Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard, Camille; Gaucheron, Frédéric

doi:10.1007/s13594-015-0220-y

Cited by 251 publications

(148 citation statements)

References 217 publications

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“…For instance, Tang et al [89] studied the susceptibility of non-micellar sodium caseinate to TGase, but the determined order of κ-casein > α S -casein > β-casein might rather be a result of false band assignments. In spite of studies that have shown an order of β-casein > α S -casein > κ-casein, e.g., [77,78,80], this information is still cited in the literature, e.g., [27,102]. On the other hand, it is generally acknowledged that κ-casein is most susceptible to TGase in case of micellar casein because of high accessibility on the micelle surface, e.g., [78,92,[103][104][105][106][107][108].…”

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

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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 Cross-linked Caseinmentioning

confidence: 99%

“…This may be achieved through acid precipitation of casein at pH 4.6 [53], which does not affect native whey proteins. After heat treatment, however, β-lactoglobulin is covalently attached to κ-casein via disulphide bonds and will therefore precipitate together with casein [102].…”

Section: Literature Review Of Studies On Cross-linked 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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“…Such modifications induce the increase of hydrophilicity, ability to dissociation, evenness of distribution of the surface charge and, correspondingly, correction of functional-technological properties [8,9].…”

Section: Food Science and Technologymentioning

confidence: 99%

Study of Influence of Calcium Content in Milk on Quality Indicators of Cottage Cheese

Grynchenko

Tyutyukova

Pyvovarov

2017

EUREKA: Life Sciences

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The analysis was realized, and the dependence between the calcium content and organoleptic and functional-technological properties of milk as a raw material for producing sour milk cheese was determined. It was demonstrated, that alongside with other factors, the important role in milk clotting belongs to calcium, which role is in binding of free OH-groups of phosphoric acid of casein micelles. As a result of the aforesaid, their negative charge and colloid stability decrease with further hydrophilicity decrease with further aggregation of casein molecules. It was established, that the excessive content of calcium in milk is negative that is manifested in formation of the dry and brittle consistence of sour milk cheese. There was offered the way of calcium content regulation in milk by its decalcification using the natural sorbent of sodium alginate. Regulation of the milk salt system, especially, the calcium content as an initial raw material for producing sour milk cheese by the change of the content and condition of calcium allowed to correct parameters of the process of sour milk cheese making and its functional-technological properties, especially, moisture-keeping ability, form stability and other. It was established, that the decrease of the calcium content in milk provides getting sour milk cheese with the soft, easily smearing consistence, without whey separation. The obtained data on the characteristic of organoleptic indicators fully correlate with studies of the microstructure and dispersity of sour milk cheese. It was determined, that milk decalcification results in raising dispersity of sour milk cheese at the synchronous increase of the percent content of protein particles with minimal size characteristics in the system. It was elucidated, that the microstructure of studied samples consists of protein grains of the same form, evenly distributed by the whole volume. Based on the obtained experimental data, there were corrected parameters of the technological process of sour milk cheese production. There were elaborated ways of formation of the culinary products assortment on the base of sour milk cheese, produced of decalcified milk.

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“…Yn-CN = (mtotal CN * Pn-CN) / (mMCN * ctotal protein, MCN) * 100 (2) where mtotal,CN refers to the mass of the obtained n-casein fraction, mMCN to the initial mass of micellar casein (MCN) powder used for the isolation, while ctotal protein, MCN refers to the calculated protein content of the micellar casein using the measured the nitrogen content. The recovery (Rn-CN) of each casein fraction is calculated according to Rn-CN = (Yn-CN, fraction / cn-CN, MCN) * 100…”

Section: Calculationsmentioning

confidence: 99%

“…Caseins are widely used in food and non-food applications. They have various important technofunctional properties such as solubility, emulsification, foam formation and stabilization, waterbinding, gelation, heat and acid stability [2][3][4]. They also play an important role in non-food applications such as the production of plastic materials [5], textile fibers [6] and glues [7].…”

Section: Introductionmentioning

confidence: 99%

Untitled

2017

AFSHN

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Abstract:The fractions of caseins (αs-, β-and κ-) are widely used in food applications due to their physiochemical properties as well as their bio-and techno-functional properties. Especially, β-casein fraction is a precursor having a variety of bioactive peptides such as antihypertensive and opioid. Different methods have been established in isolating and purifying the casein fractions, particularly on β-casein isolation. However, the obtained yield for each fraction still requires further improvement. The aim of this study was to increase the yield and purity of the fractions by constructing a set of experiments on technical scale and determining the main process parameters. Based on our previous studies on laboratory scale, a method for the technical scale isolation of casein fractions from micellar casein powder was developed. A comparable yield and purity values for β-casein were obtained.

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Modifications of structures and functions of caseins: a scientific and technological challenge

Cited by 251 publications

References 217 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

Study of Influence of Calcium Content in Milk on Quality Indicators of Cottage Cheese

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