Hostname: page-component-cd9895bd7-hc48f Total loading time: 0 Render date: 2024-12-28T17:30:39.042Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of the thermal denaturation degree of a whey protein isolate on the strength of acid milk gels and the dissociation of κ-casein

Published online by Cambridge University Press:  03 March 2022

Daiki Oka ,
Wataru Ono ,
Shojiro Tamaki ,
Tomohiro Noguchi  and
Katsumi Takano
Daiki Oka*
Affiliation:
Department of Agricultural Chemistry, Tokyo University of Agriculture, Tokyo 156-8502, Japan
Wataru Ono
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan
Shojiro Tamaki
Affiliation:
Milk Science Research Institute, Megmilk Snow Brand Co., Ltd., Saitama 350-1165, Japan
Tomohiro Noguchi
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan
Katsumi Takano
Affiliation:
Department of Agricultural Chemistry, Tokyo University of Agriculture, Tokyo 156-8502, Japan
*
Author for correspondence: Daiki Oka, Email: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

In this study, the effects of the degree of thermal denaturation of whey protein (WP) added to milk on the dissociation of κ-casein from casein micelles were investigated, since they are related to the strength of acid milk gel and its factors. Acid milk gels were prepared by heating thermally denatured WP isolate (WPI) and undenatured milk mixtures and treating them with glucono-δ-lactone as a coagulant. The strength of these gels was negatively correlated with the WPI denaturation degree and strongly positively correlated with the extent of κ-casein dissociation from casein micelles. This behavior was ascribed to the fact that α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) contained in WPI denatured after heating and engaged in disulfide bond formation with each other. With an increase in the degree of denaturation and disulfide bond formation, the bonding between β-lactoglobulin and κ-casein was suppressed to decrease the amount of κ-casein–WPI complexes. When β-Lg forms SS bonds with α-La, the number of highly reactive, free SH groups decreases, which complicates the formation of SS bridges between β-Lg and κ-casein. Thus, the denaturation degree of WPI largely determined the degree of κ-casein dissociation from casein micelles and, consequently, the strength of acid milk gels. Adding WP to milk increases the strength of acid milk gel, and it can be controlled by changing the degree of thermal denaturation of the WP. Furthermore, it was clarified for the first time that the dissociation of κ-casein from casein micelles influences this effect. Further studies are needed to elucidate the structural features of κ-casein-dissociated micelles.

Keywords

Casein micellewhey protein isolateβ-lactoglobulinκ-casein
Type
Research Article
Information
Journal of Dairy Research , Volume 89 , Issue 1 , February 2022 , pp. 104 - 108
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press on behalf of Hannah Dairy Research Foundation

