Caseins, Caseinates and Micellar Casein

Raak, Norbert; Corredig, Milena

doi:10.1016/b978-0-12-818766-1.00135-5

Cited by 7 publications

(4 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lauzin et al (2020) also found a slight reduction in soluble casein (5% of total) and significantly (P < 0.05) lower Ca and P (% of total) in the serum phase of $2× concentrated skim milk by UF and RO compared with that of skim milk, although the authors claimed there was no change in protein equilibrium. Others claimed that internal structural rearrangements or equilibration cause the release of some micellar casein and Ca-phosphate into the serum phase especially in combination with diafiltration using water (Srilaorku et al 1991;Singh 2007;Ferrer et al 2011Ferrer et al , 2014Li et al 2015;Lin et al 2015;Nair and Corredig 2015;Cos ¸kun et al 2022;Raak et al 2023aRaak et al , 2023b. The solubilisation of caseins was attributed to micellar rearrangements induced by shear and/or pressure and changes in ionic equilibrium (the reverse is also true i.e.…”

Section: Approaches To Standardisation Of Cheese Milkmentioning

confidence: 99%

“…The solubilisation of caseins was attributed to micellar rearrangements induced by shear and/or pressure and changes in ionic equilibrium (the reverse is also true i.e. dissociation of caseins from micelles causes micellar rearrangements) and was found to be limited by increasing the transmembrane pressure during MF (Raak et al 2023a(Raak et al , 2023b. In contrast, a most recent study (Raak et al 2023a) on MCC (concentrated 2-4×) revealed that the integrity of casein micelles is more preserved when UF permeate is used during diafiltration.…”

Section: Approaches To Standardisation Of Cheese Milkmentioning

confidence: 99%

See 1 more Smart Citation

Partitioning of casein and fat in Cheddar cheese manufacturing as affected by cheese milk standardisation: A review

Kayihura

2023

Int J of Dairy Tech

View full text Add to dashboard Cite

Cheesemaking offers the opportunity to exploit the unique nutritional, sensory, biological and other functionalities of both cheese and whey‐derived products. Milk standardisation is one of the essential cheesemaking operations designed to preserve the intrinsic cheese quality and may also improve whey composition because of its impact on partitioning of milk constituents between the two coproducts. The effectiveness of cheese milk standardisation in controlling constituent partitioning depends on the method and ingredients selected. This review explores how and why cheese milk standardisation affects the partitioning of casein and fat in Cheddar cheese and provides some perspective on a better approach.

show abstract

Section: Approaches To Standardisation Of Cheese Milkmentioning

confidence: 99%

Section: Approaches To Standardisation Of Cheese Milkmentioning

confidence: 99%

Partitioning of casein and fat in Cheddar cheese manufacturing as affected by cheese milk standardisation: A review

Kayihura

2023

Int J of Dairy Tech

View full text Add to dashboard Cite

show abstract

“…In microfiltration, skimmed milk is passed over a membrane layer with pores large enough to allow for the transmission of whey proteins and small molecular weight constituents, which are typically 0.08-0.2 µm, to increase the casein micelle fraction. This process is often combined with diafiltration, which is the introduction of water or other media to enhance the transmission of permeable compounds while maintaining high efficiencies [1]. Microfiltration in combination with diafiltration is a common way to produce micellar casein concentrates (MCCs), i.e., milk protein concentrates with an increased ratio of casein to whey proteins [2,3].…”

Section: Introductionmentioning

confidence: 99%

Transmembrane Pressure during Micro- and Diafiltration of Milk Affects the Release of Non-Sedimentable Caseins

Raak

Coşkun

Corredig

2023

Foods

View full text Add to dashboard Cite

Membrane filtration, especially in combination with diafiltration, can affect the colloidal structure of casein micelles in milk and concentrated milks. The partial dissociation of casein proteins from the casein micelles into the serum phase has been shown to depend on diafiltration conditions. This dissociation can affect the technological functionality of the milk concentrates. The present study aimed at determining the contribution of the gel layer deposited onto the membrane during filtration in the colloidal equilibrium between soluble and micellar caseins. Skimmed milk was concentrated by microfiltration combined with diafiltration using a cross-flow spiral-wound membrane at two transmembrane pressure (TMP) levels, causing differences in the extent of the gel layer formed. Non-sedimentable casein aggregates were formed to a greater extent at a low TMP compared to a high operating TMP. This difference was attributed to the greater compression of the deposit layer during filtration at a high TMP. This study contributes new knowledge to the understanding of how to modulate the functionality of milk concentrates through the control of processing conditions.

show abstract

“…While membrane separated casein (MC) was a functional natural milk protein isolate powder obtained by membrane ltration of skim milk. And membrane ltration can maintain the original structure of casein micelles to a large extent (Raak & Corredig, 2022).…”

Section: Introductionmentioning

confidence: 99%

Effect of hydrolysis and succinylation on the stability of dual-modified rennet casein and membrane separated casein emulsions under different environments

Hou

et al. 2022

Preprint

View full text Add to dashboard Cite

Casein is a common ingredient and can be used to improve the stability of dairy products. However, the poor solubility and emulsification properties of casein limit its further application. Therefore, modification of casein to improve its application properties is important. In this study, hydrolysis and succinylation were used to modify the casein separated with different methods (rennet casein (RC) and membrane separated casein (MC)). And Turbiscan stability index (TSI), salt ion (Na+) stability, freeze-thaw stability and storage stability of emulsions prepared by RC and MC were investigated. The results showed that succinylation modified protein structure and improved the stability of oil-in-water emulsions prepared by succinylated casein and succinylated casein hydrolysates. The TSI of succinylated rennet casein (RC-SA) and succinylation of membrane separated casein hydrolysates (MC-CHs-SA) stabilized emulsions showed a better stability. Protein succinylation could prevent adsorption and aggregation between droplets, improving the Na+ stability and storage stability of the emulsion. Succinylated casein had the best emulsification activity and emulsion stability. And the solubility of succinylated casein hydrolysates was significantly improved compared with succinylated casein. Emulsions prepared with succinylated RC hydrolysates had the smallest particle size and a more uniform particle size distribution compared with other samples. Succinylated MC hydrolyzates showed the best freeze-thaw stability. Therefore, hydrolysis could reduce the molecular weight of casein and significantly improved the solubility of succinylated casein, and succinylation could modify the protein structure and significantly improved the emulsion stability. Overall, hydrolysis and succinylation can be applied to modify casein to effectively improve the application properties in emulsion system.

show abstract

Caseins, Caseinates and Micellar Casein

Cited by 7 publications

References 21 publications

Partitioning of casein and fat in Cheddar cheese manufacturing as affected by cheese milk standardisation: A review

Partitioning of casein and fat in Cheddar cheese manufacturing as affected by cheese milk standardisation: A review

Transmembrane Pressure during Micro- and Diafiltration of Milk Affects the Release of Non-Sedimentable Caseins

Effect of hydrolysis and succinylation on the stability of dual-modified rennet casein and membrane separated casein emulsions under different environments

Contact Info

Product

Resources

About