New insights into perceptions of technology claims in greek-style yogurt: A view in the COVID-19 pandemic.

The Covid-19 pandemic has strongly impacted people's lives and the food industry. In this sense, food products claiming nutritional and health-promoting benefits due to the presence of bioactive peptides and probiotics, such as Greek-style yogurt, have been in demand. The objective of this work was to investigate, through word association, the perception of the consumers regarding the seven concepts related to Greek-style yogurt (traditional, ultra-creamy, zero fat, high content proteins, zero lactose, light and with no added sugars), in the context of social isolation due to Covid-19. In this online survey, 346 participants completed a questionnaire. The participants were divided according to health concerns (increased, not changed, or decreased) and eating habits (improved, not changed, or worsened) during the Covid-19 pandemic. Chi-square and prototypical analysis were used as statistical tests. During the Covid-19 pandemic, based on self-report, around 66% of the participants had their eating habits and their concerns about health changed. The general associations were related to the categories pleasure, health, creamy, pleasant texture, food restriction, and loss of sensory quality. 'Health' and 'pleasure' were negatively associated with the conceptualization of Greek-style yogurt. For the zero-fat, light, and sugar-free Greek-style yogurts, the terms creamy and ultra-creamy are sensory appealing to the consumers. In general, the price and concerns about health are factors that strongly influence the purchase intention of Greek-style yogurts. The yogurts were associated with sensory and non-sensory characteristics, which can be useful for marketing strategies for of different product concepts.

Betalains nanodispersions: Effects on betalains stability and on rheological properties of Greek yogurt.

Red beetroot (Beta vulgaris L.) is a great source of betalains. The main betalains are the betacyanins, responsible for the purple color, and betaxanthins, which present a brownish color. These pigments can present antioxidant activity and are very unstable under certain conditions, such as temperature, extreme ranges of pH, and exposure to light. The aim of this work was to obtain beetroot extract (BE) via ultrasound and transform it into nanoparticles by using polyethylene glycol (PBE) and polyethylene glycol with low molecular weight chitosan (PCBE) as dispersants. The stability of the main betalains in the nanodispersions and the effects of the nanodispersions on the color and rheological properties of commercial Greek yogurt were evaluated. Compared to pristine BE, PCBE nanoparticles presented increased stability for the main betalains in acidic conditions (pH 3.0 and 5.0) of 56% and 22%, respectively. Both PBE and PCBE showed enhanced relative thermal stability compared to pristine BE. Furthermore, PCBE improved commercial Greek yogurt's rheological properties and color parameters. PCBE nanodispersions can be successfully applied as a color additive to commercial Greek yogurt.

ß-lactoglobulin and resveratrol nanocomplex formation is driven by solvation water release.

Despite some thermodynamics studies about ß-lactoglobulin (ßLG) and resveratrol (RES) interactions, there is a gap regarding kinetics data about ßLG-RES complex formation. Here, we determined the kinetic and thermodynamic parameters of ßLG-RES interactions by using surface plasmon resonance (SPR). The kinetic association parameters were dependent on the 3D water structure present on the solvation shell of both interacting molecules. At lower temperature (285.15 K), all activation energies were positive (Eacta‡= 82.86 kJ.mol-1,TΔSa‡= 32.26 kJ.mol-1, and ΔCpa‡= 4.15 kJ.mol-1K-1) due to the higher water structuration on the RES and ßLG solvation shell. All these energetic barriers become mainly from the energetic cost for the desolvation process of RES and ßLG. At higher temperature (301.15 K), the solvation water structure decreases and all the above activation energies become negative (Eacta‡=-121.58 kJ.mol-1,TΔSa‡=-173.59 kJ.mol-1, and ΔCpa‡=-29.92 kJ.mol-1K-1) because the direct interaction between desolvated RES and ßLG molecules released more energy than it is absorbed by desolvation process. However, kinetic dissociation parameters were not dependent on the hydrogen bond density of the water solvation shell as showed by the temperature independence of dissociation energetic parameters. This non-dependence of the dissociation process from the desolvation step probably is because the water molecules interacting with the ßLG-RES complex is not concentrated around/inside the protein site of interaction. The association of free molecules was 1.5 times faster than the dissociation of the thermodynamically stable complex (ΔG(a)‡â€¯â‰… 48.15 kJ.mol-1, ΔG(d)‡â€¯â‰… 73.10 kJ.mol-1). The lower free energy barrier observed for the association came from an isokinetic process where entropic and enthalpic parameters compensated for each other. The ΔG° values indicate that the thermodynamically stable complex predominates over free molecules. At low temperature (285.15 K), the hydrophobic interaction (ΔH° = 73.06 kJ.mol-1; TΔS° = 99.60 kJ.mol-1) drove the ßLG-RES complex formation while at high temperature (301.15 K), hydrophilic interactions became dominant (ΔH° = -142.50 kJ.mol-1; TΔS° = -118.18 kJ.mol-1).

