Properties of acid casein gels made by acidification with glucono-δ-lactone. 1. Rheological properties

Lucey, J.A.; Vliet, T. van; Grolle, Katja; Geurts, T.J.; Walstra, P.

doi:10.1016/s0958-6946(97)00027-7

Cited by 172 publications

(122 citation statements)

References 13 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…3). These findings are in agreement with the acidinduced aggregation of casein micelles at different temperatures (Haque et al 2001;Lee and Lucey 2004;Lucey et al 1997b;Vétier et al 1997), and the temperatureinduced aggregation of casein submicelles (20-80°C; Panouillé et al 2004) or the growth kinetics of nanocrystals (Lee et al 2006). Thus, temperature plays an important role in the rearrangement of particles which was proposed to be related to the increased mobility due to lower bond energy (Mellema et al 2002).…”

Section: Influence Of the Temperaturesupporting

confidence: 88%

“…In the network consisting of aggregated particle clusters, the protein bonds are dynamic (van Vliet et al 1991), which could lead to rearrangement of particles and clusters on all length scales resulting in particle fusion and an increase of the size of the building blocks (Mellema et al 2002). Higher temperatures may enhance both extensive particle rearrangement during gel formation and the formation of dense clusters of aggregated particles (Lucey et al 1997b). The structure before and immediately after stirring was shown to be crucial for the generated gel fragments upon shearing (Renan et al 2009).…”

Section: Influence Of Temperaturementioning

confidence: 99%

“…Thus, temperature plays an important role in the rearrangement of particles which was proposed to be related to the increased mobility due to lower bond energy (Mellema et al 2002). This, in turn, should increase the collision frequency between particles and, consequently, the number of successful collisions leading to extensive particle rearrangement with increasing temperature (Lucey et al 1997b).…”

Section: Influence Of the Temperaturementioning

confidence: 99%

“…Hydrophobic interactions were shown to be predominant in such acid and acid-rennet microgel suspensions like yogurt or fresh cheese (Hinrichs and Keim 2007). Lucey et al (1997b) reported that at low temperatures casein particles have a higher voluminosity and are probably more deformable, which would allow particles to aggregate with a larger number of protein-protein bonds, thereby causing less rearrangement. In contrast, higher temperatures increase hydrophobic interactions which in principle leads to a stronger driving force for particle fusion (Mellema et al 2002).…”

Section: Influence Of the Temperaturementioning

confidence: 99%

See 3 more Smart Citations

Post-processing of concentrated fermented milk: influence of temperature and holding time on the formation of particle clusters

Hahn

Sramek

Nöbel

et al. 2011

Dairy Science & Technol.

View full text Add to dashboard Cite

Graininess is a common structural defect in microgel suspensions, e.g., yogurt or fresh cheese. The aim of this study was to investigate the impact of the temperature (23-54°C) and the holding time (1-300 min) on the formation of particle clusters in concentrated, fermented milk (protein content 8.2% (w/w)) during post-processing. Since graininess is correlated with the presence of large protein aggregates, temperature treatment during post-processing was varied systematically to promote particle growth and the particle size d 75.3 was measured. The samples revealed a polydisperse particle size distribution present at all temperatures and holding times. With longer holding times, rearrangement led to larger particle clusters while the number of smaller particles decreased. The increase in the d 75.3 was fitted with a power law function while higher temperatures promoted both the aggregation rate and the particle size. By using the Arrhenius equation, the activation energy, E A , was calculated (26 kJ.mol −1 ), which was in agreement with the aggregation kinetics occurring at smaller scales, e.g., the acid-induced aggregation of casein micelles and the temperature-induced aggregation of casein submicelles. According to the activation energy, the particle growth in microgel suspensions was proposed to be predominantly diffusion-limited. The results of this study imply that particle size during post-processing is adjustable. Furthermore, the particle size increases with increasing temperature load, thus, rapid cooling reduces the Dairy Sci. & Technol. (2012) 92:91-107 DOI 10.1007/s13594-011-0046-

show abstract

Section: Influence Of the Temperaturesupporting

confidence: 88%

Section: Influence Of Temperaturementioning

confidence: 99%

Section: Influence Of the Temperaturementioning

confidence: 99%

Section: Influence Of the Temperaturementioning

confidence: 99%

See 2 more Smart Citations

Post-processing of concentrated fermented milk: influence of temperature and holding time on the formation of particle clusters

Hahn

Sramek

Nöbel

et al. 2011

Dairy Science & Technol.

