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Genetic polymorphism of kappa casein and casein micelle size in the Bulgarian Rhodopean cattle breed [PDF]

open access: yesBiotechnology in Animal Husbandry, 2014
The present study aimed to compare the size of casein micelle in cow milk sample in function of kappa casein (CSN3) genetic polymorphism. Sixteen cows from Bulgarian Rhodopean cattle breed were genotyped by PCR-RFLP analysis.
Hristov P.   +5 more
doaj   +2 more sources

The influence of high temperatures on milk proteins [PDF]

open access: yesHemijska Industrija, 2002
High temperatures Induce certain changes in milk constituents, but the degree of these changes depends on both the temperature and time of heat treatment. The most pronounced changes take place in milk proteins. The forewarming of milk causes an increase
Maćej Ognjen D.   +2 more
doaj   +1 more source

Sodium caseinate hinders chymosin-induced aggregation of caseins in concentrated milk: The role of soluble caseins and calcium ions

open access: yesJDS Communications, 2021
Concentrated casein micelle suspensions show an altered balance between the colloidal and soluble phases compared with native skim milk. The objective of this research was to probe the role of such a change on the chymosin-driven destabilization of ...
P. Krishnankutty Nair, M. Corredig
doaj   +1 more source

Linking variation in the casein fraction and salt composition to casein micelle size in milk of Dutch dairy goats

open access: yesJournal of Dairy Science
: The casein composition, salt composition, and micelle size varies substantially between milk samples of individual animals. In goats, the links between those casein characteristics are unknown and could provide useful insights into goat casein micelle ...
Swantje Breunig   +4 more
doaj   +1 more source

Structure of biomimetic casein micelles: Critical tests of the hydrophobic colloid and multivalent-binding models using recombinant deuterated and phosphorylated β-casein

open access: yesJournal of Structural Biology: X
Milk contains high concentrations of amyloidogenic casein proteins and is supersaturated with respect to crystalline calcium phosphates such as apatite. Nevertheless, the mammary gland normally remains unmineralized and free of amyloid.
Jared K. Raynes   +5 more
doaj   +1 more source

Structure and biological functions of milk caseins

open access: yesRussian Open Medical Journal, 2022
Caseins, which are contained in milk, play a significant role in the development of clinical symptoms of allergic reactions in adults and children. To date, the properties of caseins have been studied, their primary structure has been identified. However,
Stanislava Yu. Petrova   +4 more
doaj   +1 more source

A sedimentation test to measure heat stability of milk protein beverages

open access: yesJournal of Dairy Science
: A small-scale oil bath immersion-heating system using sealed stainless-steel process tubes was developed that has the flexibility to evaluate a wide range of holding temperatures and times. After heat treatment and rapid cooling, the liquid product was
Drew Hargrove   +2 more
doaj   +1 more source

Casein micelle structure: a concise review [PDF]

open access: yesSongklanakarin Journal of Science and Technology (SJST), 2005
Milk is a complex biological fluid with high amount of proteins, lipid and minerals. The function of milk is to supply nutrients such as essential amino acids required for the growth of the newborn. In addition, due to the importance of casein and casein
Chanokphat Phadungath
doaj  

α‐Synuclein Forms Distinct Micelle‐Like Assemblies at Low Ionic Strengths

open access: yesAdvanced Science, EarlyView.
At high ionic strength, α‐synuclein forms diverse assemblies, including oligomers, fibrils, and condensates. Here, we show that at low ionic strength, α‐synuclein adopts a distinct, low‐abundance assembly state. These assemblies maintain a constant size above a critical concentration and do not coalesce, suggesting a micelle‐like organization ...
Sophie Hertel   +10 more
wiley   +1 more source

Effect of Pre-Heating Prior to Low Temperature 0.1 µm-Microfiltration of Milk on Casein–Whey Protein Fractionation

open access: yesFoods, 2021
During skim milk microfiltration (nominal pore size of 0.1 µm) at 10 °C, the whey protein purity in the permeate is reduced by an enhanced serum casein permeation, primarily of β-casein.
Simon Schiffer   +4 more
doaj   +1 more source

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