Application of Congo red dye as a molecular probe to investigate the kinetics and thermodynamics of the formation processes of arachin and conarachin nanocomplexes.

The thermodynamics and kinetics of arachin-Congo red (ARA-CR) and conarachin-Congo red (CON-CR) interactions were studied using surface plasmon resonance. KCl led to a reduction of up to 55% in the values of the associated kinetic constants, but it had less influence on the dissociation rates (less than 12%). The change in ionic strength had little effect on the thermodynamic stability of the complexes, but it did reduce their affinities ( [Formula: see text] from 3.52 to 2.44 × 103 M-1 and [Formula: see text] from 15.1 to 12.5 × 103 M-1). The shielding of the electrical double layer favored ARA-CR hydrophilic interactions ( [Formula: see text] decreased from -30.60 to -42.98 kJ mol-1). On the other hand, hydrophobic interactions came to dominate during the formation of [CON-CR]0 ( [Formula: see text] increased from -11.21 to 28.34 kJ mol-1 and [Formula: see text] increased from 12.64 to 51.73 kJ.mol-1). The data presented here improve our understanding of plant-based protein nanocarriers of small bioactive molecules.

Thermodynamic and kinetic insights into the interactions between functionalized CdTe quantum dots and human serum albumin: A surface plasmon resonance approach.

To explore in vivo application of quantum dots (QDs), it is essential to understand the dynamics and energetics of interactions between QDs and proteins. Here, surface plasmon resonance (SPR) and molecular docking were employed to investigate the kinetics and thermodynamics of interactions between human serum albumin (HSA) and CdTe QDs (~3 nm) functionalized with mercaptopropionic acid (MPA) or thioglycolic acid (TGA). Kinetic analysis showed that HSA-QD interactions involved transition-complex formation. Despite the structural similarities between MPA and TGA, the [HSA-CdTe@TGA]‡ formation by association of free HSA and QDs demanded 70% more energy and higher entropic gain (Ea-TGA‡= 65.10 and T∆Sa-TGA‡= 28.62 kJ mol-1) than the formation of [HSA-CdTe@MPA]‡ (Ea-MPA‡ = 38.13 and T∆Sa-MPA‡ = 0.53kJ mol-1). While the [HSA-CdTe@MPA]° dissociation required higher energy and lower entropy loss (Ed-MPA‡ = 49.96 and T∆Sd-MPA‡ = - 32.18kJ mol-1) than the [HSA-CdTe@TGA]° dissociation (Ed-TGA‡= 30.78 and T∆Sd-TGA‡= - 51.12 kJ mol-1). The stability of [HSA-QDs]° was independent of the temperature and functionalizing group. However, the enthalpic and entropic components were highly affected by the substitution of MPA (ΔH° = - 11.83 and TΔS° = 32.72 kJ mol-1) with TGA (ΔH° = 34.31 and TΔS° = 79.73 kJ mol-1). Furthermore, molecular docking results indicated that the metal site on the QDs contributes to the stabilization of [HSA-QDs]°. Therefore, differences in QD functionalization and surface coverage densities can alter the HSA-QD interaction, thus their application.

Human serum albumin-resveratrol complex formation: Effect of the phenolic chemical structure on the kinetic and thermodynamic parameters of the interactions.

The thermodynamics and kinetics of binding between human serum albumin (HSA) and resveratrol (RES) or its analog (RESAn1) were investigated by surface plasmon resonance (SPR). The binding constant and the kinetic constants of association and dissociation indicated that RESAn1 has higher affinity toward HSA than does RES. The formation of these complexes was entropically driven ( [Formula: see text] , [Formula: see text]  KJ mol-1). However, for both polyphenols, the activation energy (Eact) of association (a) of free molecules was higher than that for dissociation (d) of the stable complex ( [Formula: see text]  KJ mol-1), and the rate of association was faster than that of dissociation since the activation Gibbs free energy (ΔG‡) was lower for the former (ΔGaHSA-RES‡â‰…54.73,ΔGdHSA-RES‡â‰…73.83,ΔGaHSA-RESAn1‡â‰…54.14,ΔGdHSA-RESAn1‡â‰…73.97 KJ mol-1). This study showed that small differences in the structure of polyphenols such as RES and RESAn1 influenced the thermodynamics and kinetics of the complex formation with HSA.

