1985
DOI: 10.1017/s0022029900023980
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Effect of heat induced interaction between β-lactoglobulin and κ-casein on syneresis

Abstract: The effect of preheating skim milk and artificial micelle milk on curd syneresis was studied. The inhibition of syneresis caused by heat was dependent on the presence of /?-lactoglobulin (/?-lg) and to a lesser extent a-lactalbumin. The degree of inhibition increased with increasing amounts of added /?-lg and preheating temperature. This agrees with the hypothesis that the detrimental effect of preheating on syneresis is due to complex formation between /?-lg and /c-casein. This complex appeared to be mediated… Show more

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Cited by 43 publications
(26 citation statements)
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References 17 publications
(16 reference statements)
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“…These proteins that are complexed with the casein micelles during heating reduce the degree of casein aggregation during subsequent rennet coagulation and curd formation and lead to a finer gel matrix structure [29][30][31].…”
Section: Rheological Measurementmentioning
confidence: 99%
“…These proteins that are complexed with the casein micelles during heating reduce the degree of casein aggregation during subsequent rennet coagulation and curd formation and lead to a finer gel matrix structure [29][30][31].…”
Section: Rheological Measurementmentioning
confidence: 99%
“…In the cheese vat, high heat treatment of milk prolongs rennet coagulation times and reduces the strength of rennet gels [5,26], leading to impaired syneresis [10,92,115]. The adverse effects on coagulation are attributed to the inhibition of hydrolysis of κ-casein by chymosin due to the β-lactoglobulin/κ-casein complex at the micelle surface impairing the accessibility of κ-casein to the coagulant [55,59,139], to reduced reactivity of renneted micelles with attached denatured whey proteins to aggregation, or to a reduction in the concentration of micellar calcium [139,142].…”
Section: Heat Treatments Other Than Pasteurisationmentioning
confidence: 99%
“…These aggregates essentially contain whey proteins and κ-casein; micelle-bound aggregates may also contain traces of α s2 -casein [26,62,121,139,144]. They can reach a diameter of 30 to 100 nm [76,157].…”
Section: Thermal Coprecipitation Of the Whey Proteins And Caseinmentioning
confidence: 99%