No description available.

Master of Science / Food Science Institute, Animal Science and Industry / Karen A. Schmidt / Yogurt is a good source of whey proteins, which have been reported to provide positive health benefits. During yogurt manufacture, the yogurt mix receives a heat treatment which pasteurizes the product, denatures the whey proteins affecting their availability, and enhances quality attributes. Thus the objective of this research was to improve the undenatured whey protein content in yogurt. The study was divided in two parts. The first part focused on the effect of pasteurization treatments of yogurt mixes (65 °C for 30 min vs. 90 °C for 10 min) on the yogurt firmness, G’, L*, syneresis and water holding capacity (WHC), and how these properties change as a function of storage. Nonfat dry milk (NFDM) was reconstituted (~11% w/v) pasteurized, cooled, inoculated with yogurt culture, incubated to pH 4.5, stored at 5 °C ±1 and evaluated for various physical and chemical properties on days 1, 15 and 29. The experiment was replicated 3 times and data were analyzed by SAS®. Yogurt samples had a 5-fold difference in whey protein denaturation (WPD) and the greater the WPD the greater the firmness, G’, L* and WHC but lesser the syneresis. During yogurt storage, L*, G’, syneresis and WHC increased. The second part of this research focused on whey protein concentrate (WPC) addition (3%) in yogurt mix combined with two pasteurization treatments (70 °C for 30 min vs. 90 °C for 10 min) to determine their effects on the yogurt quality. Yogurt mixes were formulated using 12.5% NFDM or 9.5% NFDM and 3% WPC and a procedure similar to the previous study was followed. The WPC addition resulted in a yogurt with decreased firmness, G’, WHC but increased syneresis. Yogurt made from mixes pasteurized at 90 °C for 10 min had ~60% WPD and comparable quality attributes regardless of WPC addition. Thus, additional WPC and less WPD in this study resulted in a yogurt with slightly lesser quality attributes but more undenatured whey proteins in the final yogurt.

No description available.

