Rennet-induced coagulation properties of yak casein micelles: A comparison with cow casein micelles
Food Research International, 2017It is essential for yak cheese processing to understand the rennet-induced coagulation properties of gel formation from casein micelles. We have previously discovered that yak milk requires a longer incubation time but forms stronger gels compared with cow milk. In this study, we are aiming to understand the rennet-induced coagulation properties of yak
Yan, Zhang +5 more
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A kinetic model of the clotting of casein by rennet
Journal of Dairy Research, 1971SummaryA kinetic model of casein clotting caused in milk by rennet was defined by measuring changes in viscosity and in the complex modulus of rigidity. Three separate stages of the process were distinguished: the enzymic, the flocculation and the gelification. The kinetic equations and the main activation parameters were defined for each stage.
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Note on the action of vegetable rennets on sodium caseinate
Journal of Dairy Research, 1963In an earlier paper, one of us (Oosthuizen, 1962) showed that vegetable rennets produce a fall in the viscosity of sodium caseinate solutions which follows the equation of first-order chemical kinetics; but that the proteolysis involved is stronger than that of calf's rennet since the vegetable rennets attack a greater proportion of the casein ensemble.
J. C. Oosthuizen, G. W. Scott Blair
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Physicochemical Variables Affecting the Rheology and Microstructure of Rennet Casein Gels
Journal of Agricultural and Food Chemistry, 2007The rheology and microstructure of a rennet casein system were studied in the pH range from 5.8 to 12.0 during cooling from 80 to 5 degrees C at four cooling rates: 0.5, 0.1, 0.05, and 0.025 degrees C/min. A dramatic increase in storage modulus with pH was observed during cooling at a fixed cooling rate. Continuous networks were formed for gels at pH 7.
Qixin, Zhong +2 more
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Casein micelles: diffusivity as a function of renneting time
Langmuir, 1992The diffueivity of K-casein micelles in renneted skim milk was measured by dynamic light scattering. By use of the Stokes-Einstein relation, the apparent particle radius was calculated. Aa a result of the enzymatic proteolysis of the K-casein peptides that provide the steric stabilization of the casein micelles, the hydrodynamic radius diminishes ...
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Rennet coagulation of casein micelles and heated casein micelles in presence of sucrose or lactose
Food Research International, 2004Abstract The effects of sucrose and lactose on the kinetics of the aggregation step of milk enzymic coagulation were studied by turbidimetric measurements for casein micelles previously heated (HCM) or not heated (CM). The initial aggregation rate showed an initial destabilizing effect by addition of polysaccharides, which could be attributed to ...
Miryam Pires +3 more
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The action of rennets on the caseins: I. Rennin action on β-casein-B in solution
Journal of Dairy Research, 1971SummaryA study of the hydrolysis of β-casein-B by crystalline rennin or rennet extract at pH 6·5, using a disk electrophoresis technique, showed that 3 bonds in β-casein are appreciably more sensitive than the others to rennin proteolysis, and that these bonds are probably located near the C-terminus of the protein.
L. K. Creamer +2 more
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718. Renneting and the caseinate particle: a viscometric study
Journal of Dairy Research, 1958A viscometric study of solutions of alkaline (sodium and potassium) caseinate was made to determine the effects of renneting with and without the addition of calcium ions. There was no real viscometric effect of these treatments at high dilutions. At a higher temperature, the viscosity increment of the solutions decreased.
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Rennet coagulation of casein micelles and heated casein micelles: action of Ca2+ and pH
Food Hydrocolloids, 1999Abstract The effect of Ca2+ and pH on the aggregation kinetics of heated para casein micelles (pHCM) was studied and compared with those of nonheated para casein micelles (pCM), using turbidimetry. Although it is known that pHCM have a higher stability than pCM, possibly because of steric stability, the increase of Ca2+ concentration and ...
M.S. Pires, G.A. Orellana, C.A. Gatti
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Action of rennet and other proteolytic enzymes on casein in casein-agar gels
Journal of Dairy Research, 1963SummaryA series of precipitation zones appears when proteolytic enzymes diffuse through an agar gel containing 1% whole casein and 10–20 mM-calcium chloride. As the enzyme diffuses through the gel the casein stability changes giving first a precipitate which subsequently redissolves followed by a second precipitate which also redissolves.
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