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Rheological and microstructural characterisation of heat-induced whey protein isolate gels affected by the addition of caseinomacropeptide

Published online by Cambridge University Press:  28 February 2022

Paula V. Guedes ,
Rilton A. de Freitas ,
Célia R. C. Franco  and
Lys Mary B. Cândido
Paula V. Guedes*
Affiliation:
Post-graduate Programme of Food Engineering, Chemical Engineering Department, Federal University of Paraná, P.O. Box 19011, Curitiba, PR, Brazil
Rilton A. de Freitas
Affiliation:
Chemistry Department, Federal University of Paraná, P.O. Box 19032, Curitiba, PR, Brazil
Célia R. C. Franco
Affiliation:
Centre of Biological Sciences, Department of Cell Biology, Federal University of Paraná, P.O. Box 19031, Curitiba, PR, Brazil
Lys Mary B. Cândido
Affiliation:
Post-graduate Programme of Food Engineering, Chemical Engineering Department, Federal University of Paraná, P.O. Box 19011, Curitiba, PR, Brazil
*
Author for correspondence: Paula V. Guedes, Email: [email protected]
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Abstract

Caseinomacropeptide (CMP) is derived from the chymosin cleavage of κ-casein during cheese production. This study developed gels from CMPs, which were isolated by different ultrafiltration systems, and whey protein isolate (WPI), and studied their rheological and ultrastructural characteristics. The 30% WPI gel showed high elastic modulus (G′) values and stronger structure than the other samples with CMP. Another gel, with 50% protein, 30% WPI and 20% CMP sample isolated from the 30 kDa retentate, had a weaker structure and lower G′ value. The third gel, with 30% WPI and 20% CMP sample from the 5 kDa retentate derived from the 30 kDa retentate, presented intermediate structural strength. Despite the increase in protein concentration from the addition of CMP, there was a decrease in the strength of the gel network. Different CMP isolation processes also contributed to differences in the microscopic analysis of gel structures with the same protein content.

Keywords

Caseinomacropeptidegelationmicrostructurerheologywhey protein isolate
Type
Research Article
Information
Journal of Dairy Research , Volume 89 , Issue 1 , February 2022 , pp. 109 - 116
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press on behalf of Hannah Dairy Research Foundation

