Linked Life Data

8675752

Source:http://linkedlifedata.com/resource/pubmed/id/8675752

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1996-8-12
pubmed:abstractText
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 degrees 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 beta-CN-4P(f7-24), alpha s1-CN-5P(f61-78), and alpha s1-CN-5P(f59-78), all containing the cluster sequence. The truncation of the tryptic peptides beta-CN-4P(1-25) and alpha s1-CN-5P(f59-79) resulted from the chy-motryptic and carboxypeptidase activities of the pancreatin. The peptides containing the cluster sequence constituted 77.8 +/- 6.7 mol/100 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-0302
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2653-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Characterization of multiply phosphorylated peptides selectively precipitated from a pancreatic casein digest.
pubmed:affiliation
Biochemistry and Molecular Biology Unit, School of Dental Science, University of Melbourne, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't