Submitted by Geandra Rodrigues (geandrar@gmail.com) on 2017-12-20T13:20:23Z No. of bitstreams: 1 israelnovaesdemoura.pdf: 1420476 bytes, checksum: 6634c39e49385490d2f7b019fb451af1 (MD5) / Approved for entry into archive by Adriana Oliveira (adriana.oliveira@ufjf.edu.br) on 2017-12-21T11:59:42Z (GMT) No. of bitstreams: 1 israelnovaesdemoura.pdf: 1420476 bytes, checksum: 6634c39e49385490d2f7b019fb451af1 (MD5) / Made available in DSpace on 2017-12-21T11:59:42Z (GMT). No. of bitstreams: 1 israelnovaesdemoura.pdf: 1420476 bytes, checksum: 6634c39e49385490d2f7b019fb451af1 (MD5) Previous issue date: 2017-08-04 / O objetivo deste trabalho foi avaliar a caracterização e eficácia de diferentes técnicas da espectroscopia de fluorescência na detecção de adulterações em formulações de Whey Protein concentrado (WPC) em pó, a partir de sua mistura com substâncias de diferentes origens. Foram estudados dois diferentes lotes de WPC provenientes do mesmo fornecedor. Adulterações foram realizadas a partir da adição individual de Cafeína (Tratamento 1), Creatina (Tratamento 2) e Lactose (Tratamento 3) a 30% (m/m) em WPC e submetidas às análises de espectroscopia de fluorescência estacionária e resolvida no tempo, utilizando-se os comprimentos de onda de excitação de 275 e 335 nm. Quando excitadas a 275 nm, as amostras apresentaram pico de emissão a 335 nm aproximadamente, com uma banda de emissão em torno de 380 nm, característica apenas na amostra contendo cafeína, enquanto lactose e creatina não induziram alterações no espectro do WPC. Quando excitadas a 335 nm, as amostras apresentam picos de emissão com máximo em 425 e 470 nm, sem diferenciação por simples observação do espectro. Análise da distância Euclidiana evidenciou que, quando excitadas a 275 nm, os espectros completos dos tratamentos 2 e 3 foram semelhantes ao Controle 1 enquanto o Tratamento 1 foi diferente. Já na excitação a 335 nm todos os espectros foram semelhantes. Análise de Componentes Principais (PCA) confirmou a diferenciação do Tratamento 1 a 275 nm mas foi inconclusiva com a excitação de 335 nm, porém determinou pontos de interesse para estudos das derivadas dos espectros. Com as derivadas, foi possível a diferenciação entre os Tratamentos 2 e 3 nos dois comprimentos de onda, com enfoque em comprimentos de ondas específicos que podem ser decisivos na diferenciação das adulterações. Em relação a espectroscopia resolvida no tempo, o Tratamento 1 demonstrou valores da intensidade média do tempo de vida de emissão superior aos tratamentos 2 e 3 nos dois comprimentos de onda de excitação empregados. A adulteração com cafeína foi realizada na amostra Controle 2 e foi observado resultado semelhante quando comparada ao Controle 1. De maneira geral, a aplicação das técnicas de espectroscopia de fluorescência estacionária e resolvida no tempo possibilitou a caracterização das amostras utilizadas no estudo. Além disso, possibilitou a observação de diferenças entre as amostras controles e aquelas adulteradas, especialmente a adicionada de cafeína e excitada no comprimento de onda 275 nm, com ajuda de ferramentas matemáticas. Os resultados aqui obtidos corroboram com o fato de que as técnicas empregadas podem ser importantes na detecção de fraudes em produtos lácteos. / The objective of this work was to evaluate the characterization and efficacy of different fluorescence spectroscopy techniques in the detection of adulterations in formulations of Whey Protein Concentrate (WPC) powder, from its mixture with substances of different origins. Two different batches of WPC from the same supplier were studied. Adulterations were performed from the individual addition of Caffeine (Treatment 1), Creatine (Treatment 2) and Lactose (Treatment 3) at 30% (w / w) in WPC and subjected to stationary fluorescence spectroscopy and time-resolved fluorescence, using the excitation wavelengths of 275 and 335 nm. When excited at 275 nm, the samples showed an emission peak at approximately 335 nm, with an emission band around 380 nm, characteristic only in the sample containing caffeine, while lactose and creatine did not induce alterations in the WPC spectrum. When excited at 335 nm, the samples showed peak emission at 425 and 470 nm, without differentiation by simple observation of the spectrum. Euclidean distance analysis showed that, when excited at 275 nm, the complete spectra of treatments 2 and 3 were similar to Control 1 while Treatment 1 was different. Regarding the excitation at 335 nm, all spectra were similar. Principal Component Analysis (PCA) confirmed the differentiation of Treatment 1 at 275 nm but it was inconclusive with 335 nm excitation, however, it determined points of interest for spectra derivative studies. With the derivatives, it was possible to differentiate between Treatments 2 and 3 in the two wavelengths, focusing on specific wavelengths that can be decisive in the differentiation of adulterations. In relation to time resolved fluorescence spectroscopy, Treatment 1 demonstrated values of the mean emission lifetime higher over Treatments 2 and 3 at the two excitation wavelengths employed. The caffeine adulteration was performed in the Control 2 sample and a similar result was observed when compared to Control 1. In general, the application of stationary and time resolved fluorescence spectroscopy techniques allowed the characterization of the samples used in the study. In addition, it made possible the observation of differences between the control and adulterated samples, especially the one with caffeine added and excited at the wavelength 275 nm, with the help of mathematical tools. The results obtained here corroborate the fact that the techniques employed may be important in the detection of fraud in dairy products.

Processed turkey rolls were prepared with 1 or 3% whey protein concentrates WPC-50 (pH=5. 8 0) , WPC-60 (pH=4. 53) and WPC-75 (pH=6.85) containing 50, 60 and 75% protein along with controls (phosphate and no phosphate) . Control rolls made with 0.5% phosphate had the highest bind strength, and sensory evaluation scores. Only WPC-75 (1%) was acceptable as a binding agent and flavor enhancer. WPC-60 reduced pink discoloration of rolls, but flavor, bind and cohesiveness scores were unacceptably low. WPC-50 was not an effective binding agent. In general, rolls made with 3% WPC had lower scores for intensity of turkey flavor. Bind strength and sensory characteristics were compared for restructured beef rolls formulated with 1% salt, 0.375% sodium tripolyphosphate (STPP) or 0.07% sodium hydroxide (NaOH), and 5, 10 or 20% added water. Controls also had 1% x salt, but no STPP or NaOH. Relative bind strength of rolls was STPP > NaOH > controls. Addition of 20% water reduced bind strength. Cooked yield, moisture content, beef flavor and texture of NaOH rolls were similar to STPP rolls. Bind strength and cohesiveness of NaOH rolls were lower than STPP rolls, but still acceptable. For measuring bind strength of turkey and beef rolls, a sensitive and inexpensive penetrometer was developed. It was equipped with a top-loading balance, accessories, IBM-compatible personal computer and Quick-Basic program that allowed continuously collected penetration force data. at specific time intervals. Penetrometer bind strength and taste panel cohesiveness of turkey and beef rolls were highly correlated (r=0.89 and r=0.93, respectively).

