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Van Hekken D.L.,Dairy and Functional Foods Research Unit | Tunick M.H.,Dairy and Functional Foods Research Unit | Farkye N.Y.,California Polytechnic State University, San Luis Obispo | Tomasula P.M.,Dairy and Functional Foods Research Unit
Journal of Dairy Science | Year: 2013

Queso Fresco (QF), a popular high-moisture, high-pH Hispanic-style cheese sold in the United States, underwent high-pressure processing (HPP), which has the potential to improve the safety of cheese, to determine the effects of this process on quality traits of the cheese. Starter-free, rennet-set QF (manufactured from pasteurized, homogenized milk, milled before hooping, and not pressed) was cut into 4.5- × 4.5- × 15-cm blocks and double vacuum packaged. Phase 1 of the research examined the effects of hydrostatic HPP on the quality traits of fresh QF that had been warmed to a core temperature of 20 or 40°C; processed at 200, 400, or 600. MPa for 5, 10, or 20. min; and stored at 4°C for 6 to 8. d. Phase 2 examined the long-term effects of HPP on quality traits when QF was treated at 600. MPa for 3 or 10. min, and stored at 4 or 10°C for up to 12. wk. Warming the QF to 40°C before packaging and exposure to high pressure resulted in loss of free whey from the cheese into the package, lower moisture content, and harder cheese. In phase 2, the control QF, regardless of aging temperature, was significantly softer than HPP cheeses over the 12. wk of storage. Hardness, fracture stress, and fracture rigidity increased with length of exposure time and storage temperature, with minor changes in the other properties. Queso Fresco remained a bright white, weak-bodied cheese that crumbled and did not melt upon heating. Although high pressures or long processing times may be required for the elimination of pathogens, cheese producers must be aware that HPP altered the rheological properties of QF and caused wheying-off in cheeses not pressed before packaging. © 2013 American Dairy Science Association. Source


Paul M.,Dairy and Functional Foods Research Unit | Phillips J.G.,U.S. Department of Agriculture | Renye J.A.,Dairy and Functional Foods Research Unit
Journal of Dairy Science | Year: 2016

An 8-AA (8mer) fragment (PFPEVFGK) of a known antihypertensive peptide derived from bovine αS1-casein (C12 antihypertensive peptide) was synthesized by microwave-assisted solid-phase peptide synthesis and purified by reverse phase HPLC. Its ability to inhibit angiotensin-converting enzyme (ACE) was assessed and compared with that of the parent 12mer peptide (FFVAPFPEVFGK) to determine the effect of truncating the sequence on overall hypotensive activity. The activity of the truncated 8mer peptide was found to be almost 1.5 times less active than that of the 12mer, with ACE-inhibiting IC50 (half-maximal inhibitory concentration) values of 108 and 69 μM, for 8mer and 12mer, respectively. Although the 8mer peptide is less active than the original 12mer peptide, its overall activity is comparable to activities reported for other small proteins that elicit physiological responses within humans. These results suggest that microbial degradation of the 12mer peptide would not result in a complete loss of antihypertensive activity if used to supplement fermented foods and that the stable 8mer peptide could have potential as a blood pressure-lowering agent for use in functional foods. © 2016 American Dairy Science Association. Source


Bonnaillie L.M.,Dairy and Functional Foods Research Unit | Zhang H.,The New School | Akkurt S.,The New School | Yam K.L.,The New School | Tomasula P.M.,Dairy and Functional Foods Research Unit
Polymers | Year: 2014

Thin casein films for food packaging applications reportedly possess good strength and low oxygen permeability, but low elasticity and high sensitivity to moisture. Modifying the films to target specific behaviors depending on environmental conditions can enable a variety of commercial applications for casein-based films. The mechanical properties of solvent-cast (15% solids) calcium-caseinate/glycerol films (CaCas:Gly ratio of 3:1) were characterized as a function of processing and environmental conditions, including film thickness, solution formulation and ambient humidity (from 22% to 70% relative humidity (RH) at ~20°C). At constant RH, the elongation at break (EAB) had a strong positive dependence on the film thickness. When RH increased, the tensile strength (TS) and modulus (E) decreased approximately linearly, while EAB increased. From 0.05% to 1% (w/w) of citric pectin (CP) was then incorporated into CaCas/Gly films following seven different formulations (mixing sequences), to alter the protein network and to evaluate the effects of CP on the tensile properties of CaCas/Gly/CP films. At constant film thickness and ~60% RH, the addition of 0.1% or 1.0% CP to the films considerably increased or decreased EAB, TS and E in different directions and to different extents, depending on the formulation, while optical micrographs also showed vastly differingnetwork configurations, suggesting complex formulation- and stoichiometry-dependent casein-pectin interactions within the dried films. Depending on the desired film properties and utilization conditions, pectin may be a useful addition to casein film formulations for food packaging applications. © 2014 by the authors. Source


Sousa A.M.M.,University of Porto | Sousa A.M.M.,Dairy and Functional Foods Research Unit | Souza H.K.S.,University of Porto | Liu L.,Dairy and Functional Foods Research Unit | Goncalves M.P.,University of Porto
International Journal of Biological Macromolecules | Year: 2015

Agar films were produced by thermo-compression using choline chloride (ChCl) as a plasticizer with urea. The three solid components were mixed together with the salt and urea (minor components) added to agar (main component) according to a fixed mass ratio of, respectively, 1.16:1:5. A central composite rotatable design (CCRD) with three parameters, 23, was used to evaluate the effects of temperature (X1; °C), time (X2; min) and applied load (X3; kN) of heat-pressing on the maximum tensile strength (TS) of the films (Y; MPa). Mixtures of urea and agar prepared at a mass ratio of 1:5 did not form homogeneous films suggesting the important plasticizing role of the salt. Heat-pressing the mixtures at more draconian conditions led to much darker and opaque films, with better mechanical resistance (higher values of TS). The most resistant film (~15MPa) was obtained at 140°C, 20min and 176kN. Selected films, including the optimal, showed similar water sorption profiles and close values of water vapor permeability (~2.5-3.7×10-9gm-1s-1Pa-1). The fracture behavior and mechanical properties of the films were greatly affected by additional water plasticization when the films were stored at different conditions of relative humidity. © 2015 Elsevier B.V. Source


Qi P.X.,Dairy and Functional Foods Research Unit | Nunez A.,U.S. Department of Agriculture | Wickham E.D.,Dairy and Functional Foods Research Unit
Journal of Agricultural and Food Chemistry | Year: 2012

In this paper, we present the first detailed study of the reaction kinetics and the characterization of the products from the endothermic reactions between β-lactoglobulin and genipin. The effects of the concentration, temperature, and pH were investigated. In the temperature range studied, the reaction was approximately a pseudo-first-order with respect to genipin and 0.22-order and -0.24-order with respect to β-lactoglobulin for pH 6.75 and 10.5 with corresponding activation energy (Ea) estimated to be 66.2 ± 3.8 and 9.40 ± 0.36 kJ/mol, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies, validated by matrix-assisted laser desorption ionization-time of flight mass spectrometry, showed the presence of oligomeric, i.e., di-, tri-, quadri-, and pentameric, forms of cross-linked β-lactoglobulin by genipin at neutral but not alkaline pH; however, an extensive cross-linked network was not observed, consistent with the atomic force microscopy images. It was demonstrated that the reaction temperature and the concentration of genipin but not that of β-lactoglobulin positively affected the extent of the cross-linking reactions. © This article not subject to U.S. Copyright. Published 2012 by the American Chemical Society. Source

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