Energetic parameters of ß-casein/quercetin activated and thermodynamically stable complex formation accessed by Surface Plasmon Resonance.

Characterizing the energetics and molecular dynamics of binding between proteins and bioactive compounds is strategic. Using surface plasmon resonance, we demonstrated that ß-casein (ß-cas) and quercetin (Qct) form supramolecular complexes driven by an increase in entropy (ΔH°â€¯= 25.86 and TΔS° =53.49 kJ∙mol-1 at 25 °C). It was possible to infer that the ß-cas/Qct complex was formed via an activated complex synthesized by an entropic reduction (TΔS‡(a)= -15.31 kJ mol-1 and TΔS‡(d)= -68.80 kJ mol-1 at 25 °C) and an enthalpic increase (ΔH‡(a) = 30.87 and ΔH‡(d) =5.0 kJ∙mol-1 at 25 °C). Independent of the nature of the Hofmeister ions, the salts KCl or KSCN increased complex stability by decreasing both the kinetic and thermodynamic enthalpy values, through shielding of the electrostatic interactions at the electric double layer of the interacting molecules. An increase in temperature favored both the association of the free interacting molecules and the dissociation of the thermodynamically stable ß-cas/Qct complexes. These results provide insights into the ß-cas/Qct interaction process and contribute to the understanding of how Hofmeister ions can modulate intermolecular interactions between proteins and small molecules.

Curcumin-micellar casein multisite interactions elucidated by surface plasmon resonance.

Determine the thermodynamic and kinetic parameters of interaction between micellar casein (MC) and curcumin (CUR) is useful for the application of MC-CUR systems in food products. We used surface plasmon resonance (SPR) and ultraviolet-visible spectrophotometry (UV-vis) to study the complex formation between MC obtained from skimmed milk and CUR, MC carrying capacity, and thermal protection for CUR at a pH of 6.6. An MC could carry about 18,000 molecules of CUR. SPR suggested an enthalpy-driven process (∆H°â€¯= -64.63 kJ∙mol-1 and T∆S° ranging from -42.45 to -44.46 kJ∙mol-1). Temperature increased reduced the rate of MC-CUR complex formation and increased its dissociation rate. The activation energy for the formation of MC-CUR activated complexes was negative for association of free MC and CUR molecules (-62.8 kJ mol-1) and positive for dissociation of the thermodynamically stable complexes (1.80 kJ mol-1). MC protected the CUR against its thermal degradation when it was subjected to different temperatures (30, 40, 50, and 60 °C for 5.5 h). This study shows the importance of characterizing MC-small molecules interactions for better application of MC as a nanocarrier.

Polydiacetylene/triblock copolymer/surfactant nanoblend: A simple and rapid method for the colorimetric screening of enrofloxacin residue.

Colorimetric nanosensors formed of polydiacetylene (PDA), triblock copolymer (L64 or F68), and sodium dodecyl sulfate (SDS), so-called nanoblends, were developed to detect enrofloxacin (ENRO) in aqueous media. The nanosensors show hydrodynamic diameter ranging from 234.2 ±â€¯3.5 to 801.6 ±â€¯17.8 nm for SDS concentrations of 13.0-21.0 mM, respectively. The lowest limit of detection was 0.054 µM, which is five times smaller than the maximum limit allowed by the European Union. The response surfaces showed that both the SDS and ENRO concentrations influenced the colorimetric response (p < 0.05), and kinetic rate of colorimetric transition (RCT). SDS concentration between 11.0 and 14.0 mM in the nanoblend yielded the most sensitive nanosensors for detecting ENRO. When L64 was replaced by F68, the colorimetric response of the nanoblends was similar, but PDA/F68/SDS showed a slower RCT than PDA/L64/SDS. The developed nanosensor is a sensitive and simple device for the fast detection of ENRO.

Lactoferrin denaturation induced by anionic surfactants: The role of the ferric ion in the protein stabilization.

