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Effect of heat-induced κ-casein dissociation on acid coagulation of milk

Published online by Cambridge University Press:  22 February 2018

Daiki Oka ,
Wataru Ono ,
Shintarou Ohara ,
Tomohiro Noguchi  and
Katsumi Takano
Daiki Oka*
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Wataru Ono
Affiliation:
Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Shintarou Ohara
Affiliation:
Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Tomohiro Noguchi
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Katsumi Takano
Affiliation:
Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
*
*For correspondence; e-mail: d3oka@nodai.ac.jp
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Abstract

In this study, the relationship between the dissociation of κ-casein from casein micelles due to heat-induced denaturation and the strength of acid milk gel was investigated. The κ-casein-dissociated micelles were fractionated by gel filtration chromatography and two-dimensional polyacrylamide gel electrophoresis, and their zeta potential and surface hydrophobicity were measured. The negative charge of the κ-casein-dissociated micelles was lower than that of native micelles, and micellar surface hydrophobicity was higher. For confirmation, the isoelectric point of the casein micelles was measured. The κ-casein-dissociated micelles were found to cohere at an earlier stage of acidification than the native micelles. These results demonstrated that the heat-induced increase in the strength of acid milk gel was partly due to the decrease in micellar surface charge and partly to the increase in surface hydrophobicity caused by the dissociation of κ-casein.

Keywords

κ-caseinYogurtheat-denaturationcasein micellesnegative charge
Type
Research Article
Information
Journal of Dairy Research , Volume 85 , Issue 1 , February 2018 , pp. 104 - 109
Copyright
Copyright © Hannah Dairy Research Foundation 2018 

