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.

Comparative physicochemical characteristics and in vitro protein digestibility of alginate/calcium salt restructured pork steak hydrolyzed with bromelain and addition of various hydrocolloids (low acyl gellan, low methoxy pectin and κ-carrageenan).

Physicochemical and in vitro protein digestibility of alginate/calcium (AC) restructured pork steak hydrolyzed with bromelain with addition of LA gellan, LM pectin and κ-carrageenan at various concentrations (0.5, 1.0, 1.5 and 2% w/w) was evaluated for masticatory dysfunction people. The AC samples with κ-carrageenan showed the lowest cooking losses and highest water holding capacity (WHC). Moreover, addition of κ-carrageenan showed the highest Kramer shear force (KSF) and higher hardness, cohesiveness, springiness, chewiness, and gumminess, but the adhesiveness value was lower than those of the other treatments. According to SEM, the gel network of AC samples with κ-carrageenan was more clearly than those with the other treatments. FTIR demonstrated that the addition of polysaccharides to AC sample enhanced the hydrogen bonds in the gel system. For in vitro protein digestibility results, addition of 0.5% (w/w) LA gellan and κ-carrageenan samples showed the highest pepsin (73-74%) and trypsin (79-80%) digestibility.

Physicochemical characteristics and textural parameters of restructured pork steaks hydrolysed with bromelain.

Enzymatic tenderisation including bromelain enhances underused cuts of meat in emerged restructuring technology. Physicochemical and textural characteristics of restructured pork steak hydrolysed with bromelain for masticatory dysfunction people were evaluated. Restructured pork steak treated with bromelain at 0.05 and 0.1% (w/w) was hydrolysed at 50 °C for 0, 3, 6, 9 and 12 min. The cooking losses of 0.05% (w/w) bromelain for 0, 3 and 6 min were lower than 0.1% (w/w) bromelain samples. The ΔE increased after increasing the enzyme concentration and hydrolysis time. Bromelain-treated samples at higher concentrations showed lower WBSF, KSF and TPA parameters, but cohesiveness of 0.05% (w/w) had higher than 0.1% (w/w) bromelain samples. Total protein, sarcoplasmic protein solubility, TCA-soluble peptide, total collagen and soluble collagen contents were the highest in 0.1% (w/w) bromelain-treated samples for 12 min (P < 0.05). According to SDS-PAGE and SEM, various proteins in the enzyme-treated samples were degraded.

Bioactive peptides from brown rice protein hydrolyzed by bromelain: Relationship between biofunctional activities and flavor characteristics.

This study evaluated the biological properties of peptides from brown rice protein hydrolyzed by bromelain (eb-RPH) in relation to flavor characteristic. The fractionation into peptides < 1 kDa was observed to improve the DPPH, ABTS, and hydroxyl radical-scavenging activities (0.19, 2.28, and 24.64 mM Trolox, respectively), angiotensin-converting enzyme (ACE)-inhibitory activity (IC50 value of 0.20 ± 0.011 mg protein/mL), as well as bitter and umami tastes. The < 1 kDa fraction was further analyzed by liquid chromatography-electrospray ionization/mass spectrometry to identify amino acid sequence associated with biological activities and flavor characteristics. Eight peptides were identified. Most of the identified peptides contained features of previously reported ACE inhibitory and antioxidant peptides, especially peptide FGGSGGPGG and FGGGGAGAGG. Evaluation of flavor characteristics using BIOPEP database demonstrated that they had high occurrence frequencies of umami peptides (ESDVVSDL, GSGVGGAK, and SSVGGGSAG) and low Q-value (938.75 to 282.22), suggesting that these peptides may be used as a fortifying health ingredient with good taste. PRACTICAL APPLICATION: The fractionated brown rice protein hydrolysate (< 1 kDa) has the potential to serve as a functional food ingredient in nutraceutical food and beverage products that can provide health benefits with good taste. Information on amino acid composition and spatial conformation of peptide may aid us to better understand the molecular mechanisms involved in bioactivities and flavor of brown rice peptide for industrial applications.