View full text Add to dashboard Cite

show abstract

“…The gelation time and the moduli decrease, the gelation pH increases and the elastic properties decrease slightly when the incubation temperature increases [5,6]. When the concentration of GDL increases, tan d and the pH at gelation increase [5] and G' slightly decreases [26]. According to Lucey et al [27], a faster gelation, such as that performed at 40°C compared with 20°C, is commonly regarded as conditions leading to coarser networks [27].…”

Section: Introductionmentioning

confidence: 99%

Article

Laligant

Famelart

Pâquet

et al. 2003

Lait

View full text Add to dashboard Cite

-The behaviour of heat-treated skim milk towards acidification by fermentation with lactic bacteria was studied at 30°C and 42°C. Rheological changes using dynamic oscillations and 1 H-NMR relaxation time, T2, were studied with time and pH. Front-face intrinsic fluorescence measurements studied with principal component analysis were performed during fermentation. The gel was formed at 42°C at a shorter time and a higher pH (5.53 ± 0.01) than at 30°C (5.24 ± 0.13). The maximum in tan d was higher at 42°C than at 30°C, but the G' values at pH 4.6 were the same at the two temperatures. The changes in T2 with pH were not greatly different at the two temperatures, but the dT2/dpH curves showed some differences with the temperature. The changes in T2 were due to the changes in the particle structure caused by the fermentation and were correlated with calcium solubilisation. Front-face fluorescence can detect a first shift of the maximal intensity toward lower wavelengths and a second shift toward longer wavelengths. These shifts were separated by the gel point and were due to changes in the environment of tryptophan residues in the protein chains. The discussion of these results and the comparison with GDL-induced gels take into account the limitation of the transfer of the acid and the protons from the aqueous to the colloidal phase and the subsequent heterogeneity of the gel.Milk / yoghurt / pH / 1 H-NMR / rheology / intrinsic fluorescence Résumé -Fermentation de lait reconstitué et chauffé par des bactéries lactiques à deux températures. II. Approche dynamique de la construction du gel. Le comportement du lait écrémé traité thermiquement au cours de l'acidification par des bactéries lactiques est étudié à 30 et 42°C. Les modifications rhéologiques par oscillations dynamiques et le temps de relaxation T2 en RMN du proton sont étudiés en fonction du temps et du pH. La fluorescence frontale intrinsèque étudiée conjointement avec l'analyse en composantes principales a été suivie au cours de la fermentation. La gélification du lait apparaît à un temps plus court et un pH plus élevé à 42°C (5,53 ± 0,01) qu'à 30°C (5,24 ± 0,13). Le pic de maximum de tan d était plus marqué à 42 qu'à 30°C, mais le G' à pH 4,6 avait la même valeur aux deux températures. Les changements de T2 au cours * Correspondence and reprints E-mail: famelart@rennes.inra.fr 308 A. Laligant et al.de l'acidification étaient peu différents aux deux températures étudiées, mais les courbes dT2/dpH montrent quelques différences entre 42 et 30°C. Les changements de T2 sont dus à des changements de structure de la particule provoqués par la fermentation et sont corrélés à la solubilisation du calcium. La fluorescence frontale détecte un premier décalage des spectres vers des longueurs d'onde plus petites puis un décalage vers des longueurs d'onde plus grandes. Le point associé à l'inversion de l'environnement des tryptophanes des chaînes protéiques correspond au point de gel. Ces résultats et les différences avec des gels acides obtenus par l'addition ...

show abstract

Utilizing Dairy Protein Functionality in Food Microstructure Design

Golding

2013

Advances in Dairy Ingredients

View full text Add to dashboard Cite

Properties of acid casein gels made by acidification with glucono-δ-lactone. 1. Rheological properties

Cited by 172 publications

References 13 publications

Post-processing of concentrated fermented milk: influence of temperature and holding time on the formation of particle clusters

Post-processing of concentrated fermented milk: influence of temperature and holding time on the formation of particle clusters

Article

Utilizing Dairy Protein Functionality in Food Microstructure Design

Contact Info

Product

Resources

About