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Dissociation and reassociation of enzyme-treated caseins under high pressure

Published online by Cambridge University Press:  01 June 2009

Kunio Ohmiya ,
Tsutomu Kajino ,
Shoichi Shimizu  and
Kunihiko Gekko
Kunio Ohmiya
Affiliation:
Department of Food Science and Technology, School of Agriculture, Nagoya University, Chikusa, Nagoya 464–01, Japan
Tsutomu Kajino
Affiliation:
Department of Food Science and Technology, School of Agriculture, Nagoya University, Chikusa, Nagoya 464–01, Japan
Shoichi Shimizu
Affiliation:
Department of Food Science and Technology, School of Agriculture, Nagoya University, Chikusa, Nagoya 464–01, Japan
Kunihiko Gekko
Affiliation:
Department of Food Science and Technology, School of Agriculture, Nagoya University, Chikusa, Nagoya 464–01, Japan
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Summary

The effects of pressure on the association states of enzyme-treated casein molecules were studied by monitoring the turbidity of the solutions under pressures up to 3000 kg/cm2. β-Casein polymers, partly degraded with immobilized trypsin, dissociated with increasing pressure up to a critical pressure (e.g. 1200 kg/cm2) and then reassociated under the higher pressure up to 3000 kg/cm2, following a parabolic turbidity-pressure curve. In the case of chymosin-treated κ-casein, a similar pressure dependence of turbidity was found under the same pressure conditions. Based on these results, the pressure effects on dissociation and reassociation of casein molecules were discussed in terms of the volume change of water around their hydrophobic moieties.

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. 435 - 442
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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References

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