Here, investigation was made of the interaction between lactoferrin (Lf) and the anionic surfactants sodium dodecyl sulfate (SDS), sodium dodecylbenzene sulfonate (SDBS), and sodium decyl sulfate (DSS), using isothermal titration calorimetry, Nano differential scanning calorimetry (NanoDSC), and fluorescence spectroscopy. The Lf-surfactant interaction was enthalpically favorable (the integral enthalpy change ranged from -5.99 kJ mol-1, for SDS at pH 3.0, to -0.61 kJ mol-1, for DSS at pH 12.0) and promoted denaturation of the protein. The Lf denaturation efficiency followed the order DSS < SDS < SDBS. The adsorption capacity of the protein with respect to surfactant strongly depended on pH and the surfactant structure, reaching a maximum value of 505 SDBS molecules per gram of Lf at pH 3.0. The different efficiencies of the surfactants in denaturing Lf were attributed to the balance of hydrophobic and electrostatic interactions, which also depended on pH and the surfactant structure, highlighting the SDBS-tryptophan residue specific interaction, where SDBS acted as a quencher of fluorescence. Interestingly, the NanoDSC and fluorescence measurements showed that the ferric ion bound to Lf increased its stability against denaturation induced by the surfactants. The results have important implications for understanding the influence of surfactants on structural changes in metalloproteins.

A simple and inexpensive thermal optic nanosensor formed by triblock copolymer and polydiacetylene mixture.

Polydiacetylene (PDA) vesicles have been applied as optical sensors in different areas, although there are difficulties in controlling their responses. In this study, we prepared nanoblends of PDA with triblock copolymers (TC) as a better sensor system for detecting temperature change. The influences of diacetylene (DA) monomer, and the TC chemical structure and concentration on the colorimetric response (CR) were examined. The TC/PDA nanoblend was remarkably more sensitive to temperature change, than classical vesicles. A higher L64 concentration of 12.0% (w/w) reduced the chromatic transition temperature (Ttr) to as low as 24°C. When using different TCs, the Ttr values can be ordered as L35

Kinetics and thermodynamics of bovine serum albumin interactions with Congo red dye.

To optimize the therapeutic applications of Congo red (CR), a potential inhibitor of protein aggregation, the kinetics and thermodynamics of the interactions between CR and a model protein need to be understood. We used surface plasmon resonance (SPR) and fluorescence techniques to determine the dynamics and thermodynamic parameters for the formation of complexes between CR and bovine serum albumin (BSA). CR interacts with BSA through a transition complex; the activation energy for association (Eact(a)) was determined to be 35.88kJmol-1, while the activation enthalpy (ΔH‡), entropy (ΔS‡), and Gibbs free energy (ΔG‡) are 33.41kJmol-1, 0.18Jmol-1K-1, and 33.35kJmol-1, respectively. When this intermediate transforms into the final CR-BSA complex, the entropy of the system increases and part of the absorbed energy is released; this process is associated with a reverse activation energy (Eact(d)) of 20.17kJmol-1, and values of ΔH‡, ΔS‡, and ΔG‡ of 17.69kJmol-1, -162.86Jmol-1K-1, and 66.25kJmol-1, respectively. A comparison of the SPR and fluorescence results suggests that there is more than one site where BSA interacts with CR.

Interaction of cinnamic acid and methyl cinnamate with bovine serum albumin: A thermodynamic approach.

Cinnamic acid (CA) and methyl cinnamate (MC) have attracted interest of researchers because of their broad therapeutic functions. Here, we investigated the interaction of CA and MC with bovine serum albumin (BSA) at pH 3.5, 5.0, and 7.4 using fluorescence spectroscopy, differential scanning nanocalorimetry, and measurements of interfacial tension, size, and zeta potential. BSA formed a complex with the ligands with stoichiometry of approximately 1.0. At pH 7.4, CA-BSA complex formation was entropically driven. The interaction between MC and BSA was more favorable than with CA and was enthalpically driven under the same conditions. The pH played an important role in BSA conformation, which altered the manner in which it interacts with the ligands. Interestingly, both CA and MC had no effect on the surface tension of BSA/air interfaces. These data contribute to the knowledge of CA/MC-BSA interactions and provide important data for application in the food industry.

Binding thermodynamics of synthetic dye Allura Red with bovine serum albumin.

