Gradual disaggregation of the casein micelle improves its emulsifying capacity and decreases the stability of dairy emulsions

Lazzaro, Fanny; Saint‐Jalmes, Arnaud; Violleau, Frédéric; Lopez, Christelle; Gaucher-Delmas, Mireille; Madec, Marie‐Noëlle; Beaucher, Eric; Gaucheron, Frédéric

doi:10.1016/j.foodhyd.2016.08.037

Cited by 33 publications

(12 citation statements)

References 53 publications

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“…Nogueira Silva et al [189] and Lazzaro et al [190] applied AF4 for the determination of the particle size distribution of casein aggregates as prepared by partial disintegration of casein micelles, and achieved a separation of intact casein micelles and smaller compounds, which became more abundant with decreasing pH or increasing concentration of trisodium citrate as a consequence of casein micelle dissociation. Guyomarc'h et al [191] used AF4 in comparison with SEC for the characterisation of unheated and heated skim milk.…”

Section: Literature Review Of Studies On Caseinmentioning

confidence: 99%

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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Abstract:Casein is the major protein fraction in milk, and its cross-linking has been a topic of scientific interest for many years. Enzymatic cross-linking has huge potential to modify relevant techno-functional properties of casein, whereas non-enzymatic cross-linking occurs naturally during the storage and processing of milk and dairy products. Two size separation techniques were applied for characterisation of these reactions: gel electrophoresis and size exclusion chromatography. This review summarises their separation principles and discusses the outcome of studies on cross-linked casein from the last~20 years. Both methods, however, show limitations concerning separation range and are applied mainly under denaturing and reducing conditions. In contrast, field flow fractionation has a broad separation range and can be easily applied under native conditions. Although this method has become a powerful tool in polymer and nanoparticle analysis and was used in few studies on casein micelles, it has not yet been applied to investigate cross-linked casein. Finally, the principles and requirements for absolute molar mass determination are reviewed, which will be of increased interest in the future since suitable calibration substances for casein polymers are scarce.

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Section: Literature Review Of Studies On Caseinmentioning

confidence: 99%

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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“…Emulsifiers such as proteins are widely employed in food processing because of their ability to be adsorbed into oil-water interfaces and form interfacial films [7]. The most employed proteins in research and the food industry are whey protein isolate [8], casein [9] and bovine serum albumin [10]. However, over the past few years, a change has been observed in the consumption trends of animal origin products.…”

Section: Introductionmentioning

confidence: 99%

Physical Stability and Interfacial Properties of Oil in Water Emulsion Stabilized with Pea Protein and Fish Skin Gelatin

et al. 2020

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This study aimed to investigate the physical stability and interfacial properties of oil-in-water (O/W) emulsions stabilized with fish skin gelatin (FG) and pea protein (PP) at pH 3. Physico-chemical properties, elemental composition and SDS-PAGE of the proteins were determined in the first part of this work. Emulsions were prepared at different ratio FG: PP (100: 0-75: 25-50: 50-25: 75-0: 100) by mechanical stirring followed by ultrasound treatment. Higher physical stability was observed in the presence of FG (ratio 100: 0), where the O/W were stable~50 h. An average hydrodynamic diameter < 1 μm was found for all the emulsions except for the ratio 75: 25, where it was 2.8 μm. The presence of the protein on the O/W interface was explored by confocal laser scanning microscopy whereas the thermal properties of the protein ratios were analyzed by differential scanning calorimetry. The lower denaturation temperature was observed for ratio 50: 50, which was founded at~89°C, whereas the denaturation temperatures for the others O/W emulsions were in the range of 99 and 108°C. A predominant viscous behavior was observed for all the ratios while a slight decrease of the surface tension was observed in the presence of PP. The equal mixing of FG with PP showed an increase in the emulsifying properties of PP forming a more stable emulsion with lower particle size.

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“…With the average dimension of casein micelles being around 200 nm, SMP dispersions are turbid (Glantz et al, 2010), and the knowledge of the importance of CCP to casein micelle structure can be used to guide the dissociation of casein micelles to reduce dispersion turbidity. Such studies have been focused on disrupting CCP linkages by high hydrostatic pressure (Huppertz and De Kruif, 2007;Orlien et al, 2010;Bravo et al, 2013) or driving the calcium-phosphate balance from CCP in casein micelles to the continuous serum phase by addition of calcium-chelating agents (Panouillé et al, 2005;Kaliappan and Lucey, 2011;Lazzaro et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…Chelators refer to materials that have high affinities to form complexes with cations and, therefore, can displace cations from original binding sites (Gaucheron, 2005). Calcium chelators can be added to milk or other dairy protein dispersions to improve rehydration properties of dairy powder or emulsifying capacity by altering physical interactions surrounding casein micelles (de Kort et al, 2011;Lazzaro et al, 2017;McCarthy et al, 2017). Various calcium chelators can dissociate casein micelles, including EDTA, citrate, and phosphate (Pitkowski et al, 2008;de Kort et al, 2011;Kaliappan and Lucey, 2011).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical properties of skim milk powder dispersions prepared with calcium-chelating sodium tripolyphosphate, trisodium citrate, and sodium hexametaphosphate

Choi

Zhong

2020

Journal of Dairy Science

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Due to health benefits of proteins, the demand for protein beverages has grown rapidly. Translucent protein drinks with neutral pH may have advantages over acidic beverages that may cause dental erosion, and skim milk powder (SMP) is an affordable protein ingredient. Dissociating casein micelles by calcium chelators is a well-known method to reduce SMP dispersion turbidity, but much is to be studied for physicochemical properties as affected by chelator type and concentration. The objective of the present study was to characterize physicochemical properties of dispersions with 5% (wt/vol) SMP after addition of 0 to 30 mM sodium tripolyphosphate, trisodium citrate, or sodium hexametaphosphate. The turbidity was decreased with increasing chelator concentration, with the lowest turbidity observed in the SMP dispersions with sodium hexametaphosphate. The smallest hydrodynamic diameter was observed at an intermediate chelator concentration, resulting from the balance of casein micelle dissociation and aggregation of dissociated caseins induced at an elevated ionic strength. Heating at 90°C for 5 min increased turbidity but lowered hydrodynamic diameter of SMP dispersions, with some exceptions. The morphology of SMP dispersions differed for each chelator and was also affected by chelator concentration and heating. Trisodium citrate was the most effective to demineralize colloidal calcium phosphate in casein micelles, but the amount of dissolved calcium was not directly correlated with the decreased turbidity, indicating different chelating mechanisms by each chelator. Analysis of serum calcium and phosphorus concentrations also suggested that the type and concentration of soluble and insoluble calcium phosphates and their partitioning in the serum and casein micelles were dynamically changed by the studied parameters to affect dispersion turbidity and structures of casein micelles. Findings from the present study may be used to formulate translucent beverages incorporating SMP and other casein micelle ingredients.

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Gradual disaggregation of the casein micelle improves its emulsifying capacity and decreases the stability of dairy emulsions

Abstract: To cite this version:Fanny Lazzaro, Arnaud Saint-Jalmes, Frédéric Violleau, Christelle Lopez, Mireille Gaucher-Delmas, et al.. Gradual disaggregation of the casein micelle improves its emulsifying capacity and decreases the stability of dairy emulsions.

Cited by 33 publications

References 53 publications

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Physical Stability and Interfacial Properties of Oil in Water Emulsion Stabilized with Pea Protein and Fish Skin Gelatin

Physicochemical properties of skim milk powder dispersions prepared with calcium-chelating sodium tripolyphosphate, trisodium citrate, and sodium hexametaphosphate

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