Mineral modulation of thermal aggregation 
and gelation of whey proteins: from ?-lactoglobulin 
model system to whey protein isolate

Caussin, Florence; Famelart, Marie-Hélène; Maubois, Jean‐Louis; Bouhallab, Saı̈d

doi:10.1051/lait:2003021

Cited by 30 publications

(19 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The present investigations show that an increase in the gel strength due to a higher salt content is only recognizable with WPI. A considerable increase in the gel firmness of WPI by addition of sodium chloride was also determined by Caussin et al [6]. It is known that addition of NaCl or CaCl 2 to dialyzed solutions of WPC or WPI results in an increase in gel strength until maximum values are reached, and then the gel strength decreases at higher salt concentration.…”

Section: Resultsmentioning

confidence: 65%

See 1 more Smart Citation

A comparative study of the gelation properties of whey protein concentrate and whey protein isolate

Lorenzen¹,

Schrader²

2006

Lait

View full text Add to dashboard Cite

-The present paper describes a comparative study of the gelation properties of whey protein concentrate (WPC) and whey protein isolate (WPI). Penetration measurements as well as rheological studies revealed that the strength of heat-induced gels prepared with WPI was higher than with WPC. In addition, gels with WPI were clearly more elastic than WPC gels. The storage modulus of WPI and the storage and loss moduli of WPC increased with increasing frequency, while the loss modulus of WPI revealed no clear dependence on the frequency, resulting in a greater decrease in the loss angle of WPI with increasing frequency. The superior gelation properties of WPI were mainly due to the higher β-lactoglobulin content as well as to lower fat, lactose and phospholipid contents. However, in this paper it is also discussed whether the low contents of glycomacropeptide, non-protein-nitrogen and proteose peptone in WPI may partly explain the superior gelation properties of these protein products. WPI were more sensible to an increase in the ionic strength (0.1-0.3% NaCl) than WPC, resulting in clearly stronger gels with WPI than with WPC. In the pH ranges of 2-3 and 7-8, elastic and translucent gels could be prepared using WPI, while their gel-forming properties were low between pH 4 and 5. The strongest gels, turbid, but still elastic, were prepared with WPI at pH 6. whey protein concentrate / whey protein isolate / gelation properties Résumé -Présentation d'une étude comparative sur les propriétés de gélification du concentré protéique de lactosérum WPC et de l'isolat protéique de lactosérum WPI. Des mesures de la pénétration ainsi que des études rhéologiques révèlent que la solidité des gels obtenus par gélifi-cation thermique est plus élevée en utilisant WPI que WPC. De plus, les gels avec WPI sont nettement plus élastiques que des gels avec WPC. Le module de stockage de WPI et les modules de stockage et de perte de WPC augmentaient avec une fréquence croissante, tandis que les modules de perte de WPI n'étaient pas influencés par la fréquence, et menaient ainsi à une forte réduction de l'angle de perte de WPI avec une fréquence croissante. Les propriétés supérieures de gélification de WPI sont principalement dues à une teneur élevée en β-lactoglobuline et à une teneur réduite en matière grasse, lactose et phospholipide. Dans l'étude présente, il est également discuté si les faibles teneurs en glycomacropeptide, en azote non-protéique de WPI et en protéose peptone dans WPI expliquent partiellement les propriétés supérieures de gélification de ces produits protéiques. WPI réagissait plus sensiblement à une augmentation de la teneur ionique (0.1-0.3% NaCl) que WPC, aboutissant à des gels ostensiblement plus solides avec WPI qu'avec WPC. Avec un pH entre 2-3 et 7-8, il a été possible de préparer des gels élastiques et translucides en utilisant WPI, tandis que les propriétés gélifiantes étaient faibles avec un pH entre 4-5. Les gels les plus solides, d'un aspect trouble mais encore élastiques, étaient préparés avec WPI à...

