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Functional properties of bovine milk protein isolate and associated enzymatic hydrolysates

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journal contribution
posted on 2018-03-09, 09:50 authored by Ger Ryan, Alice B. Nongonierma, Jonathan O'Regan, Richard J. Fitzgerald
The nitrogen solubility (pH 2.0–8.0), heat stability (pH 6.2–7.4) and viscosity (pH 6.2–7.4) properties of bovine milk protein isolate (MPI) and its Flavourzyme™, Neutrase™ and Protamex™ enzymatic hydrolysates were studied. Gel permeation chromatography indicated digestion of individual milk proteins in all hydrolysates. MPI had low solubility at pH 4.0–5.0; however, hydrolysis with all enzymes significantly increased solubility between pH 4.0–7.0. MPI was highly heat stable at 140 °C above pH 6.8 (>10 min). All hydrolysates coagulated within 64 s at 140 °C between pH 6.2–7.4. All hydrolysates displayed increased apparent viscosities upon exposure to simulated high temperature short time (HTST) heating and cooling conditions between pH 6.2–7.4. The results demonstrate that enzymatic hydrolysis of MPI increased protein solubility; however, the heat stability was reduced. The apparent viscosity was lower than the control at ambient temperature and increased at 90 °C

History

Publication

International Dairy Journal;81, pp. 113-121

Publisher

Elsevier

Note

peer-reviewed

Other Funding information

EI

Rights

This is the author’s version of a work that was accepted for publication in International Dairy Journal. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in International Dairy Journal, 2018, 81, pp. 113-121,

Language

English

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