Stability of Casein Micelles Cross-Linked by Transglutaminase

Smiddy, Mary; Martin, Janet L.; Kelly, Alan L.; Kruif, C. G. de; Huppertz, Thom

doi:10.3168/jds.s0022-0302(06)72258-5

Cited by 111 publications

(81 citation statements)

References 39 publications

(47 reference statements)

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“…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]. This was also shown for cross-linking with laccase [35,98,99].…”

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 85%

“…Corresponding bands may also be identified in mixed system, but overall resolution is rather poor because the variety of heteropolymers causes a pronounced smear. Furthermore, very large polymers cannot penetrate the separating or stacking gel and remain as condensed stains at the top (Figure 7a,b; see also [89][90][91], which may even result in a loss of sample material [92,93]. The separation limit can be slightly expanded by decreasing the pore size of the gel matrix (reduction of acrylamide concentration) or by using a gradient gel (compare Figure 7a,b), but a thorough analysis of high molar mass casein polymers by SDS-PAGE is not possible since even low acrylamide concentrations of typical stacking gels (40 mg/mL) can hardly be reduced without limiting practicability.…”

Section: Advantages and Limitations In The Context Of Casein Investigmentioning

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: 85%

Section: Advantages and Limitations In The Context Of Casein Investigmentioning

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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“…For micellar casein, the order of susceptibility to TGase-induced cross-linking is κ-CN > β-CN > α s -CN, which is predominantly related to the easy of accessibility of the caseins for the enzyme [131]. Lightscattering measurements have shown that, in unconcentrated milk, cross-linking of micellar caseins is exclusively intramicellar and not inter-micellar [64].…”

Section: Applications Of Transglutaminase In Cheese-makingmentioning

confidence: 99%

“…Lightscattering measurements have shown that, in unconcentrated milk, cross-linking of micellar caseins is exclusively intramicellar and not inter-micellar [64]. This intra-micellar cross-linking stabilizes the micelle against disintegration under unfavourable conditions [64,131] and also has major implications for the hairy brush, consisting predominantly of κ-CN, which provides colloidal stability to the micelle [64].…”

Section: Applications Of Transglutaminase In Cheese-makingmentioning

confidence: 99%

Pre-treatment of cheese milk: principles and developments

Kelly

Huppertz

Sheehan

2008

Dairy Sci. Technol.

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-Classically, very few pre-treatments are applied to milk for cheese-making, with some cheese varieties simply made from raw whole milk, but most made from pasteurised milk of which the composition (e.g., fat:protein ratio) may have been standardized. However, there has been consistent interest in more novel and sophisticated strategies for pre-treatment of cheese-milk. Approaches explored include the use of alternative processing technologies (e.g., membrane filtration, high-pressure treatment, homogenisation, heat treatments more severe than pasteurisation) or addition of sources of protein or milk solids (e.g., milk powders, whey protein products) or enzymes. The principal reasons for such pre-treatments of cheese-milk are: (1) to control the microbiology of the raw milk and the resulting cheese better than is possible by pasteurisation (e.g., inactivation or removal of spores, control of non-starter lactic acid bacteria); (2) increasing the yield of cheese, e.g., through heat-or pressure-induced incorporation of whey proteins, or enhancing sensory properties of reduced fat cheese by direct addition of microparticulated whey proteins; (3) manipulation of cheese ripening, e.g., reducing the likelihood of off-flavour development by inactivation of enzymes or accelerating ripening through increasing enzyme-substrate interactions; or (4) improving the texture and other functional properties, e.g., melting. Finally, the considerations for manufacture and ripening of different cheese varieties, or sub-classes of specific varieties (e.g., low-fat cheese) will clearly differ and add to the complexity of the technological options available. This article will review the key principles for pre-treatment of cheese-milk, as summarised briefly above. Résumé -Pré-traitement du lait de fabrication de fromage : principes et avancées.Classiquement, très peu de pré-traitements sont appliqués au lait de fabrication de fromage : quelques variétés de fromage sont faites simplement à partir de lait entier cru, mais la plupart d'entre elles sont fabriquées à partir de lait pasteurisé dont la composition (par exemple rapport matière grasse/protéine) a pu être standardisée. Cependant, un intérêt constant s'est manifesté pour des stratégies nouvelles et plus sophistiquées pour le pré-traitement du lait de fromagerie. Les approches explorées incluent l'utilisation de technologies de traitement alternatives (par exemple filtration membranaire, haute pression, homogénéisation, traitements thermiques plus sévères que la pasteurisation) ou addition de sources de protéines ou de matière sèche de lait (par exemple poudres de lait, protéines de lactosérum) ou d'enzymes. Les principales raisons de tels pré-traitements du lait de fabrication fromagère sont : (1) de contrôler la microbiologie du lait cru et du fromage résul-tant, mieux que ce qui est possible par pasteurisation (par exemple inactivation ou retrait des spores, contrôle des bactéries lactiques non levain) ; (2) d'accroître le rendement en fromage, par exemple en induisant...

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“…insoluble phosphoproteins organized in complex multi-molecular aggregates, named micelles, that at certain conditions of temperature and acidity (T ~ 20 ºC, pH = 4.6), precipitate from skim milk (Thompson et al 1965). Besides caseins, micelles contain inorganic materials such as calcium phosphate and calcium citrate (Smiddy et al 2006). In ruminants, four casein types have been distinguished so far : S1-casein (CSN1S1), S2-casein (CSN1S2), -casein (CSN2) and κ-casein (CSN3).…”

Section: Introductionmentioning

confidence: 99%