Effects of cluster dextrin encapsulation on the properties and antioxidant stability of fractionated Riceberry protein hydrolysate powder prepared by bromelain.

In this work, the biological properties of fractionated Riceberry bran protein hydrolysate obtained by ultrafiltration (URBPH) were evaluated and the possibility of using cluster dextrin to produce hydrolysate powder by spray-drying was investigated. Fractionation into peptides < 3 kDa was observed to improve antioxidant activity. URBPH < 3 kDa was then freeze-dried (FD-URBPH) and spray-dried (SD-URBPH) at different inlet air temperatures of 100-160 °C.

Functional Characterization of Mung Bean Meal Protein-Derived Antioxidant Peptides.

The aim of this work was to characterize the antioxidant properties of some of the peptides present in bromelain mung bean meal protein hydrolysate (MMPH). The MMPH was subjected to two rounds of bioassay-guided reversed-phase HPLC separation followed by peptide identification in the most potent fractions using tandem mass spectrometry. Twelve antioxidant peptides, namely, HC, CGN, LAN, CTN, LAF, CSGD, MMGW, QFAAD, ERF, EYW, FLQL, and QFAW were identified and assayed for antioxidant properties.

Assessment of antioxidant properties of membrane ultrafiltration peptides from mungbean meal protein hydrolysates.

Background: Bioactive peptides can prevent damage associated with oxidative stress in humans when consumed regularly. Recently, peptides have attracted immense interest because of their beneficial functional properties, safety and little or no side effects when used at high concentration. Most antioxidant peptides are small in size, less than 1 kDa, and contains a high proportion of hydrophobic amino acid.

Volatile flavour compounds, sensory characteristics and antioxidant activities of mungbean meal protein hydrolysed by bromelain.

Enzymatic mungbean meal protein hydrolysate (eb-MPH) is a novel natural flavour/antioxidant source. A 15% bromelain (w/w) concentration with a hydrolysis time of 12 h was the optimum conditions to produce eb-MPH, which showed the greatest antioxidant activities and sensory characteristics. eb-MPH was composed of oligopeptides that had low molecular weight (< 10 kDa) as well as surface hydrophobicity and high content of hydrophobic amino acids.

Physicochemical and flavor characteristics of flavoring agent from mungbean protein hydrolyzed by bromelain.

Enzymatic bromelain mungbean meal protein hydrolysate (eb-MPH) was produced from mungbean meal protein isolate (MPI). Enzymatic bromelain, with a known protease activity of 98,652 (unit/g), was used at concentrations of 0, 2, 6, 10, 14 and 18% (w/w) and with hydrolysis times of 0.5, 3, 6, 12, and 24 h.