °C.…”

Effects of thermal processing on antioxidant activities, amino acid composition and protein molecular weight distributions of jasmine rice bran protein hydrolysate

“…It is well known that thermal treatments can cause thermoxidation of compounds, causing the degradation of antioxidant substances and a subsequent decrease in antioxidant activity (Korczek et al, 2020). In addition, black bean protein hydrolysate showed that the high-MW (>30 kDa) fraction had higher DPPH radical-scavenging activity than the small-MW (10 kDa) fraction (Aguilar et al, 2019). However, the small-size peptides of Zizyphus jujube hydrolysate showed the high activity of DPPH expressed by EC 50 0.6 and 0.5 mg mL À1 , respectively (Memarpoor-Yazdi et al, 2013).…”

Current understanding of bioaccessibility and bioavailability of food‐derived bioactive peptides

“…Food protein-derived peptides have been recognised as an important category of functional food materials, which exert various bioactivities and possible health-promoting impacts in human beyond their traditional nutritional values (Hern andez-Ledesma & Hsieh, 2017;Aguilar et al, 2019). Bioactive peptides could be produced by food processing processes such as fermentation, etc., from longer polypeptides or proteins.…”