Influence of calcium-binding salts on heat stability and fouling of whey protein isolate dispersions

peer-reviewedThe effect of the calcium-binding salts (CBS), trisodium citrate (TSC), tripotassium citrate (TPC) and disodium hydrogen phosphate (DSHP) at concentrations of 1–45 mm on the heat stability and fouling of whey protein isolate (WPI) dispersions (3%, w/v, protein) was investigated. The WPI dispersions were assessed for heat stability in an oil bath at 95 °C for 30 min, viscosity changes during simulated high-temperature short-time (HTST) and fouling behaviour using a lab-scale fouling rig. Adding CBS at levels of 5–30 mm for TSC and TPC and 25–35 mm for DSHP improved thermal stability of WPI dispersions by decreasing the ionic calcium (Ca2+) concentration; however, lower or higher concentrations destabilised the systems on heating. Adding CBS improved heat transfer during thermal processing, and resulted in lower viscosity and fouling. This study demonstrates that adding CBS is an effective means of increasing WPI protein stability during HTST thermal processing

A comparison of pilot-scale supersonic direct steam injection to conventional steam infusion and tubular heating systems for the heat treatment of protein-enriched skim milk-based beverages

peer-reviewedDirect supersonic steam injection, direct steam infusion, and indirect tubular heating were each applied to protein-enriched skim milk-based beverages with 4, 6 and 8% (w/w) total protein, and the effect of final heat temperature on the physical properties of these beverages was investigated. Supersonic steam injection resulted in significantly lower levels of denaturation of β-lactoglobulin (34.5%), compared to both infusion (76.3%) and tubular (97.1%) heating technologies. Viscosity, particle size and accelerated physical stability of formulations did not differ significantly between the heating technologies, while noticeable colour differences due to heat treatment (mainly attributed to increasing b* value) were observed, particularly for tubular heating. Overall, the extent of protein denaturation in high-protein dairy products was significantly influenced by the particular heating technology applied. The application of supersonic steam injection technology, with rapid heating and high shear characteristics, may enable differenciated product characteristics for ready-to-drink ambient-delivery high-protein dairy beverages. Industrial relevance: The design and application of novel direct supersonic steam injection technology was comprehensively studied and found to provide significant benefits over direct steam infusion and indirect tubular heating technologies for skim milk-based protein beverages. This type of injection heating system resulted in heat-treated formulations with lower levels of denatured whey proteins, compared to tubular and infusion heating, offering an alternative opportunity to the industry in terms of producing shelf-stable dairy protein beverages

Composition, morphology and pasting properties of Orchis anatolica tuber gum

Orchis anatolica (O. anatolica) tuber is commonly used in the production of Salep gum or O. anatolica tuber gum (OaG) for use as a thickener, flavouring agent, gelling agent, film former and emulsifier in the food industry. The aim of this study was to investigate the chemical composition, physical, morphological and pasting properties of OaG. Physical and morphological analyses, and pasting properties of OaG were analysed using static light scattering, scanning electron microscopy, light microscopy and rotational rheometry, respectively. Volume-weighted mean particle diameter (D [4,3]) value of OaG was 180 ± 1.25 μm. OaG was composed mainly of starch (41.6%), dietary fiber (32.3%) and glucomannan (18.5%). The powder of OaG had irregular shaped particles with smooth surfaces and round edges. After pasting treatment, the initial and final viscosity values of the OaG dispersions at a concentration of 0.5% OaG were 33.7 ± 0.24 and 34.3 ± 0.45 mPa.s, whereas, the corresponding values at a concentration of 2.5% OaG were 1193 ± 92.0 and 1437 ± 83.3 mPa.s, respectively. The glucomannan and dietary fiber components and their possible interactions with starch, in OaG appear to have influenced the peak temperature and viscosity on pasting, due to limitation of the leaching of amylose and amylopectin from starch granules. Therefore, O. anatolica tuber gum, a complex biopolymer, can provide interesting and unique functionality to the food industry in the development of novel food structures