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References

Anema, SG 2007 Role of κ-casein in the association of denatured whey proteins with casein micelles in heated reconstituted skim milk. Journal of Agricultural and Food Chemistry 55 3635–3642 CrossRefGoogle ScholarPubMed
Anema, SG & Li, Y 2003a Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect of casein micelle size. Journal of Dairy Research 70 73–83 CrossRefGoogle ScholarPubMed
Anema, SG & Li, Y 2003b Effect of pH on the association of denatured whey proteins with casein micelles in heated reconstituted skim milk. Journal of Agricultural and Food Chemistry 51 1640–1646 CrossRefGoogle ScholarPubMed
Anema, SG & Li, Y 2015 Reassociation of dissociated caseins upon acidification of heated pH-adjusted skim milk. Food Chemistry 174 339–347 CrossRefGoogle ScholarPubMed
Aschaffeburg, R & Drewry, J 1957 Improved method for the preparation of crystalline β-Lactoglobulin and α-Lactoalbumin from cow's milk. Biochemical Journal 65 680–685 Google Scholar
Berggren, K, Chernokalskaya, E, Steinberg, TH, Kemper, C, Lopez, MF, Diwu, Z, Haugland, RP & Patton, WF 2000 Background-free, high sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex. Electrophoresis 21 2509–2521 3.0.CO;2-9>CrossRefGoogle ScholarPubMed
Bradford, MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 248–254 CrossRefGoogle ScholarPubMed
Cases, E, Vidal, V & Cuq, JL 2003 Effect of κ-casein deglycosylation on the acid coagulability of milk. Journal of Food Science 68 2406–2410 CrossRefGoogle Scholar
Cayot, P, Fairise, JF, Colas, B, Lorient, D & Brulé, G 2003 Improvement of rheological properties of firm acid gels by skim milk heating is conserved after stirring. Journal of Dairy Research 70 423–431 CrossRefGoogle ScholarPubMed
Cobos, A, Horne, DS & Muir, DD 1995 Rheological properties of acid milk gels. 1. Effect of composition, process and acidification conditions on products from recombined milks. Milchwissenschaft 50 444–447 Google Scholar
Corredig, M & Dalgleish, DG 1996 Effect of temperature and pH on the interactions of whey proteins with casein micelles in skim milk. Food Research International 29 49–55 CrossRefGoogle Scholar
Donato, L, Alexander, M & Dalgleish, DG 2007 Acid gelation in heated and unheated milk: interactions between serum protein complexes and the surfaces of casein micelles. Journal of Agricultural and Food Chemistry 55 4160–4168 CrossRefGoogle ScholarPubMed
Fairise, JF, Cayot, P & Lorient, D 1999 Characterization of the protein composition of casein micelles after heating. International Dairy Journal 9 249–254 CrossRefGoogle Scholar
Gastaldi, E, Triak, N, Guillaume, C, Gontard, N & Cuq, JL 2003 Effect of controlled κ-casein hydrolysis on rheological properties of acid milk gels. Journal of Dairy Science 86 704–711 CrossRefGoogle ScholarPubMed
Guyomarc'h, F, Law, AJ & Dalgleish, DG 2003a Formation of soluble and micelle-bound protein aggregates in heated milk. Journal of Agricultural and Food Chemistry 51 4652–4660 CrossRefGoogle ScholarPubMed
Guyomarc'h, F, Queguiner, C, Law, AJ, Horne, DS & Dalgleish, DG 2003b Role of the soluble and micelle-bound heat-induced protein aggregates on network formation in acid skim milk gels. Journal of Agricultural and Food Chemistry 51 7743–7750 CrossRefGoogle ScholarPubMed
Guyomarc'h, F, Renan, M, Chatriot, M, Gamerre, V & Famelart, MH 2007 Acid gelation properties of heated skim milk as a result of enzymatically induced changes in the micelle/serum distribution of the whey protein/κ-casein aggregates. Journal of Agricultural and Food Chemistry 55 10986–10993 CrossRefGoogle ScholarPubMed
Guyomarc'h, F, Violleau, F, Surel, O & Famelart, MH 2010 Characterization of heat-induced changes in skim milk using asymmetrical flow field-flow fractionation coupled with multiangle laser light scattering. Journal of Agricultural and Food Chemistry 58 12592–12601 CrossRefGoogle ScholarPubMed
Hayakawa, S & Nakai, S 1985 Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 50 486–491 CrossRefGoogle Scholar
Huppertz, T, Fox, PF & Kelly, AL 2004 Properties of casein micelles in high pressure-treated bovine milk. Food Chemistry 87 103–110 CrossRefGoogle Scholar
Jean, K, Renan, M, Famelart, MH & Guyomarc'h, F 2006 Structure and surface properties of the serum heat-induced protein aggregates isolated from heated skim milk. International Dairy Journal 16 303–315 CrossRefGoogle Scholar
Jovanović, S, Barać, M, Maćej, O & Djurdjević, JD 2005 Page analysis of milk proteins altered by high thermal treatment. Acta Alimentaria 34 105–112 CrossRefGoogle Scholar
Lucey, JA & Singh, H 1997 Formation and physical properties of acid skim milk gels: a review. Food Research International 30 529–542 CrossRefGoogle Scholar
Lucey, JA, Munro, PA & Singh, H 1998 Rheological properties and microstructure of acid milk gels as affected by fat content and heat treatment. Journal of Food Science 63 660–664 CrossRefGoogle Scholar
Matsuno, K & Suzuki, S 2008 Simple fluorimetric method for quantification of sialic acids in glycoproteins. Analytical biochemistry 375 53–59 CrossRefGoogle ScholarPubMed
Morand, M, Guyomarc'h, F & Famelart, MH 2011 How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk – a review. Dairy Science & Technology 91 97–126 CrossRefGoogle Scholar
Nock, CM, Ball, MS, White, IR, Skehel, JM, Bill, L & Karuso, P 2008 Mass spectrometric compatibility of Deep Purple and SYPRO Ruby total protein stains for high-throughput proteomics using large-format two-dimensional gel electrophoresis. Rapid Communications in Mass Spectrometry 22 881–886 CrossRefGoogle ScholarPubMed
Oldfield, DJ, Singh, H & Taylor, MW 1998 Association of β-lactoglobulin and α-lactalbumin with the casein micelles in skim milk heated in an ultra-high temperature plant. International Dairy Journal 8 765–770 CrossRefGoogle Scholar
Ono, T, Yoshida, M, Tanaami, H & Ohkosi, H 1999 Changes in casein micelle size induced by heating. International Dairy Journal 9 405–406 CrossRefGoogle Scholar
Rao, PS, Sharama, R & Rajput, YS 2012 Direct estimation of sialic acid in milk and milk products by fluorometry and its application in detection of sweet whey adulteration in milk. Journal of Dairy Research 79 495–501 Google Scholar
Schagger, H & Von Jagow, G 1991 Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Analytical biochemistry 199 223–231 CrossRefGoogle ScholarPubMed
Schagger, H, Cramer, WA & Vonjagow, G 1994 Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Analytical Biochemistry 217 220–230 CrossRefGoogle ScholarPubMed
Singh, H & Creamer, LK 1991 Aggregation and dissociation of milk protein complexes in heated reconstituted concentrated skim milks. Journal of Food Science 56 238–246 CrossRefGoogle Scholar
Tuinier, R & De Kruif, CG 2002 Stability of casein micelles in milk. Journal of Chemical Physics 117 1290–1295 CrossRefGoogle Scholar
Vasbinder, AJ, Alting, AC & de Kruif, KG 2003 Quantification of heat-induced casein-whey protein interactions in milk and its relation to gelation kinetics. Colloids and surfaces B: Biointerfaces 31 115–123 CrossRefGoogle Scholar