Hostname: page-component-78c5997874-fbnjt Total loading time: 0 Render date: 2024-11-04T19:51:12.825Z Has data issue: false hasContentIssue false
  • English
  • Français

Enzymic modification of αs1-casein with peptidylarginine deiminase: preparation of less acid-coagulable and less calcium-sensitive casein

Published online by Cambridge University Press:  01 June 2009

Norihiro Azuma ,
Kazutoshi Nara  and
Choemon Kanno
Norihiro Azuma
Affiliation:
Department of Animal Science, Faculty of Agriculture, Utsunomiya University, Utsunomiya 321, Japan
Kazutoshi Nara
Affiliation:
Department of Animal Science, Faculty of Agriculture, Utsunomiya University, Utsunomiya 321, Japan
Choemon Kanno
Affiliation:
Department of Animal Science, Faculty of Agriculture, Utsunomiya University, Utsunomiya 321, Japan
Get access Rights & Permissions [Opens in a new window]

Summary

Enzymic modification with peptidylarginine deiminase (EC 3.5.3.15) enabled five out of six arginyl residues in αs1-casein to be convcrted to citrullyl residues, only the N-terminal arginyl residue remaining unaffected. An increase in the net negative charge was confirmed by PAGE. The isoelectric point was decreased from 4·46 for the intact αsl-casein to 4·30 for the deiminated type, while simultaneously lowering the acid-precipitation starting point from pH 5·17 to pH 4·62. The deiminated αs1-casein self-associated less in the absence of Ca and was less Ca-sensitive than the native type, although its Ca-binding ability was slightly enhanced. In the presence of 25 mM-CaC12 and K-casein, Ca-induced precipitation of αs1-casein did not occur, the solution of the mixture remaining transparent. Deimination of αs1-casein resulted in altering its characteristics, possibly by interfering with interactions through hydrophobicity and/or hydrogen bonding. The positive charge of the arginyl residues might play an important role in casein micelle formation.

Type
Original Articles
Information
Journal of Dairy Research , Volume 58 , Issue 4 , November 1991 , pp. 421 - 429
Copyright
Copyright © Proprietors of Journal of Dairy Research 1991

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Azuma, N., Aizawa, M. & Yamauchi, K. 1989 Effect of bound phosphate on the calcium-binding ability and calcium-dependent precipitability of human β-casein. Agricultural and Biological Chemistry 53 1037–1041Google Scholar
Azuma, N., Kaminogawa, S. & Yamauchi, K. 1985 Reconstitution of human casein micelle and its properties. Agricultural and Biological Chemistry 49 2655–2660Google Scholar
Bingham, E. W., Farrell, H. M. & Carroll, R. J. 1972 Properties of dephosphorylated αs1-casein. Precipitation by calcium ions and micelle formation. Biochemistry 11 2450–2454CrossRefGoogle Scholar
Creamer, L. K., Roeper, J. & Lohrey, E. H. 1971 Preparation and evaluation of some acid soluble casein derivatives. New Zealand Journal of Dairy Science and Technology 6 107–111Google Scholar
Evans, M. T. A., Irons, L. & Petty, J. H. P. 1971 Physicochemical properties of some acyl derivatives of β-casein. Biochimica et Biophysica Acta 243 259–272CrossRefGoogle Scholar
Fujisaki, M. & Sugawara, K. 1981 Properties of peptidylarginine deiminase from the epidermis of newborn rats. Journal of Biochemistry 89 257–263CrossRefGoogle ScholarPubMed
Hoagland, P. D. 1966 Acylated β-caseins: electrostatic interactions and aggregation. Journal of Dairy Science 49 783–787CrossRefGoogle ScholarPubMed
Horne, D. S. 1983 Calcium-induced precipitation of αs1-casein: effect of modification of lysine residues. International Journal of Biological Macromolecules 5 296–300CrossRefGoogle Scholar
Horne, D. S. & Dalgleish, D. G. 1980 Electrostatic interaction and the kinetics of protein aggregation: αs1-casein. International Journal of Biological Macromolecules 2 154–160CrossRefGoogle Scholar
Horne, D. S. & Moir, P. D. 1984 Iodination of αs1-casein and its effect on the calcium-induced aggregation reaction of the modified protein. International Journal of Biological Macromolecules 6 316–320CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. 1951 Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193 265–275CrossRefGoogle ScholarPubMed
Markwell, M. A. K., Haas, S. M., Bieber, L. L. & Tolbert, N. E. 1978 A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Analytical Biochemistry 87 206–210CrossRefGoogle ScholarPubMed
Mercier, J.-C., Grosclaude, F. & Ribadeau-Dumas, B. 1971 [Primary structure of bovine αs1-casein. Complete sequence.] European Journal of Biochemistry 23 41–51CrossRefGoogle Scholar
Panyim, S. & Chalkley, R. 1969 High resolution acrylamide gel electrophoresis of histones. Archives of Biochemistry and Biophysics 130 337–346CrossRefGoogle ScholarPubMed
Sugawara, K., Oikawa, Y. & Ouchi, T. 1982 Identification and properties of peptidylarginine deiminase from rabbit skeletal muscle. Journal of Biochemistry 91 1065–1071CrossRefGoogle ScholarPubMed
Takahara, H., Okamoto, H. & Sugawara, K. 1985 Specific modification of the functional arginine residue in soybean trypsin inhibitor (Kunitz) by peptidylarginine deiminase. Journal of Biological Chemistry 260 8378–8383CrossRefGoogle ScholarPubMed
Thompson, M. P. 1966 DEAE-cellulose-urea chromatography of casein in the presence of 2-mercaptoethanol. Journal of Dairy Science 49 792–795CrossRefGoogle ScholarPubMed
Waugh, D. F. & Von Hippel, P. H. 1956 κ-Casein and the stabilization of casein micelles. Journal of the American Chemical Society 78 4576–4582CrossRefGoogle Scholar
Yamauchi, K., Takemoto, S. & Tsugo, T. 1967 Calcium-binding property of dephosphorylated caseins. Agricultural and Biological Chemistry 31 54–63CrossRefGoogle Scholar
Yoshikawa, M., Sasaki, R. & Chiba, H. 1981 Effects of chemical phosphorylation of bovine casein components on the properties related to casein micelle formation. Agricultural and Biological Chemistry 45 909–914Google Scholar
Yoshikawa, M., Tamaki, M., Sugimoto, E. & Chiba, H. 1974 Effect of dephosphorylation on the self-association and the precipitation of β-casein. Agricultural and Biological Chemistry 38 2051–52Google Scholar
Zittle, C. A. & Custer, J. H. 1963 Purification and some of the properties of αs-casein and κ-casein. Journal of Dairy Science 46 1183–1188CrossRefGoogle Scholar