Thermosonication for the Production of Sulforaphane Rich Broccoli Ingredients

A large proportion of broccoli biomass is lost during primary production, distribution, processing, and consumption. This biomass is rich in polyphenols and glucosinolates and can be used for the production of bioactive rich ingredients for food and nutraceutical applications. This study evaluated thermosonication (TS) (18 kHz, 0.6 W/g, 40–60 °C, 3–7 min) for the pre-treatment of broccoli florets to enhance enzymatic conversion of glucoraphanin into the bioactive sulforaphane. TS significantly increased sulforaphane yield, despite a decrease in myrosinase activity with increasing treatment intensity. The highest sulforaphane yield of ~2.9 times that of untreated broccoli was observed for broccoli thermosonicated for 7 min at 60 °C, which was 15.8% higher than the corresponding yield for thermal processing without sonication (TP) at the same condition. This was accompanied by increase in the residual level of glucoraphanin (~1.8 and 2.3 time respectively after TP and TS at 60 °C for 7 min compared to control samples) indicating that treatment-induced release of bound glucoraphanin from the cell wall matrix and improved accessibility could be at least partially responsible for the enhanced sulforaphane yield. The result indicates the potential of TS for the conversion of broccoli biomass into high sulforaphane broccoli-based ingredients

Quality Attributes of Ultra-High Temperature-Treated Model Beverages Prepared with Faba Bean Protein Concentrates

The objective of this research was to develop a model faba bean drink with a high concentration of protein (>4% w/w). The protein molecular weights and frequency for both faba and soy were assessed using SDS-PAGE. Results showed similarities in the protein molecular weight of both faba and soy (mainly 11S globulin ~Glycinin and 7S globulin ~β-conglycinin). Thus, faba can be considered as a potential soy replica in plant-based milk beverages. Oil-in-water emulsions (5–8% w/w available protein) were prepared using faba bean protein concentrate (FPC), 1% sunflower oil, and 0.2% sunflower lecithin. These emulsions were used as model beverages and were further investigated for UHT processibility, stability, and physicochemical properties. The physicochemical properties of emulsions at various processing stages viz., coarse emulsification, homogenisation, and UHT, were measured. An increase in the protein concentration and thermal treatment resulted in an increased oil droplet size, coalescence and flocculation, and protein aggregation. Lower protein concentrations viz., 5–6%, showed greater negative ζ-potential, and thereby, high dispersibility through enhanced electrostatic repulsions than those of higher concentrations (7–8%). Furthermore, an increase in protein concentration and UHT treatment resulted in an increased creaming index. In total, 21 different volatile compounds were detected and quantified, representing different chemical classes, namely alcohols, aldehydes, ketones, esters, furan, and acids. These volatiles have major consequences for the overall flavour chemistry of the model beverage product. Overall, this study showed the potential for application of faba bean as a protein source in UHT-treated legume-based beverages and identified areas for further development

Thermosonication of Broccoli Florets Prior to Fermentation Increases Bioactive Components in Fermented Broccoli Puree

The aim of this study was to compare the effects of thermosonication (18 kHz at 60 °C for 7 min) pre-treatment with thermal treatment alone (60 °C for 7 min) of broccoli florets prior to pureeing and fermentation on selected bioactive components of fermented broccoli puree. Both thermal and thermosoncation pre-treatments significantly increased the rate of acidification of broccoli puree compared to control untreated broccoli puree, with the time to reach pH 4 being 8.25, 9.9, and 24 h, respectively, for thermally treated, thermosonicated, and control samples. The highest sulforaphane yield of 7268 µmol/kg dry weight (DW) was observed in the thermosonicated samples, followed by 6227 µmol/kg DW and 3180 µmol/kg DW in the thermally treated and untreated samples, respectively. The measurable residual glucoraphanin content was 1642 µmol/kg DW, 1187 µmol/kg DW, and 1047 µmol/kg DW, respectively, in the thermonsonicated, thermally pre-treated, and control fermented samples, indicating that pre-treatment specially by thermosonication increases the extractability of glucoraphanin. The higher sulforaphane yield in the thermosonicated and thermally pre-treated samples could be due to increased extractability and accessibility of glucoraphanin and interaction with myrosinase in addition to the inactivation of epthiospecifier protein (ESP), which directs conversion away from sulforaphane into sulforaphane nitrile

Regulation of milk protein solubility by a whey-derived proline-rich peptide product

The effects of a bovine whey peptide product enriched in proline (wPRP) on the solubility of milk proteins were tested under ambient conditions or following heat treatment at 75 and 100Â °C, for 1 and 15Â min, followed by post-incubation storage at either ambient temperature or 4Â °C for up to 7Â d. wPRP promoted solubilisation of milk proteins in a concentration-dependent manner without heat treatment and also after heat treatment at 75 and 100Â °C, and the effect was enhanced after storage under either ambient or refrigerated storage conditions. Interactions of wPRP and milk proteins were monitored by particle size analysis and tryptic digestion and specifically linked with solubilisation of αS1 casein (αS1-Cn), which supported observed changes in milk protein solubility. The results suggested that wPRP preferably prevented or reversed physical versus covalent protein aggregation, with the relaxation of hydrophobic interactions at 4Â °C providing an additive effect. This application of wPRP represents a novel approach to stabilisation of dairy proteins following thermal processing with industrial usefulness yet to be explored. Copyright © Proprietors of Journal of Dairy Research 2013Â