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- W2156848968 abstract "Summary The relationship between extent of κ -casein proteolysis and aggregatability of milk casein micelles has been studied using chymosin either bound to porous glass supports or free in solution. Both enzyme preparations demonstrated that, overall, 86–90 % of the κ -casein had to be destroyed before any aggregation could occur. Based on these results, a mathematical model of chymosin action on casein is described involving (i) the attack on κ -casein by chymosin, via a Michaelis–Menten mechanism (ii) the probability that sufficient κ -casein on any micelle is destroyed to allow aggregation, and (iii) the aggregation of para-casein micelles by a von Smoluchowski mechanism." @default.
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- W2156848968 date "1979-11-01" @default.
- W2156848968 modified "2023-09-26" @default.
- W2156848968 title "Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin" @default.
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- W2156848968 doi "https://doi.org/10.1017/s0022029900020719" @default.
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