Probiotic dairy foods, especially non- and low-fat dairy products, are becoming popular in the US. A non-fat goat's milk yogurt containing probiotics (Lactobacillus acidophilus and Bifidobacterium spp.) was developed using heat-treated whey protein concentrate (HWPC) as a fat replacer and pectin as a thickening agent. Yogurts containing non-heat treated whey protein concentrate (WPC) and pectin as well as one with only pectin were also produced. A fat-free cow's milk yogurt with pectin was also used as a control yogurt. The yogurts were analyzed for chemical composition, water holding capacity (syneresis), microstructure, changes in pH and viscosity, mold, yeast and coliform counts, and probiotic survivability during storage at 4°C for 10 weeks. The results showed that the non-fat goat's milk yogurt made with 12% HWPC (12.5% WPC solution heated at 85°C for 30 min at pH 8.5) and 0.35% pectin, had a significantly higher viscosity (P<0.01) than any of the other yogurts and low syneresis than the goat’s yogurt with only pectin added (P<0.01). After 10 weeks in storage, viscosity and pH remained constant throughout all of the yogurts. Mold, yeast, and coliform counts were negative throughout the 10 week study. Bifidobacterium spp. remained stable and counts remained above 10⁶CFU g⁻ ¹ during the 10 week storage. However, the population of Lactobacillus acidophilus dropped below 10⁶CFU g⁻ ¹ after 2 weeks of storage. Microstructure analysis of the non - fat goat’s milk yogurt determined by scanning electron microscopy revealed that HWPC interacted with casein micelles to form a more comprehensive network in the yogurt gel. The results indicate that HWPC could be used as a fat replacer to improve the consistency of non - fat goat’s milk yogurt and other products alike.

Whey is a byproduct of cheese making; whey proteins are globular proteins which can be modified and polymerized to add functional benefits, these benefits can be both nutritional and structural in foods. Modified proteins can be used in non-foods, being of particular interest in polymer films and coatings. Food packaging materials, including plastics, can linings, interior coatings of paper containers, and beverage cap sealing materials, are generally made of synthetic petroleum based compounds. These synthetic materials may pose a potential human health risk due to presence of certain chemicals such as Bisphenol A (BPA). They also add to environmental pollution, being difficult to degrade. Protein-based materials do not have the same issues as synthetics and so can be used as alternatives in many packaging types. As proteins are generally hydrophilic they must be modified structurally and their performance enhanced by the addition of waterproofing agents. Polymerization of whey proteins results in a network, adding both strength and flexibility. The most interesting of the food-safe waterproofing agents are the (large aspect ratio) nanoclays. Nanoclays are relatively inexpensive, widely available and have low environmental impact. The clay surface can be modified to make it organophilic and so compatible with organic polymers. The objective of this study is the use of polymerized whey protein (PWP), with reinforcing nanoclays, to produce flexible surface coatings which limit the transfer of contents while maintaining food safety. Four smectite and kaolin type clays, one treated and three natural were assessed for strengthening qualities and the potential waterproofing and plasticizing benefits of other additives were also analyzed. The nutritional benefits of whey proteins can also be used to enhance the protein content of various foodstuffs. Drinkable yogurt is a popular beverage in the US and other countries and is considered a functional food, especially when produced with probiotic bacteria. Carbonation was applied to a drinkable yogurt to enhance its benefits. This process helps reduce the oxygen levels in the foodstuff thus potentially being advantageous to the microaerophilic probiotic bacteria while simultaneously producing a product, somewhat similar to kefir, which has the potential to fill a niche in the functional foods market. Yogurt was combined with a syrup to reduce its viscosity, making it drinkable, and also to allow infusion of CO2. This dilution reduced the protein content of the drink and so whey protein concentrate was added to increase levels in the final product. High-methoxyl pectins were used to provide stability by reducing the tendency of the proteins to sediment out. The objectives of this study were to develop a manufacturing technology for drinkable carbonated symbiotic yogurts, and to evaluate their physicochemical properties. Two flavors of yogurt drink, pomegranate and vanilla, were formulated containing inulin as prebiotic, along with probiotic bacteria, producing symbiotic dairy beverages.

