2006
DOI: 10.1016/j.cocis.2005.11.005
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Casein micelle structure: What can be learned from milk synthesis and structural biology?

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Cited by 215 publications
(152 citation statements)
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“…By contrast, crosslinking with transglutaminase appears not to affect casein micelle size or substructure, as measured by a range of scattering methods, and produces particles that are resistant to drastic changes in solvent quality (de Kruif et al, 2012). In protein submicellar models of casein micelle structure, the average separation of the dense substructures, about 18 nm, has been interpreted as the diameter of the submicelles (Stothart and Cebula, 1982;Stothart, 1989;Hansen et al, 1996;Farrell et al, 2006a). Notwithstanding the many difficulties of sample preparation, a number of recent electron microscopical methods have yielded images of casein micelles that do not support any submicelle model but are consistent with nanocluster models (Holt et al, 1978;McMahon and McManus 1998;Marchin et al, 2007;Trejo et al, 2011).…”
Section: Casein Micelle Structurementioning
confidence: 99%
See 1 more Smart Citation
“…By contrast, crosslinking with transglutaminase appears not to affect casein micelle size or substructure, as measured by a range of scattering methods, and produces particles that are resistant to drastic changes in solvent quality (de Kruif et al, 2012). In protein submicellar models of casein micelle structure, the average separation of the dense substructures, about 18 nm, has been interpreted as the diameter of the submicelles (Stothart and Cebula, 1982;Stothart, 1989;Hansen et al, 1996;Farrell et al, 2006a). Notwithstanding the many difficulties of sample preparation, a number of recent electron microscopical methods have yielded images of casein micelles that do not support any submicelle model but are consistent with nanocluster models (Holt et al, 1978;McMahon and McManus 1998;Marchin et al, 2007;Trejo et al, 2011).…”
Section: Casein Micelle Structurementioning
confidence: 99%
“…A diversity of views on the structure of the casein micelle have been expressed in recent reviews from the colloid and food science perspective Horne, 2008;Dalgleish and Corredig, 2012;McMahon and Oommen, 2012) and from a somewhat different biological perspective to that developed here (Farrell et al, 2006a). In this review, we consider the structure of the casein micelle in relation to 3 of its recognized biological functions.…”
Section: Introductionmentioning
confidence: 99%
“…6 The structure of casein micelles has been intensively investigated in the past, and numerous models have been postulated. [7][8][9][10][11][12] In a recent development, the internal assembly and structure of the casein micelle has been described by the dual-binding model. 8 Here two distinct forms of binding are involved in the micellar assembly.…”
Section: Introductionmentioning
confidence: 99%
“…Over the same period, several different competing models, attempting to reconcile and explain a growing body of diverse experimental observations have emerged (Dalgleish, 2011). Despite some fundamental differences between these different models (Farrell, Malin, Brown, & Qi, 2006;Horne, 2006), and various revisions that have been made to them over years, a strikingly common feature that has remained the same is the role that -casein (KC) plays in providing colloidal stability to casein aggregates. It is envisaged that most, if not all of KC fraction resides at the surface of casein micelles.…”
Section: Introductionmentioning
confidence: 99%