Results 31 to 40 of about 88,994 (216)

Research Progress on Structural Properties of Casein Micelles and Their Application in Delivery Systems [PDF]

open access: yesShipin Kexue
Milk is considered an important source of protein in human diets. As the major protein component in milk, casein has attracted extensive attention from scholars due to its biparental structure and self-assembly properties. However, the poor pH, Ca2+, and
YE Jingying, WU Fan, ZHANG Zhaoyue, WEN Xin, NI Yuanying, LI Mo
doaj   +1 more source

Lactoferrin binding to transglutaminase cross-linked casein micelles [PDF]

open access: yes, 2012
Casein micelles in skim milk were either untreated (untreated milk) or were cross-linked using transglutaminase (TGA-milk). Added lactoferrin (LF) bound to the casein micelles and followed Langmuir adsorption isotherms.
de Kruif, C.G.   +3 more
core   +1 more source

Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions

open access: yesJDS Communications, 2022
In the midst of rising consumer health and environmental concerns, pea protein has increased in popularity as an alternative to animal-origin proteins.
Abigail Krentz   +2 more
doaj   +1 more source

Structure and Stability of Casein Micelles

open access: yesJournal of Dairy Science, 1975
The structure and stability of casein micelles are determined in large measure by the amino acid sequences of the constituent alphas1-, beta-, and kappa- caseins. In this paper we review, and attempt to connect with sequence data where possible: (1) molecular weight, structure, and dissociation of casein micelles; (2) physical characteristics of ...
V A, Bloomfield, R J, Mead
openaire   +2 more sources

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

Pressure-induced dissociation of casein micelles: size distribution and effect of temperature

open access: yesBrazilian Journal of Medical and Biological Research, 2005
Pressure-induced dissociation of a turbid solution of casein micelles was studied in situ in static and dynamic light scattering experiments. We show that at high pressure casein micelles decompose into small fragments comparable in size to casein ...
R. Gebhardt, W. Doster, U. Kulozik
doaj   +1 more source

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

open access: yesFoods, 2023
Membrane filtration, especially in combination with diafiltration, can affect the colloidal structure of casein micelles in milk and concentrated milks.
Norbert Raak   +2 more
doaj   +1 more source

Incorporation of Individual Casein Constituents into Micelles in Artificial Casein Micelles

open access: yesNihon Chikusan Gakkaiho, 1989
カゼイン濃度が2.5%の人工カゼインミセルを調製し,ミセル形成とコロイド状リン酸カルシウム(CCP)による架橋形成を調べた.なお,すべての試料においてクエン酸は10mMとし,カルシウムとリン酸は10mMカルシウムと12mMリン酸に2:1の割合で加えた.10mMカルシウム-12mMリン酸では,ミセルもCCP架橋も形成されなかった.ミセルカゼイン含量は20mMカルシウム-17mMリン酸で全カゼインの85%,30mMカルシウム-27mMリン酸では全カゼインの95%であった。CCP架橋形成とミセル形成とは必ずしも対応していなかった.低いカルシウムとリン酸濃度で形成されたミセルでは全カゼインに比べてαs1-およびαs2-カゼイン含量が高く,β-およびκ-カゼイン含量が低かった ...
AOKI, Takayoshi   +2 more
openaire   +2 more sources

Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization

open access: yesJournal of Dairy Science, 2022
: The dairy industry struggles to maintain consumer attention in the midst of declining fluid milk sales. Current trends create an opportunity to incorporate plant-based proteins with milk to produce a high-protein, multisourced, functional food product.
Abigail Krentz   +3 more
doaj   +1 more source

On the Stability of Casein Micelles

open access: yesJournal of Dairy Science, 1990
Abstract A view of the structure of the casein micelle is given. It is built of submicelles, roughly spherical aggregates of several casein molecules held together by hydrophobic bonds and salt bridges. Regions of amorphous calcium phosphate link the submicelles to each other, the ester phosphate groups form part of this colloidal phosphate.
openaire   +1 more source

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