Results 161 to 170 of about 2,575 (207)
The effect of β-casein addition on properties and rennet behavior of reassembled casein micelles
Food ChemistryBovine milk contains four types of caseins with β-casein being one of the most abundant. Previous studies on cow milk have reported seemingly contradictory effects of β-casein on milk renneting behavior.
Huifang Cai +2 more
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Tailoring the structure of casein micelles through a multifactorial approach to manipulate rennet coagulation properties [PDF]
Food Hydrocolloids, 2020 International audienceThe properties of casein micelles are known to be affected by modifications to the environment, such as variations in pH or the addition of salts, yet the scientific literature typically considers the effects of one factor at a time,
Antoine Bouchoux +2 more
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Food Hydrocolloids, 2012 International audiencePulsed field gradient - nuclear magnetic resonance (PFG-NMR) was used to monitor the diffusion of caseins throughout the rennet coagulation of a highly concentrated casein suspension.
Steven Le Feunteun, François Mariette
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Effects of structural rearrangements on the rheology of rennet-induced casein particle gels
Advances in Colloid and Interface Science, 2002 During ageing of casein or skim milk gels, structural changes take place that affect gel parameters, such as pore size and storage modulus. These changes can be explained in terms of rearrangements of the gel network at various length scales.
M Mellema, P Walstra, T Van Vliet
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Kinetics of rennet casein gelation at different cooling rates
Journal of Colloid and Interface Science, 2004A mathematical model was developed to quantitatively analyze the rheological data of rennet casein gelation at different cooling rates. Kinetic parameters were estimated and correlated with the microstructure development of the protein network. The kinetic model identified structure development upon cooling to be first order, and the network forming ...
C R Daubert
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The Coagulation of Differently Sized Casein Micelles by Rennet
European Journal of Biochemistry, 1981Fractions of bovine casein micelles of different sizes were prepared by sucessive centrifugation steps, and dilute suspensions of the different fraction were reacted with rennet. The molecular weight increas with time after addition of rennet was measured by light scattering.
D G, Dalgleish +2 more
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Proteolysis of goat casein by calf rennet
International Dairy Journal, 1997Abstract The proteolytic activity of calf rennet on goat casein (CN) was studied under various conditions which affect cheesemaking and ripening processes (pH, salt, calf rennet concentration and α s 1 -CN polymorphism). Electrophoretic studies showed that goat casein was hydrolysed to give characteristic breakdown products derived from individual
A.J. Trujillo, B. Guamis, C. Carretero
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Proteolysis in rennet casein-based cheese analogues
International Dairy Journal, 2000Abstract Rennet caseins manufactured from mid- or late-lactation milk were used to prepare pilot- and commercial-scale Mozzarella-type cheese analogues. Mid-lactation rennet casein and analogues made from it contained low levels of plasmin; late-lactation rennet caseins and analogues made from them had higher levels of plasmin while pilot-scale ...
Daniel M Mulvihill, Tanoj K Singh
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The influence of temperature on the flocculation rate of renneted casein micelles
Biophysical Chemistry, 1984The flocculation rate constant of completely renneted casein micelles in milk ultrafiltrate was measured by Rayleigh light scattering between 20 and 35 degrees C. In this temperature range an apparent energy of activation of 103 kJ mol (+/-11 kJ mol : n = 50) was measured. At 15 degrees C clotting was not longer perceptible.
J, Brinkhuis, T A, Payens
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