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Hydrophobic surface areas and net charges of αs1-, κ-casein and αs1-casein: κ-casein complex

Published online by Cambridge University Press:  01 June 2009

Shun'ichi Dosako
Affiliation:
Technical Research Institute, Snow Brand Milk Products Co., Ltd, 1–2 Minamidai 1-chome, Kawagoe, 350, Japan
Shuichi Kaminogawa
Affiliation:
Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, Japan
Shin'ichi Taneya
Affiliation:
Technical Research Institute, Snow Brand Milk Products Co., Ltd, 1–2 Minamidai 1-chome, Kawagoe, 350, Japan
Kunio Yamauchi
Affiliation:
Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, Japan

Summary

Hydrophobic surface areas of αs1- and κ-casein polymers and αs1-casein: κ-casein complex were estimated by the salting-out technique using various salts according to the theory of Melander & Horvath (1977). Calculated hydrophobic surface areas of αs1, κ-casein polymers and αs1-casein: κ-casein complex were 1976, 3571 and 2989 Å2 respectively. Assuming that κ-casein polymer dissociated into 4 particles in complex formation and that 1 mole of αs1-casein: κ-casein complex was produced from 2 mole of αs1-casein polymer and one of these dissociated κ-casein particles, the hydrophobic surface area of αs1-casein: κ-casein complex was less than those of 2 mole of αs1-casein polymer plus a quarter κ-casein polymer. On the other hand, the net charge of αs1-casein: κ-casein complex was nearly equal to that of 2 mole of αs1-casein polymer plus a quarter of κ-casein polymer. From these results, it was concluded that the complex formation of αs1- and κ-casein polymers was hydrophobic and that electrostatic interaction did not participate in complex formation.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1980

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References

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