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

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
Bobe, G, Beitz, DG, Freeman, AE and Lindberg, GL (1998) Separation and quantification of bovine milk proteins by reversed-phase high-performance liquid chromatography. Journal of Agricultural and Food Chemistry 46, 458–463.CrossRefGoogle ScholarPubMed
Bonfatti, V, Grigoletto, L, Cecchinato, A, Gallo, L and Carnier, P (2008) Validation of a new reversed-phase high-performance liquid chromatography method for separation and quantification of bovine milk protein genetic variants. Journal Chromatography A 1195, 101–106.CrossRefGoogle ScholarPubMed
Cheng, LJ, Augustin, MA and Clarke, PT (2000) Yogurts from skim milk – whey protein concentrate blends. Australian Journal of Dairy Technology 55, 110.Google Scholar
Considine, T, Patel, HA, Singh, H and Creamer, LK (2005) Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B. Journal of Agricultural and Food Chemistry 53, 3197–3205.CrossRefGoogle ScholarPubMed
Delikanli, B and Ozcan, T (2014) Effects of various whey proteins on the physicochemical and textural properties of set type nonfat yoghurt. International Journal of Dairy Technology 67, 495–503.CrossRefGoogle Scholar
Donato, L, Alexander, M and 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
Elfagm, AA and Wheelock, JV (1978) Heat interaction between a-lactalbumin, β-lactoglobulin and casein in bovine milk. Journal of Dairy Science 61, 159–163.CrossRefGoogle Scholar
Guyomarc'h, F, Dalgleish, DG and Law, AJR (2003) 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, Renan, M, Chatriot, M, Gamerre, V and 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 and Famelart, NH (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
Hiller, RM and Cheeseman, GC (1979) Thermal denaturation of α-lactalbumin and β-lactoglobulin in cheese whey: effect of total solids concentration and pH. Journal of Dairy Research 46, 103–111.CrossRefGoogle Scholar
Hollar, CM, Parris, AH and Cockley, KD (1995) Factors affecting the denaturation and aggregation of whey proteins in heated whey protein concentrate mixtures. Journal of Dairy Science 78, 260–267.CrossRefGoogle Scholar
Huffman, LM (1996) Processing of whey protein for use as a food ingredient. Food Technology 50, 49–52.Google Scholar
Ikeuchi, M, Kato, M, Sugai, S, Fujino, M and Kuwajima, K (1998) Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond. Protein Science 7, 1564–1574.CrossRefGoogle Scholar
Karam, MC, Hosri, C, Hussain, R, Barbar, R, Gaian, C and Scher, J (2017) Effect of whey powder rehydration and dry-denaturation state on acid milk gels characteristics. Journal of Food Processing Preservation 41, e13200.CrossRefGoogle Scholar
Kinekawa, Y and Kitabatake, N (1995) Turbidity and rheological properties of gels and sols prepared by heating process whey protein. Bioscience Biotechnology Biochemistry 59, 834–840.CrossRefGoogle Scholar
Kuramoto, S, Jenness, R, Coulter, ST and Choi, RP (1959) Standardization of the Harland-Ashworth test for whey protein nitrogen. Journal of Dairy Science 42, 28–38.CrossRefGoogle Scholar
Lucey, JA, Michelle, T, Harjinder, S and Peater, AM (1998) Effect of interactions between denatured whey proteins and casein micelles on the formation and rheological properties of acid skim milk gels. Journal of Dairy Research 65, 555–567.CrossRefGoogle Scholar
Mangino, ME, Liao, YY, Harper, NJ, Morr, CV and Zadow, JG (1987) Effect of heat processing on the functionality of whey protein concentrates. Journal of Food Science 52, 1522–1524.CrossRefGoogle Scholar
Mohomud, MD, Katsuno, N and Nishizu, N (2017) Formation of soluble protein complexes and yoghurt properties influenced by the addition of whey protein concentrate. Innovative Food Science & Emerging Technology 44, 173–180.CrossRefGoogle Scholar
Morand, M, Guyomarc'h, F and 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 and Technology 91, 97–126.CrossRefGoogle Scholar
Morr, CV and Foegeding, EA (1990) Composition and functionality of commercial whey and milk protein concentrates and isolates: a status report. Food Technology 44, 100–112.Google Scholar
Oka, D, Ono, W, Ohara, S, Noguchi, T and Takano, K (2018) Effect of heat-induced κ-casein dissociation on acid coagulation of milk. Journal of Dairy Research 85, 104–109.CrossRefGoogle Scholar
Rector, D, Matsudomi, N and Kinsella, JE (1991) Changes in gelling behavior of whey protein isolate and β-lactoglobulin during storage: possible mechanism(s). Journal of Food Science 56, 782–788.10.1111/j.1365-2621.1991.tb05381.xCrossRefGoogle Scholar
Schokker, EP, Singh, H and Creamer, LK (2000) Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin. International Dairy Journal 10, 843–853.CrossRefGoogle Scholar
Sodini, I, Mattas, J and Tong, PS (2006) Influence of pH and heat treatment of whey on the functional properties of whey protein concentrates in yoghurt. International Dairy Journal 16, 1464–1469.CrossRefGoogle Scholar
Vasbinder, AJ, Alting, AC and de Kruif, KG (2003) Quantification of heat-induced casein-whey protein interactions in milk and its relation to gelation kinetics. Colloids Surfaces B: Biointerfaces 31, 115–123.CrossRefGoogle Scholar
Vasbinder, AJ, Valde, VD and de Kruif, CG (2004) Gelation of casein-whey protein mixtures. Journal of Dairy Science 87, 1167–1176.CrossRefGoogle ScholarPubMed
Supplementary material: PDF

Oka et al. supplementary material

Oka et al. supplementary material

Download Oka et al. supplementary material(PDF)
PDF 196.5 KB