The interaction between Allura Red and bovine serum albumin (BSA) was studied in vitro at pH 7.4. The fluorescence quenching was classified as static quenching due to the formation of AR-BSA complex, with binding constant (K) ranging from 3.26±0.09 to 8.08±0.0610(4)L.mol(-1), at the warfarin binding site of BSA. This complex formation was driven by increasing entropy. Isothermal titration calorimetric measurements also showed an enthalpic contribution. The Allura Red diffusion coefficient determined by the Taylor-Aris technique corroborated these results because it reduced with increasing BSA concentration. Interfacial tension measurements showed that the AR-BSA complex presented surface activity, since interfacial tension of the water-air interface decreased as the colorant concentration increased. This technique also provided a complexation stoichiometry similar to those obtained by fluorimetric experiments. This work contributes to the knowledge of interactions between BSA and azo colorants under physiological conditions.

Polydiacetylene/triblock copolymer nanosensor for the detection of native and free bovine serum albumin.

Bovine serum albumin (BSA) has been recognized as a marker of the cow's health, milk quality, an allergenic protein and as a carrier. Its detection is important in the food, pharmaceutical and medical industries. However, traditional techniques used to detect BSA are often time-consuming, expensive, and show limited sensitivity. This paper describes properties of polydiacetylene-triblock copolymer (L64) nanosensors, synthesized to easily detect BSA. Sensor efficiency was studied as a function of nanosensor composition, polydiacetylene chemical structures, BSA conformation and hydrophobic domain availability, using spectroscopic, calorimetric, light scattering, and electrokinetic analyses. Nanosensors were sensitive to detect the average BSA concentration of milk and dairy products and discriminated between native and denatured protein through naked-eye detectable blue-to-red transition. The standard Gibbs free energy (-10.44<ΔG°<-49.52kJM), stoichiometry complex (1<"n"<3), and binding constant (6.7×102

Polydiacetylene/triblock copolymer nanoblend applied as a sensor for micellar casein: A thermodynamic approach.

Polydiacetylene (PDA) and triblock copolymer nanoblends were synthesized to detect micellar casein (MC), the main milk protein and an indicator of milk quality. UV-Vis spectrum showed that MC induced blue-to-red transition in nanoblends. When nanoblends and MC were separated by dialysis membrane colorimetric response (CR) was similar, whereas a remarkable CR reduction was noticed after addition of dialyzed-MC, suggesting that small molecules present in MC (salts) caused PDA color change. Interaction enthalpy variation between nanoblends and MC showed an abrupt increase that coincided with MC concentration when colorimetric transition occurred. Copolymer hydrophobic/hydrophilic balance and presence of other molecules in the system affected nanoblends CR. MC salts were found to interact with nanoblends leading to color changes. MC concentration, MC salt release, copolymer hydrophobic/hydrophilic balance, and presence of other molecules in the system affected responses of the sensors. These results contribute to future applications of PDA/copolymer nanosensors to dairy models.

Effect of 1-Butyl-3-methylimidazolium Halide on the Relative Stability between Sodium Dodecyl Sulfate Micelles and Sodium Dodecyl Sulfate-Poly(ethylene oxide) Nanoaggregates.

It is well-known that ionic liquids (ILs) alter the properties of aqueous systems containing only surfactants. However, the effect of ILs on polymer-surfactant systems is still unknown. Here, the effect of 1-butyl-3-methylimidazolium bromide (bmimBr) and chloride (bmimCl) on the micellization of sodium dodecyl sulfate (SDS) and its interaction with poly(ethylene oxide) (PEO) was evaluated using conductimetry, fluorimetry, and isothermal titration calorimetry. The ILs decreased the critical micellar concentration (cmc) of the surfactant, stabilizing the SDS micelles. A second critical concentration (c2thc) was verified at high SDS concentrations, due to the micelle size decrease. The stability of PEO/SDS aggregates was also affected by ILs, and the critical aggregation concentration (cac) of SDS increased. Integral aggregation enthalpy changed from -0.72 in water to 2.16 kJ mol(-1) in 4.00 mM bmimBr. IL anions did not affect the SDS micellization or the beginning of PEO/SDS aggregation. Nevertheless, when chloride was replaced with bromide, the amount of SDS bound to the polymer increased. At 100.0 mM IL, the PEO-SDS interaction vanished. We suggest that the effect of ILs comes from participating in the structure of the formed aggregates, interacting with the SDS monomers at the core/interface of the micelles, and promoting preferential solvation of the polymer.