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References

Abd El-Salam, MH, El-Shibiny, S and Salem, A (2009) Factors affecting the functional properties of whey protein products: a review. Food Reviews International 25, 251–270.CrossRefGoogle Scholar
ASSOCIATION OF OFFICIAL ANALYTICAL CHEMISTS (AOAC) (2010) Official Methods of Analysis of AOAC International, 18ªth edn. Gaithersburg: AOAC International, Washington, USA.Google Scholar
Brody, EP (2000) Biological activities of bovine glycomacropeptide. British Journal of Nutrition 84, 39–46.10.1017/S0007114500002233CrossRefGoogle ScholarPubMed
Brummer, R (2006) Rheology Essentials of Cosmetic and Food Emulsions. Berlin, Germany: Springer-Verlag.Google Scholar
Burgardt, VCF, Zuge, LCB, de Bonna Sartor, G, et al. (2015) The addition of carboxymethylcellulose in caseinomacropeptide acid gels: rheological, optical and microstructural characteristics. Food Hydrocolloids 49, 11–17.CrossRefGoogle Scholar
Delfour, A, Jolles, J, Alais, C and Jolles, P (1965) Caseino-glycopeptides: characterization of a methionin residue and of the N-terminal sequence. Biochemical and Biophysical Research Communications 19, 452–455.CrossRefGoogle ScholarPubMed
Donato, I, Schmitt, C, Rouvet, M and Bovetto, L (2009) Mechanism of formation of stable heat-induced ß-lactoglobulin microgels. International Dairy Journal 19, 295–306.CrossRefGoogle Scholar
Folin, O and Wu, H (1920) A simplified and improved method for the determination of sugar. Journal of Biological Chemistry 41, 367–374.10.1016/S0021-9258(18)87198-8CrossRefGoogle Scholar
Fu, X, Chen, X, Wen, R, He, X, Shang, X, Liao, Z and Yang, L (2007) Polyethylene-octene elastomer/starch blends: miscibility, morphology and mechanical properties. Journal of Polymer Research 14, 297–304.10.1007/s10965-007-9110-1CrossRefGoogle Scholar
Gaspard S, J, Sharma, P, Fitzgerald, C, et al. (2021) Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2. Food Hydrocolloids 112, 106–249.10.1016/j.foodhyd.2020.106249CrossRefGoogle Scholar
Ikeda, S and Foegeding, EA (1999) Effects of lecithin on thermally induced whey protein isolate gels. Food Hydrocolloids 13, 239–244.10.1016/S0268-005X(99)00005-3CrossRefGoogle Scholar
Kreuβ, M, Strixner, T and Kulozik, U (2009) The effect of glycosylation on the interfacial properties of bovine caseinomacropeptide. Food Hydrocolloids 23, 1818–1826.Google Scholar
Kuhn, KR, Cavallieri, ALF and Cunha, RL (2011) Cold-set whey protein-flaxseed gum gels induced by mono or divalent salt addition. Food Hydrocolloids 25, 1302–1310.CrossRefGoogle Scholar
Kutschmann, EM (2003) Rheological analysis of the stability of pharmaceutical suspensions. Manufacturing Chemist 74, 50–51.Google Scholar
Loria, KG, Pilosof, AMR and Farías, ME (2018) Influence of calcium and sodium chloride on caseinomacropeptide self-assembly and flow behaviour at neutral pH. LWT – Food Science and Technology 98, 598–605.10.1016/j.lwt.2018.09.029CrossRefGoogle Scholar
Loveday, SM, Wang, XL, Rao, MA, Anema, SG, Creamer, LK and Singh, H (2010) Tuning the properties of B-lactoglobulin nanofibrils with pH, NaCl and CaCl2. International Dairy Journal 20, 571–579.CrossRefGoogle Scholar
Mollé, D and Léonil, J (2005) Quantitative determination of bovine k-casein macropeptide in dairy products by liquid chromatography electrospray coupled to tamed mass spectrometry (LC-ESI MS) and liquid chromatography electrospray coupled to tamed mass spectrometry (LC-ESI MS MS). International Dairy Journal 15, 419–428.CrossRefGoogle Scholar
Ono, T, Yada, R, Yutani, K and Nakai, S (1987) Comparison of conformations of k-casein, para-k-casein and glycomacropeptide. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology 911, 318–325.10.1016/0167-4838(87)90072-0CrossRefGoogle Scholar
Otte, J, Schumacher, E, Ipsen, R, Ju, ZY and Qvist, KB (1999) Protease-induced gelation of unheated and heated whey proteins: effects of pH, temperature, and concentrations of protein, enzyme and salts. International Dairy Journal 9, 801–912.CrossRefGoogle Scholar
Purwanti, N, Peters, JPCM and Goot, AJVD (2013) Protein micro-structuring as a tool to texturize protein foods. Food & Function 4, 277–282.CrossRefGoogle ScholarPubMed
Schramm, G (2006) Rheology and Rheometry: Theoretical and Practical Foundations. Translation and adaptation: Cheila Mothé et al. Sao Paulo: Artliber.Google Scholar
Smith, MH, Edwards, PJ, Palmano, KP and Creamer, LK (2002) Structural features of bovine caseinomacropeptide A and B by 1 H nuclear magnetic resonance spectroscopy. Journal of Dairy Research 69, 85–94.10.1017/S0022029901005271CrossRefGoogle Scholar
Steffe, JF (1996) Rheological Methods in Food Process Engineering, 2ªnd edn. Michigan: Freeman.Google Scholar
Svanborg, S, Johansen, A, Abrahamsen, RK, et al. (2016) Caseinomacropeptide influences the functional properties of a whey protein concentrate. International Dairy Journal 60, 14–23.CrossRefGoogle Scholar
Thoma-worringer, C, Sorensen, J and López Fandiño, R (2006) Health effects and technological features of caseinomacropeptide. International Dairy Journal 16, 1324–1333.10.1016/j.idairyj.2006.06.012CrossRefGoogle Scholar
Thomar, P, Benyahia, L, Durand, D, et al. (2014) The influence of adding monovalent salt on the rheology of concentrated sodium caseinate suspensions and the solubility of calcium caseinate. International Dairy Journal 37, 48–54.CrossRefGoogle Scholar
Veith, PD and Reynolds, EC (2004) Production of a high gel strength whey protein concentrate from cheese whey. Journal of Dairy Science 87, 831–840.CrossRefGoogle ScholarPubMed
Villumsen, NS, Jensen, HB, Thu Le, TT, Moller, HS, Nordvang, RT, Nielsen, LR, et al. (2015) Self-assembly of caseinomacropeptide as a potential key mechanism in the formation of visible storage induced aggregates in acidic whey protein isolate dispersions. International Dairy Journal 49, 8–15.10.1016/j.idairyj.2015.05.003CrossRefGoogle Scholar
Wang, G, Liu, M, Cao, L, Yongsawatdigul, J, Xiong, S and Liu, R (2018) Effects of different NaCl concentration on self-assembly of silver carp myosin. Food Bioscience 24, 1–8.10.1016/j.fbio.2018.05.002CrossRefGoogle Scholar