Journals / Journal of Advanced Research in Natural and Applied Sciences / 2020 / Cilt: 6 Sayı: 1

Interactions of Native and Denatured Whey Proteins with Caseins and Polysaccharides

Pages
180–189
Publication Date
2020-05-22
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Such interactions are important for the stability of food materials especially during processing and storage, therefore, a deep insight on this subject is important.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:In this review, interactions of native or denatured whey proteins with other proteins and polysaccharides were addressed.
📊
Key Findings & Data:Chemical structures of whey proteins and caseins as representatives of proteins and of gum Arabic and dextran as representatives of polysaccharides were explained.
💡
Conclusion & Impact:Such interactions are important for the stability of food materials especially during processing and storage, therefore, a deep insight on this subject is important.
🔬Design:Review & Systematic Survey
📍Scope:Comprehensive Sample
⚙️Variables:Aggregtion · dextran · gum Arabic

Abstract

In this review, interactions of native or denatured whey proteins with other proteins and polysaccharides were addressed. Chemical structures of whey proteins and caseins as representatives of proteins and of gum Arabic and dextran as representatives of polysaccharides were explained. Whey protein, as a mixture of different proteins, such as beta-lactoglobulin, alpha-lactalbumin, or bovine serum albumin, has a highly complex nature, and therefore, the main interaction occurs within these proteins upon processing. Structu-re of whey protein includes hydrogen bonds, disulfide bridges and free thiol group, all of which allows whey proteins highly reactive with other polymers. With these properties, whey proteins can be denatured via heating or acidification in a controlled way; and therefore, several functional particles with different sizes and shapes could be obtained. Here we explained the interactions of native and denatured whey proteins with caseins, gum Arabic and dextran in terms of their behaviuor in solutions or dispersions, their functional and rheological properties. Denaturation process includes mainly hydrophobic interacti-ons and is most of the time irreversible, whereas the complex formation of proteins with polysaccharides includes electrostatic and/or steric interactions and complex formation could be reversible or irreversible depending on the type of application. Such interactions are important for the stability of food materials especially during processing and storage, therefore, a deep insight on this subject is important.

Özet

In this review, interactions of native or denatured whey proteins with other proteins and polysaccharides were addressed. Chemical structures of whey proteins and caseins as representatives of proteins and of gum Arabic and dextran as representatives of polysaccharides were explained. Whey protein, as a mixture of different proteins, such as beta-lactoglobulin, alpha-lactalbumin, or bovine serum albumin, has a highly complex nature, and therefore, the main interaction occurs within these proteins upon processing. Structu-re of whey protein includes hydrogen bonds, disulfide bridges and free thiol group, all of which allows whey proteins highly reactive with other polymers. With these properties, whey proteins can be denatured via heating or acidification in a controlled way; and therefore, several functional particles with different sizes and shapes could be obtained. Here we explained the interactions of native and denatured whey proteins with caseins, gum Arabic and dextran in terms of their behaviuor in solutions or dispersions, their functional and rheological properties. Denaturation process includes mainly hydrophobic interacti-ons and is most of the time irreversible, whereas the complex formation of proteins with polysaccharides includes electrostatic and/or steric interactions and complex formation could be reversible or irreversible depending on the type of application. Such interactions are important for the stability of food materials especially during processing and storage, therefore, a deep insight on this subject is important.

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Cite This Article

COŞKUN, A. E. İ., ÖTLEŞ, S. (2020). Interactions of Native and Denatured Whey Proteins with Caseins and Polysaccharides. Journal of Advanced Research in Natural and Applied Sciences, Cilt: 6 Sayı: 1, 180–189. https://ajindex.com/articles/907476

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References (12)

  1. van den Akker, C. C., Schleeger, M., Bonn, M., & Koenderink, G. H. (2014). Structural basis for the polymorphism of β-lactoglobulin amyloid-like fibrils (Chapter 31). Bio-nanoimaging, Protein Misfolding and Aggregation, 333-343.
  2. Ako, K., Nicolai, T., Durand, D., & Brotons, G. (2009). Micro-phase separation explains the abrupt structural change of denatured globular protein gels on varying the ionic strength or the pH. Soft Matter, 5, 4033-4041.
  3. Anema, S. G., & Li, Y. (2003). 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.
  4. Benichou, A., Aserin, A., & Garti, N. (2002). Protein-polysaccharide interactions for stabilization of food emulsions. Journal of Dispersion Science and Technology, 23, 93-123.
  5. Carrasco, F., Chornet, E., Overend, R. P., & Costa, J. (1989). A generalized correlation for the viscosity of dextrans in aqueous solutions as a function of temperature, concentration, and molecular weight at low shear rates. Journal of Applied Polymer Science, 37, 2087-2098.
  6. Clare, D. A., & Daubert, C. R. (2010). Transglutaminase catalysis of modified whey protein dispersions. Journal of Food Science, 75, 369-377.
  7. Corredig, M., & Dalgleish, D. G. (1996). Effect of temperature and pH on the interactions of whey proteins with casein micelles in skim milk. Food Research International, 29, 49-55.
  8. Dai, Q., Zhu, X., Abbas, S., Karangwa, E., Zhang, X., Xia, S., Feng, B., & Jia, C. (2015). Stable nanoparticles prepared by heating electrostatic complexes of whey protein isolate-dextran conjugate and chondroitin sulfate. Journal of Agricultural and Food Chemistry, 63, 4179-4189.
  9. Doublier, J. L., Garnier, C., Renard, D., & Sanchez, C., 2000. Protein-polysaccharide interactions. Current Opinion in Colloid & Interface Science, 5, 202-214.
  10. Elzoghby, A. O., Elgohary, M. M., & Kamel, N. M. (2015). Implications of protein- and peptide-based nanoparticles as potential vehicles for anticancer drugs (Chapter 6). Advances in Protein Chemistry and Structural Biology, 98, 169-221.
  11. Ge, S., Kojio, K., Takahara, A., & Kajiyama, T. (1998). Bovine serum albumin adsorption onto immobilized organotrichlorosilane surface: influence of the phase separation on protein adsorption patterns. Journal of Biomaterials Science, Polymer Edition, 9, 131–50.
  12. Ghosh, A. K., & Bandyopadhyay, P. (2012). Polysaccharide-protein interactions and their relevance in food colloids. In D. N. K