show abstract

Section: Resultsmentioning

confidence: 65%

“…[6,9,10,14,17,34,39]. Comparative studies on the compositional, physicochemical and functional properties of whey protein concentrate (WPC) and whey protein isolate (WPI) are also described in the literature e.g.…”

Section: Introductionmentioning

confidence: 99%

A comparative study of the gelation properties of whey protein concentrate and whey protein isolate

Lorenzen¹,

Schrader²

2006

Lait

View full text Add to dashboard Cite

show abstract

“…Holo α‐lactalbumin (holo α‐LA) was purified from bovine whey as reported by Caussin et al . [31]. Apo α‐lactalbumin (apo α‐LA) was prepared by dialysis of a solution of holo α‐LA against deionized water at pH 3 during 48 h at 4 °C using a 6–8000 Da nominal cut‐off membrane (Spectrum Laboratories, Gardena, CA, USA) in order to remove calcium ions.…”

Section: Methodsmentioning

confidence: 99%

Apo α‐lactalbumin and lysozyme are colocalized in their subsequently formed spherical supramolecular assembly

et al. 2007

View full text Add to dashboard Cite

We have reported previously that the calcium‐depleted form of bovine α‐lactalbumin (apo α‐LA) interacts with hen egg‐white lysozyme (LYS) to form spherical supramolecular structures. These supramolecular structures contain an equimolar ratio of the two proteins. We further explore here the organization of these structures. The spherical morphology and size of the assembled LYS/apo α‐LA supramolecular structures were demonstrated using confocal scanning laser microscopy and scanning electron microscopy. From confocal scanning laser microscopy experiments with labelled proteins, it was found that LYS and apo α‐LA were perfectly colocalized and homogeneously distributed throughout the entire three‐dimensional structure of the microspheres formed. The spatial colocalization of the two proteins was also confirmed by the occurrence of a fluorescence resonance energy transfer phenomenon between labelled apo α‐LA and labelled LYS. Polarized light microscopy analysis revealed that the microspheres formed differ from spherulites, a higher order semicrystalline structure. As the molecular mechanism initiating the formation of these microspheres is still unknown, we discuss the potential involvement of a LYS/apo α‐LA heterodimer as a starting block for such a supramolecular assembly.

show abstract

“…Commercial whey protein products, such as WPI or WPC, contain several minerals that may influence their applications in food products. The presence of minerals affects the formation of aggregates in whey protein products that lead to gelation (Caussin and others ). Calcium is one of the minerals that make a significant contribution to whey protein gelation.…”

Section: Approaches To Reduce Aggregation Of Whey Proteinsmentioning

confidence: 99%

Stability of Whey Proteins during Thermal Processing: A Review

Wijayanti

Bansal

Deeth

2014

Comp Rev Food Sci Food Safe

286

186

View full text Add to dashboard Cite

Whey proteins have many benefits due to their high nutritional value and their various applications in food products. A drawback of whey proteins is their instability to thermal processing, which leads to their denaturation, aggregation, and, under some conditions, gelation. As thermal processing is a major treatment in the processing of milk and milk products, its influence on whey proteins has been extensively studied. Understanding the mechanisms involved during each stage of denaturation and aggregation of whey proteins is critical to devising ways of improving their stability. These aspects are reviewed in this paper. Also covered are approaches to preventing or reducing heat-induced aggregation of whey proteins. Inhibition of aggregate formation has considerable potential for alleviating the problems that arise from the instability of whey proteins.

show abstract

Mineral modulation of thermal aggregation and gelation of whey proteins: from ?-lactoglobulin model system to whey protein isolate

Cited by 30 publications

References 27 publications

A comparative study of the gelation properties of whey protein concentrate and whey protein isolate

A comparative study of the gelation properties of whey protein concentrate and whey protein isolate

Apo α‐lactalbumin and lysozyme are colocalized in their subsequently formed spherical supramolecular assembly

Stability of Whey Proteins during Thermal Processing: A Review

Contact Info

Product

Resources

About