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Enzymic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula

Published online by Cambridge University Press:  01 June 2009

Eunice Li-Chan  and
Shuryo Nakai
Eunice Li-Chan
Affiliation:
Department of Food Science, University of British Columbia, Vancouver, B.C., Canada, V6T 1W5
Shuryo Nakai
Affiliation:
Department of Food Science, University of British Columbia, Vancouver, B.C., Canada, V6T 1W5
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Summary

To improve acid clotting properties, enzymic dephosphorylation of caseins with calf intestinal alkaline phosphatase (CAP) or potato acid phosphatase (PAP) was investigated. Greater dephosphorylation was achieved using αs1- or β-casein as substrates, compared to whole casein or skim milk. Electrophoresis of PAP-modified caseins revealed bands with lower mobility and a multibanded pattern in the β-casein region which was similar to that of human β-casein. On the other hand, CAP modification produced electrophoretic bands having lower mobility of the β-casein component, but with higher mobility in the αs1-casein component as well as increased net negative charge in the CAP-casein. PAP-casein formed a fine dispersion upon acidification to pH 4. with a microstructure similar to that of acidified human casein. Greater initial rates of hydrolysis by pepsin at pH 4 were observed for both CAP- and PAP-modified caseins, compared to bovine and human caseins. The rate and extent of hydrolysis remained high for CAP-casein but tended to level off with PAP-casein during sequential digestion with pepsin and pancreatin. There may be advantages in the use of partial dephosphorylation to improve acid clotting and digestibility properties of bovine casein for infant feeding.

Type
Original Articles
Information
Journal of Dairy Research , Volume 56 , Issue 3: Special Issue: Proceedings of the Hannah Research Institute Casein Conference , May 1989 , pp. 381 - 390
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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