Results 11 to 20 of about 2,242 (180)

Milk-Clotting Protease From <i>Bacillus stercoris</i>NCCP-3139: A Potential Microbial Rennet for Cheese Production. [PDF]

Food Sci Nutr
A milk‐clotting protease from Bacillus stercoris NCCP‐3139 was isolated from soil and purified via ammonium sulfate precipitation and sequential chromatographic techniques, yielding a homogeneous enzyme confirmed by SDS–PAGE. The protease exhibited high catalytic selectivity, with a marked increase in milk‐clotting‐to‐proteolytic activity ratio (50–550)
Sibtain M, Qurtam AA, Javaria S, Murtaza G, Al-Zharani M, Ain NU, Chaman S, Nasr FA, Zaman A.   +8 more
europepmc   +2 more sources

Innovative Processing Technologies for Clean-Label Liquid Foods With High Protein Content: Advances in Process Development and Quality Evaluation. [PDF]

Compr Rev Food Sci Food Saf
ABSTRACT The demand for protein‐based liquid foods is increasing due to growing awareness of the impact of diet on human health. This trend has prompted the food industry to explore minimal processing technologies that ensure both safety and clean‐label appeal.
Janahar JJ, Seth D, Balasubramaniam VM.
europepmc   +2 more sources

Formation of artificial casein micelles. [PDF]

Agricultural and Biological Chemistry, 1983
The reformation of casein micelles was investigated by dialysis of simulated milk ultrafiltrate or skimmilk at a fixed temperature or by increasing the temperature from 5°c to 3°C. When submicelles were dialyzed at a fixed temperature the micelles were not reformed, but were when the submicelles were dialyzed as the temperature was increased from 5°c ...
ONO, Tomotada, FURUYAMA, Tomomi, ODAGIRI, Satoshi   +2 more
openaire   +2 more sources

Association of casein micelle size and enzymatic curd strength and dry matter curd yield

Ciência Rural, 2019
: The aim of the present study was to explore the association between milk protein content and casein micelle size and to examine the effects of casein micelle size on enzymatic curd strength and dry matter curd yield using reduced laboratory-scale ...
Denise Ribeiro de Freitas, Fernando Nogueira de Souza, Jamil Silvano de Oliveira, Diêgo dos Santos Ferreira, Cristiane Viana Guimarães Ladeira, Mônica Maria Oliveira Pinho Cerqueira   +5 more
doaj   +1 more source

The membrane-associated form of α(s1)-casein interacts with cholesterol-rich detergent-resistant microdomains. [PDF]

PLoS ONE, 2014
Caseins, the main milk proteins, interact with colloidal calcium phosphate to form the casein micelle. The mesostructure of this supramolecular assembly markedly influences its nutritional and technological functionalities.
Annabelle Le Parc, Edith Honvo Houéto, Natascha Pigat, Sophie Chat, Joëlle Leonil, Eric Chanat   +5 more
doaj   +1 more source

Effect of Temperature, Added Calcium and pH on the Equilibrium of Caseins between Micellar State and Milk Serum

Foods, 2021
Micellar casein and casein monomers in milk serum are in a dynamic equilibrium. At temperature below 15–20 °C a considerable amount of casein monomers, β-casein in particular, is released from the casein micelle into the aqueous serum phase.
Simon Schiffer, Eva Scheidler, Tim Kiefer, Ulrich Kulozik   +3 more
doaj   +1 more source

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

Shipin 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

α_S1-casein, which is essential for efficient ER-to-Golgi casein transport, is also present in a tightly membrane-associated form

BMC Cell Biology, 2010
Background Caseins, the main milk proteins, aggregate in the secretory pathway of mammary epithelial cells into large supramolecular structures, casein micelles.
Le Parc Annabelle, Leonil Joëlle, Chanat Eric   +2 more
doaj   +1 more source

Effect of temperature and protein concentration on the protein types within the ultracentrifugation supernatant of liquid micellar casein concentrate

Journal of Dairy Science, 2023
: Liquid micellar casein concentrate (MCC) is an ideal milk-based protein ingredient for neutral-pH ready-to-drink beverages. The texture and mouthfeel of liquid MCC-based beverages depend on the beverage protein content, as well as the composition of ...
Joice Pranata, Marshall Dunn, MaryAnne Drake, David M. Barbano   +3 more
doaj   +1 more source

Implications of kappa-casein evolutionary diversity for the self-assembly and aggregation of casein micelles [PDF]

Royal Society Open Science, 2019
Milk alpha-, beta- and kappa-casein proteins assemble into casein micelles in breast epithelial cells. The glycomacropeptide (GMP) tails of kappa-casein that extend from the surface of the micelle are key to assembly and aggregation.
Jean Manguy, Denis C. Shields
doaj   +1 more source