Les émulsions laitières sont des systèmes thermodynamiquement instables qui doivent résister aux contraintes technologiques (chauffage, congélation) appliquées lors de leur fabrication ou usage. Les émulsions riches en protéines de lactosérum sont particulièrement sensibles et l’emploi d’additifs alimentaires est un moyen de ralentir leur déstabilisation. Dans l’objectif d’offrir des produits 100 % lait aux consommateurs, concevoir des émulsions, riches en protéines de lactosérum, sans additifs alimentaires et stables aux traitements technologiques, constitue un réel challenge. La stratégie employée dans ce projet de thèse a été de combiner les propriétés des agrégats de protéines de lactosérum et des caséines pour stabiliser des émulsions aux cours des traitements technologiques sur une large gamme de concentration.Des émulsions ont été préparées avec des agrégats de protéines de lactosérum de structure différente et avec différents ratios agrégats/caséines. Quelle que soit leur structure, la présence d’agrégats à la surface des globules gras déstabilise l’émulsion (gélification /séparation de phase) alors que dans la phase dispersante ceux-ci sont stables aux traitements technologiques. A l’inverse, les émulsions dont la surface des globules gras est recouverte de caséines sont très stables aux traitements technologiques. Ainsi, il est possible de moduler la stabilité des émulsions riches en protéines de lactosérum aux cours des traitements technologiques en exploitant les propriétés des agrégats et des caséines et en contrôlant leur répartition entre la surface des glo / Dairy emulsions are thermodynamically unstable systems, which have to be resistant to the technological treatments (heating, freezing/thawing) applied during their manufacture or use. Whey protein-rich emulsions are particularly sensitive to technological treatments and instabilities are currently tackled by the use of non-dairy additives. With aim to offer products that are more natural to consumers (additive-free), the preparation of whey protein-rich emulsions without additive and stable during technological treatments constitutes a major challenge for dairy companies. The strategy adopted during this thesis was to combine the properties of the whey proteins aggregates and caseins in order to stabilize emulsion during technological treatments in a large range of protein concentrationsEmulsions were prepared with various whey protein aggregates and various whey protein aggregates/caseins ratio. Whatever the whey protein aggregates, their presence at the fat droplet surface destabilize the emulsions (gelation/phase separation) whereas they are stable in the continuous phase of the emulsions during technological treatments. In contrast, emulsions are extremely stable during technological treatments when caseins fully cover the fat droplet surface. The results obtained highlighted the possibility of modulating the stability during technological treatments of whey protein-rich emulsions by combining the properties of the whey protein aggregates and the caseins and by controlling their repartition between the fat droplet surface and the continuous phase of the emulsion.

