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. The water solubility and antioxidant activity of FD-URBPH were higher than those of SD-URBPH. Nevertheless, encapsulation of hydrolysate with 10% cluster dextrin and an inlet temperature of 120 °C was also successful in maintaining protein qualities, which showed high 2,2'-azino-bis 3-ethylbenzthiazoline-6-sulfonic (ABTS•+) scavenging activity (89.14%) and water solubility index (92.49%) and low water activity (aw = 0.53). Moreover, encapsulation preserved the antioxidant activity of peptides during gastrointestinal digestion better than the free form. URBPH and its spray-dried microcapsules could be used as bioactive ingredients in functional drinks or foods.

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. CTN, HC, CGN, and CSGD were the most potent (p < 0.05) DPPH radical scavengers with EC50 values of 0.30, 0.29, 0.28, and 0.30 mg/mL, respectively, which are lower than the 0.03 mg/mL obtained for reduced glutathione (GSH). CTN, HC, CGN, and CSGD exhibited the most potent (p < 0.05) scavenging activities against hydroxyl and superoxide radicals with EC50 values that are similar to those of GSH. The cysteine-containing peptides also had stronger ferric reducing antioxidant power and metal chelation activity than peptides devoid of cysteine. In contrast, MMGW, ERF, and EYW had poor radical scavenging and metal chelation activities. We conclude that the availability of the sulfhydryl group may have enhanced antioxidant potency while the presence of bulky groups such phenylalanine and tryptophan had an opposite effect.

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. Particularly, tyrosine, leucine, alanine, isoleucine, valine, lysine, phenyalanine, cysteine, methionine and histidine in peptide chain exhibited high antioxidant activity. Mungbean meal protein (MMP) is highly abundant in hydrophobic amino acids. It indicated that MMP might be a good source of antioxidants. Therefore, the objectives were to optimize the conditions used to generate mungbean meal protein hydrolysate (MMPH) with antioxidant activity from bromelain and to investigate the antioxidant activities of different molecular weight (MW) peptide fraction. METHODS: Response Surface Methodology (RSM) was used for screening of the optimal conditions to produce MMPH. After that MMPH was fractionated using ultrafiltration membranes with different MW distributions. Crude-MMPH and four fractions were investigated for five antioxidant activities: 2,2,1-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, ferric reducing antioxidant power (FRAP) and metal ion chelation activity. RESULTS: The optimal condition to produce the MMPH was 15% (w/w) of bromelain and hydrolysis time for 12 h which showed the greatest DPPH and ABTS radical scavenging activity. After mungbean protein from optimal condition was separated based on different molecular weight, the DPPH radical scavenging activity was the highest for the F4 (less than 1 kDa) peptide fraction. Metal ion chelating activity was generally weak, except for the F4 that had a value of 43.94% at a protein concentration of 5 mg/mL. The F4 also exhibited high hydroxyl and superoxide activities (54 and 65.1%), but moderate activity for ferric reducing antioxidant power (0.102 mmole Fe2+/g protein) compared to other peptide fractions and crude-MMPH. Molecular weight and amino acid were the main factors that determined the antioxidant activities of these peptide fractions. Results indicated that F4 had strong antioxidant potentials. DISCUSSION: The lowest MW fraction (less than 1 kDa) contributed to the highest DPPH, superoxide, hydroxyl and metal chelation activity because influence of low MW and high content of hydrophobic amino acid in peptide chain. Results from this study indicated that MMPH peptides donate protons to free radicals because they had significantly high DPPH value compared to superoxide, hydroxyl and FRAP, which reactions were electron donation. Moreover, MMPH peptides had the ability to inhibit transition metal ions because of highly abundant glutamic acid and aspartic acid in peptide chain.

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. eb-MPH contributed to DPPH (80) and ABTS (95%) scavenging activities and to savoury/sweet flavour volatile compounds (3-methyl-butanal, furfural and benzaldehyde), bouillon odour, sweet odour, chicken odour, meaty odour, moderate bitter taste and umami. In addition, principal component analysis (PCA) showed that 72.87% of the total variance confirmed the correlation between DH, S0, DPPH, ABTS, sensory characteristics and volatile flavour compounds. These results suggested that eb-MPH can be used as a natural food flavouring agent and antioxidant.

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. The pH and temperature were controlled at 6.0 and 50 °C, respectively. It was found that the best treatment combination for eb-MPH production by response surface methodology (RSM) was 18% bromelain and a hydrolysis time of 3 h, resulting in the greatest degree of hydrolysis (% DH) and percent yield, with values of 61.04 and 45.63%, respectively. Results also showed that the phenylalanine, tyrosine and leucine contents of the optimally produced eb-MPH were 20.88, 14.50 and 10.93%, respectively. Twelve volatile compounds were identified using gas chromatography mass spectrometry in eb-MPH; benzaldehyde, 2-pentylfuran and furfural were the predominant odorants.