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Journal of Dairy Science Vol. 78 No. 12 2653-2659
© 1995 by American Dairy Science Association ®
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Characterization of Multiply Phosphorylated Peptides Selectively Precipitated from a Pancreatic Casein Digest

N. J. Adamson 1 and E. C. Reynolds 1

1 Biochemistry and Molecular Biology Unit, School of Dental Science, University of Melbourne, Melbourne 3OO0, Australia

Anticariogenic phosphopeptides, released during the hydrolysis of casein with trypsin, contain the cluster sequence Ser(P)-Ser(P)Ser(P)-Glu-Glu and have commercial potential as toothpaste, mouthwash, and food additives for the prevention of dental caries. To develop a commercial-scale process for the production of these peptides, we have comprehensively characterized casein phosphopeptides that were selectively precipitated using Ca2+ and ethanol from an acid-clarified pH 4.6) pancreatic casein hydrolysate. Casein was hydrolyzed using pancreatin at 50°C for 2 h. The precipitate contained a series of casein phosphopeptides that were slightly truncated relative to tryptic casein phosphopeptides. The major casein phosphopeptides released by pancreatin were ß-CN-4P(f7-24), as1-CN-5P(f61-78), and aS1-CN-5P(f59-78), all containing the cluster sequence. The truncation of the tryptic peptides ß-CN-4P(f1-25) and aS1-CN-5P(f59-79) resulted from the chymotryptic and carboxypeptidase activities of the pancreatin. The peptides containing the cluster sequence constituted 77.8 ± 6.7 mol/1OO mol of the total peptides that were selectively precipitated. This composition was not significantly different from that of casein phosphopeptides produced under identical conditions using trypsin. In conclusion, pancreatin should be a suitable enzyme preparation for the production of anticariogenic casein phosphopeptides on a commercial scale.

Key Words: casein phosphopeptides • pancreatin • high performance liquid chromatography • sequence analysis

Submitted on December 5, 1994
Accepted on July 11, 1995




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