Isolation and characterisation of antioxidative peptides from bromelain-hydrolysed brown rice protein by proteomic technique.

In this study, proteins from Thai brown rice (Khao Dawk Mali 105) were separated into albumin (2.18 %), globulin (3.98 %), glutelin (84.23 %), and prolamin (9.61 %) fractions, and were hydrolysed with various bromelain concentrations and hydrolysis times. Liquid chromatography-electrospray ionization/mass spectrometry (LC-ESI-MS/MS) was conducted to assess the composition, molecular weight (MW) distribution, and sequence of the resulting peptides, and showed that most peptides have a MW below 2000 Da (60-70 %). Glutelin fraction hydrolysates exhibited the highest 2,2'-azino-bis 3-ethylbenzthiazoline-6-sulfonic (ABTS•+) radical-scavenging (0.69 ± 0.04 µM trolox) and copper chelating (4.12 ± 0.01 mg ethylenediaminetetraacetic acid; EDTA) activities, which was further fractionated into six fractions using reversed-phase high-performance liquid chromatography. The fourth fraction showed the highest ABTS•+ scavenging (1.08 ± 0.03 mM trolox) and copper chelating (5.00 ± 0.02 mg EDTA) activity. LC-MS/MS analysis revealed that the peptides with MW less than 1500 Da and hydrophobic or aromatic N-terminal residues, such as SPFWNINAHS, MPVDVIANAYR, VVYFDQTQAQA, and VEVGGGARAP, possibly contributed to the highest antioxidant activity in fourth fraction.

A novel multi-biofunctional protein from brown rice hydrolysed by endo/endo-exoproteases.

Brown rice, which is a less allergenic food grain and contains essential amino acids, was hydrolysed by bromelain and PROTEASE FP51® to improve its functionalities and taste for food applications. The hydrolysate prepared by bromelain (eb-RPH) had high protein solubility, surface hydrophobicity, low molecular weight peptides, hydrophobic amino acids (leucine, valine and glycine) and flavor amino acids (glutamic acid and aspartic acid). The eb-RPH exhibited higher 1,1-diphenyl-2-picrylhydrazyl (DPPH˙) and 2,2'-azino-bis 3-ethylbenzthiazoline-6-sulfonic (ABTS˙(+)) radical-scavenging activities of 76.62% and 52.96%, respectively, and possessed a better foaming capacity (221.76%) and emulsifying capacity (32.34%) than the hydrolysate prepared by PROTEASE FP51® (ep-RPH) did. The eb-RPH gave the desired taste, which is attributed to volatile flavor compounds (benzaldehyde, benzeneacetaldehyde and 2-acetyl-1-pyrroline) and non-volatile flavor compounds, such as monosodium glutamate, 5'-guanosine monophosphate and 5'-inosine monophosphate (0.07, 0.03 and 0.05 mg mL(-1), respectively). Brown rice peptides generated by bromelain were novel bioactive peptides with multifunctional properties.

Seafood-like flavour obtained from the enzymatic hydrolysis of the protein by-products of seaweed (Gracilaria sp.).

An enzymatic bromelain seaweed protein hydrolysate (eb-SWPH) was characterised as the precursor for thermally processed seafood flavour. Seaweed (Gracilaria fisheri) protein after agar extraction was hydrolysed using bromelain (enzyme activity=119,325 U/g) at 0-20% (w/w) for 0.5-24 h. Optimal hydrolysis conditions were determined using response surface methodology. The proposed model took into account the interaction effect of the enzyme concentration and hydrolysis time on the physicochemical properties and volatile components of eb-SWPH. The optimal hydrolysis conditions for the production of eb-SWPH were 10% bromelain for 3h, which resulted in a 38.15% yield and a 62.91% degree of hydrolysis value. Three free amino acids, arginine, lysine, and leucine, were abundant in the best hydrolysate. Ten volatile flavours of the best eb-SWPH were identified using gas chromatography/mass spectrometry. The predominant odourants were hexanal, hexanoic acid, nonanoic acid, and dihydroactinidiolide. The thermally processed seafood flavour produced from eb-SWPH exhibited a roasted seafood-like flavouring.