Two studies were conducted to evaluate the effects of milk solids on restructured and emulsified turkey rolls. the milk solids used were nonfat dry milk (NFDM), whey protein concentrate (WPC), and calcium caseinate (CC). Turkey rolls consisted of 100% breast meat or 90:10 or 70:30 breast-to-thigh, salt (1%), water (10%), internal or cluster fat (10%), and 3% of various milk solids (WPC, NFDM, CC). The objectives of these studies were to 1) determine which ratio between light and dark meat is preferred; 2) determine which of milk solids evaluated will permit the highest level of dark meat incorporation into evaluated products; 3) determine if there is a mechanism by which milk proteins lighten poultry meat; and 4) determine which milk protein produces the best bind between meat pieces. Panelists were used in the first study to evaluate cooked meat attributes of color intensity, color uniformity, cohesiveness, tenderness, roasted turkey flavor, juiciness, and overall acceptability. The attributes were rated on a seven-point scale. Rolls made with WPC or NFDM scored significantly higher for color uniformity, cohesiveness, roasted turkey flavor, and overall acceptability than rolls made with CC. No differences were noted among treatments for juiciness or toughness with rolls of the same light-to-dark meat ratio. However, the 90:10 rolls were rated significantly more tender than the rolls made with the 70:30 ratio. Rolls containing milk solids had significantly higher yields than the controls. In the second study, rolls were made using the preferred meat ratio (90:10 breast:thigh meat). NFDM and WPC were used as binders, but not CC, since in the first study it was an ineffective binding agent. The second study showed that no whitening or lightening occurred in turkey rolls. This researcher also found that both NFDM and WPC increased bind strength between meat pieces. Controls made without added milk solids had less bind strength between the meat particles. Meat particle size also affected bind strength in finished products, with finely chopped rolls having higher bind strength than coarsely ground rolls. Moreover, the second study had unexpected results indicating that NFDM will prevent development of pink discoloration during refrigerated storage. The penetrometer used for bind measurements is described.

Resumo: Objetivo: O objetivo do estudo foi comparar os efeitos de uma dose-única de caseína micelar (MCa) com a ingestão de caseína micelar associada à proteína do soro do leite (whey protein) (1:1) sobre a resposta aminoacidêmica e a via de sinalização do alvo da rapamicina (mTOR) em músculos esqueléticos de ratos durante a fase de inatividade (período de luz ambiente). Métodos: Após 10h de jejum durante a fase ativa, os ratos foram alimentados com MCa ou PB (5,6g proteína por kg de massa corporal) por gavagem e a água foi usada como veículo (grupo controle, PLA). Em 30 e 450 min após a suplementação das proteínas, os animais foram sacrificados e as amostras de sangue e do músculo gastrocnêmio foram coletadas para análises bioquímicas. Resultados: Os níveis plasmáticos dos aminoácidos de cadeia ramificada (BCAA) aumentaram após as suplementações de MCa (3 vezes) e PB (3,2 vezes). Ainda mais relevante, os níveis estimulatórios da fosforilação da mTOR e do seu alvo downstream p70S6K foram maiores 30 min após MCa (2,6 e 2,9 vezes, respectivamente) e PB (2,8 e 3,8 vezes, respectivamente) quando comparado com PLA. As concentrações plasmáticas de leucina forma correlacionadas com a ativação da mTOR (r = 0,60; p < 0,05) e p70S6K (r = 0,77; p < 0,05) em 30 min. Não existiu diferença para as concentrações plasmáticas de BCAA e a via de sinalização da mTOR em 450 min. Conclusão: Nós concluímos que a suplementação de MCa e PB resultaram em um efeito anabólico semelhante no músculo esquelético ... (Resumo completo, clicar acesso eletrônico abaixo) / Abstract: Objective: The aim of the study was to compare the effects of single-dose supplementation of a protein blend (PB) composed of micellar casein and whey protein (1:1) with isolated micellar casein (MCa) on aminoacidemic response and the mammalian target of the rapamycin (mTOR) signaling pathway 30 and 450 min after the beginning of the inactive phase in Wistar rats. Methods: After 10h of fasting during the active phase, rats were fed with MCa or PB (5.6g protein per kg of body mass) by gavage and water was used as the vehicle (PLA, placebo group). At 30 and 450 min after protein supplementation, the animals were euthanized and blood and gastrocnemius muscle samples were collected for biochemical and immunoblot analysis. Results: Plasma BCAA levels increased after MCa (3-fold) and PB (3.2-fold) supplementations. More importantly, the stimulatory phosphorylation levels of mTOR and its downstream target ribosomal protein S6 kinase (p70S6K) were higher 30 min after MCa (2.6 and 2.9-fold, respectively) and PB (2.8 and 3.8-fold, respectively) when compared with PLA. Plasma leucine levels were correlated with activation of mTOR (r = 0.60, p < 0.05) and p70S6K (r = 0.77; p < 0.05) at 30 min. There were no differences for plasma amino acids levels and the mTOR signaling pathway at 450 min. Conclusions: MCa and PB supplementations resulted in a similar anabolic milieu in rat skeletal muscle by inducing a transient increase in BCAA plasma levels and activation of the mTOR/p70S6K axis. / Mestre