Analysis of Johne’s disease ELISA status and associated performance parameters in Irish dairy cows

peer-reviewedBackground Infection with Mycobacterium avium subspecies paratuberculosis (MAP) has been associated with reductions in milk production in dairy cows and sub optimal fertility. The aim of this study was to highlight the production losses associated with testing MAP ELISA positive in Irish dairy cows. Secondary objectives included investigation of risk factors associated with testing MAP ELISA positive. A survey of management practices on study farms was also conducted, with examination of associations between management practices and herd MAP status. Blood samples were collected from 4188 breeding animals on 22 farms. Samples were ELISA tested using the ID Screen Paratuberculosis Indirect Screening Test. Production parameters examined included milk yield, milk fat, milk protein, somatic cell count, and calving interval. The association between MAP ELISA status and production data was investigated using multi-level mixed models. Logistic regression was used to identify risk factors for testing JD blood ELISA positive at individual cow level and to identify associations between farm management practices and herd MAP status. Results Data were available for 3528 cows. The apparent prevalence recorded was 7.4 %. Mixed model analysis revealed no statistically significant association between testing MAP ELISA positive and dairy cow production parameters. Risk factors associated with testing positive included larger sized herds being over twice more likely to test positive than smaller herds (OR 2.4 P = <0.001). Friesians were less likely to test positive relative to other breeds. A number of study farmers were engaged in management practices that have previously been identified as high risk for MAP transmission e.g., 73.1 % pooled colostrum and 84.6 % of study farmers used the calving area to house sick animals throughout the year. No significant associations however, were identified between farm management practices and herd MAP status. Conclusion No production losses were identified; however an apparent prevalence of 7.4 % was recorded. With the abolition of EU milk quotas herd size in Ireland is expanding, as herds included in this study were larger than the national average, results may be indicative of future JD levels if no JD control programmes are implemented to minimise transmission

Influence of emulsifier type on the spray-drying properties of model infant formula emulsions

The objective of this study was to compare the drying performance and physicochemical properties of model infant formula (IF) emulsions containing 43, 96 and 192 g L−1 protein, oil and maltodextrin (MD), respectively, prepared using different emulsifier systems. Emulsions were stabilised using either whey protein isolate (WPI), whey protein hydrolysate (WPH; DH 8%), WPH + CITREM (9 g L−1), WPH + lecithin (5 g L−1) or WPH conjugated with maltodextrin (DE 12) (WPH-MD). Homogenised emulsions had 32% solids content and oil globules with mean volume diameter WPH + LEC > WPH > WPH- MD > WPI, WPI > WPH > WPH- MD > WPH + LEC > WPH + CIT and WPH- MD > WPI > WPH > WPH + LEC > WPH + CIT, respectively. Additionally, differences in wettability, surface topography and oil globule distribution within the powder matrix and in reconstituted powders were linked to the emulsifier system used. Inclusion of the WPH-MD conjugate in the formulation of IF powder significantly improved drying behaviour and physicochemical properties of the resultant powder, as evidenced by lowest powder build-up during drying and greatest emulsion quality on reconstitution, compared to the other model formula systems

Effects of milk heat treatment and solvent composition on physicochemical and selected functional characteristics of milk protein concentrate

peer-reviewedMilk protein concentrate (MPC) powders (∼81% protein) were made from skim milk that was heat treated at 72°C for 15 s (LHMPC) or 85°C for 30 s (MHMPC). The MPC powder was manufactured by ultrafiltration and diafiltration of skim milk at 50°C followed by spray drying. The MPC dispersions (4.02% true protein) were prepared by reconstituting the LHMPC and MHMPC powders in distilled water (LHMPCw and MHMPCw, respectively) or milk permeate (LHMPCp and MHMPCp, respectively). Increasing milk heat treatment increased the level of whey protein denaturation (from ∼5 to 47% of total whey protein) and reduced the concentrations of serum protein, serum calcium, and ionic calcium. These changes were paralleled by impaired rennet-induced coagulability of the MHMPCw and MHMPCp dispersions and a reduction in the pH of maximum heat stability of MHMPCp from pH 6.9 to 6.8. For both the LHMPC and MHMPC dispersions, the use of permeate instead of water enhanced ethanol stability at pH 6.6 to 7.0, impaired rennet gelation, and changed the heat coagulation time and pH profile from type A to type B. Increasing the severity of milk heat treatment during MPC manufacture and the use of permeate instead of water led to significant reductions in the viscosity of stirred yogurt prepared by starter-induced acidification of the MPC dispersions. The current study clearly highlights how the functionality of protein dispersions prepared by reconstitution of high-protein MPC powders may be modulated by the heat treatment of the skim milk during manufacture of the MPC and the composition of the solvent used for reconstitution

