摘要 : Isolated beta-casein was hydrolysed using chymosin to form numerous peptides in a 1% buffered aqueous solution at pH 5.5 and 15deg C. The hydrolysis was not limited to 15 weeks and was described by a non-linear equation with a fra... 展开 Isolated beta-casein was hydrolysed using chymosin to form numerous peptides in a 1% buffered aqueous solution at pH 5.5 and 15deg C. The hydrolysis was not limited to 15 weeks and was described by a non-linear equation with a fractional exponent a<1.Comparatively low amounts of high molecular weight products of hydrolysis, beta-casein I, II, IIIa and IIIb were formed. Low molecular weight peptides were produced with different hydrophobicities and chain lengths. Hydrolysis was accelerated in 0.5-4.0%sodium chloride; simultaneously the specificity of chymosin was altered. At the same coagulation activity of chymosin as in the batches containing 1% of the protein, no significant hydrolysis was detected in the protein containing 50% DM. The electrophoretic characterization of the peptide pattern of a 15-week ripened Gouda cheese confirmed the results obtained from the model experiments. It is concluded that the hydration of proteins has priority over the use of water for the hydrolysis of beta-caseinby chymosin. Hydrolysis is retarded when water is limited. 收起