Tradução e validação para a língua portuguesa da escala de neofobia em relação à tecnologia de alimentos: food technology neophobia scale / Translation and validation to portuguese language of food technology neophobia scale

As indústrias de alimentos vêm inovando e desenvolvendo novos produtos e processamentos, e os consumidores estão mais conscientes e preocupados em relação às novas tecnologias alimentares, o que pode influenciar a aceitação dos alimentos. Nesse contexto, objetivou-se disponibilizar para a língua portuguesa o questionário originalmente desenvolvido em inglês que avalia a neofobia em relação à tecnologia de alimentos, denominado Food Technology Neophobia Scale (FNTS). O instrumento original composto por treze afirmações foi inicialmente traduzido para o português por três indivíduos bilíngues, de forma independente; na sequência, as versões em português foram traduzidas novamente para o inglês por outros três indivíduos bilíngues, também de forma independente. Procedeu-se então à análise das versões e ajustes para se obter uma única versão em português com equivalência conceitual e linguística, a qual recebeu o nome de Escala de Neofobia em relação à Tecnologia de Alimentos. As versões original e traduzida foram aplicadas a 30 indivíduos bilíngues para avaliação da confiabilidade e reprodutibilidade do questionário. Os resultados obtidos demonstraram que a tradução do instrumento foi adequada e confiável, podendo, portanto, ser empregada em estudos com consumidores brasileiros.

The food industries have been innovating and developing new products and processes.Consumers are aware and well concerned about new food technologies, which can influence food acceptance . In this context, the objective was to provide a portuguese version of the questionnaire developed in English to evaluate neophobia for food technology called Food Technology Neophobia Scale (FNTS). The original instrument consists of thirteen items and was initially translated into Portuguese by three bilingual individuals independently. Following the Portuguese versions were translated back into English by three other bilingual individuals, also independently. Analysis of versions and adjustments were performed to obtain a single version in Portuguese with linguistic and conceptual equivalence, which was called "Escala de Neofobia em relação à Tecnologia de Alimentos". The original and translated versions were applied to 30 bilingual individuals to evaluate the reliability and reproducibility of the questionnaire. The results showed that the translation of the instrument was adequate and reliable, therefore can be used in studies with Brazilian consumers.

Work of adhesion of dairy products on stainless steel surface

The adhesion of the solids presents in food can difficult the process of surface cleaning and promotes the bacterial adhesion process and can trigger health problems. In our study, we used UHT whole milk, chocolate based milk and infant formula to evaluate the adhesion of Enterobacter sakazakii on stainless steel coupons, and we determine the work of adhesion by measuring the contact angle as well as measured the interfacial tension of the samples. Inaddition we evaluated the hydrophobicity of stainless steel after pre-conditioning with milk samples mentioned. E. sakazakii was able to adhere to stainless steel in large numbers in the presence of dairy products. The chocolate based milk obtained the lower contact angle with stainless steel surface, higher interfacial tension and consequently higher adhesion work. It was verified a tendency of decreasing the interfacial tension as a function of the increasing of protein content. The pre-conditioning of the stainless steel coupons with milk samples changed the hydrophobic characteristics of the surfaces and became them hydrophilic. Therefore, variations in the composition of the milk products affect parameters important that can influence the procedure of hygiene in surface used in food industry.

Acceptance of microfiltered milk by consumers aged from 7 to 70 years

Microfiltration of milk reduces its microbial load providing a longer shelf life and preserving its nutritional and sensory characteristics. The present study compared the effect of the microfiltration treatment and of the milk pasteurization regarding the sensory acceptability by consumers aged from 7 to 70 years using a 7-point hedonic scale. The obtained results were evaluated by variance analysis and Duncan’stest. Microbiological, acidity, instrumental color and heat treatment extent analyses were also performed. Microfiltered milk showed a higher microbial counting reduction and lower acidity; and lesser change incolor coordinates was found when compared to pasteurized milk, indicating the lack of reactions causedby heating. In the sensory acceptability, two groups were formed (p > 0.05) for microfiltered milk, being a group consisted of children, adolescents and elderly, who rated the highest sensory scores, and these cond one formed by adults. Comparing the two kinds of milk, pasteurized and microfiltered samples, no difference in the acceptation was found only in the group constituted by children. These findings highlights the importance in assessing the sensory quality of milk, seeing that the sensory perception is linked with the consumer purchase choice.