Covalent labelling of β-casein and its effect on the microstructure and physico-chemical properties of emulsions stabilized by β-casein and whey protein isolate

peer-reviewedThe objective of this work was to investigate the effect of covalent labelling on the physico-chemical properties of β-casein (β-CN) in solution and in emulsions stabilized by β-CN and whey protein isolate (WPI). β-CN was covalently labelled by 5-(and 6)-carboxytetramethylrhodamine, succinimidyl ester (NHS-Rhodamine). The effect of conjugating β-CN with NHS-Rhodamine on the spectroscopic properties of labelled β-CN (β-CNlabelled) was examined. No significant difference in interfacial tension (p > 0.05) was found between mixture of WPI and β-CNlabelled (0.5% w/w WPI/β-CNlabelled) and of WPI and β-CN (0.5% w/w WPI/β-CN) in 10 mM phosphate buffer (pH 7.0) at 20 °C. Oil-in-water emulsions stabilized with either WPI/β-CN or WPI/β-CNlabelled (0.5% w/w) were also investigated using laser-light scattering, analytical centrifugation, rheometry and CLSM. It was shown that labelling had no significant effect on the physico-chemical properties of emulsions (p > 0.05) in terms of droplet size, creaming stability, viscosity or zeta-potential. Confocal micrographs of emulsions made with WPI/β-CNlabelled showed that both β-CN and whey proteins could be observed simultaneously, and were co-localized at the surface of fat globules. Furthermore, it was found through image analysis that β-CN produced a thicker interfacial layer than WPI

Characterisation of heat-induced protein aggregation in whey protein isolate and the influence of aggregation on the availability of amino groups as measured by the ortho-phthaldialdehyde (OPA) and trinitrobenzenesulfonic acid (TNBS) methods

Whey protein isolate (WPI) solutions, with different levels of aggregated protein, were prepared by heating (5% protein, pH 7, 90 °C for 30 min) WPI solutions with either 20 mM added NaCl (WPI + NaCl), 5 mM N-ethylmaleimide (WPI + NEM) or 20 mM added NaCl and 5 mM NEM (WPI + NaCl + NEM). Gel electrophoresis demonstrated that the heated WPI and WPI + NaCl solutions had higher levels of aggregated protein, due to more covalent interactions between proteins, than the heated WPI + NEM and WPI + NaCl + NEM solutions. There were marked differences in the levels of amino groups between all heated WPI solutions when measured by the OPA and TNBS methods, with lower levels being measured by the TNBS method than by the OPA method. These results demonstrate that the measurement of available amino groups by the OPA method is less impacted than by the TNBS method after heat-induced structural changes, arising from disulfide or sulfhydryl-disulfide bond-mediated aggregation of whey protein molecules

Pilot-scale ceramic membrane filtration of skim milk for the production of a 'humanised' protein base ingredient for infant milk formula

The protein composition of bovine skim milk was modified using pilot scale membrane filtration to produce a whey protein-dominant ingredient with a casein profile closer to human milk. Bovine skim milk was processed at low (8.9 °C) or high (50 °C) temperature using ceramic microfiltration (MF) membranes (0.1 μm mean pore diameter). The resulting permeate stream was concentrated using polyethersulfone ultrafiltration (UF) membranes (10 kDa cut-off). The protein profile of MF and UF retentate streams were determined using reversed phase-high performance liquid chromatography and polyacrylamide gel electrophoresis. Permeate from the cold MF process (8.9 °C) had a casein:whey protein ratio of ∼35:65 with no αS- or κ-casein present, compared with a casein:whey protein ratio of ∼10:90 at 50 °C. This study has demonstrated the application of cold membrane filtration (8.9 °C) at pilot scale to produce a dairy ingredient with a protein profile closer to that of human milk

Isolation and characterisation of κ-casein/whey protein particles from heated milk protein concentrate and role of κ-casein in whey protein aggregation

peer-reviewedMilk protein concentrate (79% protein) reconstituted at 13.5% (w/v) protein was heated (90 °C, 25 min, pH 7.2) with or without added calcium chloride. After fractionation of the casein and whey protein aggregates by fast protein liquid chromatography, the heat stability (90 °C, up to 1 h) of the fractions (0.25%, w/v, protein) was assessed. The heat-induced aggregates were composed of whey protein and casein, in whey protein:casein ratios ranging from 1:0.5 to 1:9. The heat stability was positively correlated with the casein concentration in the samples. The samples containing the highest proportion of caseins were the most heat-stable, and close to 100% (w/w) of the aggregates were recovered post-heat treatment in the supernatant of such samples (centrifugation for 30 min at 10,000 × g). κ-Casein appeared to act as a chaperone controlling the aggregation of whey proteins, and this effect was stronger in the presence of αS- and β-casein.This work was supported by Dairy Levy Research Trust (project MDDT6261 “ProPart”). S. J. Gaspard was funded under the Teagasc Walsh Fellowship Scheme (reference number 2012211