T. Ono et al., CASEIN PHOSPHOPEPTIDES FROM CASEIN MICELLES BY SUCCESSIVE DIGESTION WITH PEPSIN AND TRYPSIN, Bioscience, biotechnology, and biochemistry, 62(1), 1998, pp. 16-21
When milk is ingested, casein micelles will be successively digested b
y pepsin in the stomach and trypsin in the intestine. Therefore, we di
gested casein micelles successively with pepsin at pH 4.0 and trypsin
at pH 7.0, and recovered casein phosphopeptides (CPP) as CPP-calcium p
hosphate (CP) complexes. The CPP-CP complexes contained 248 mg of calc
ium/g peptides and 175 mg of inorganic phosphorus/g peptides, which we
re higher than those of CPP-CP complexes driven from acid-precipitated
casein and casein micelles by tryptic digestion only. It contained mo
re (alpha(S1)-CN-5P(f59-79) than the other CPP preparations did.