Dergiler / Celal Bayar Üniversitesi Fen Bilimleri Dergisi / 2020 / Cilt: 16 - Sayı: 1

pH-Dependent Behavior and Stability of Protein-Based Particles in Aqueous Media

Sayfa
95–102
Yayın Tarihi
2022-10-12
DOI
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⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

This review explained the chemical differences of proteins, preparation ofparticles using different methods, and stability of particles and their dispersions at different conditions.Such differences in protein particles should be carefully investigated before they are used in foodproducts, which could have complex matrix.

📌 3 Maddede Bu Makale

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Amaç & Hipotez:This review focused on the characteristics of protein particles from different sources, namely wheyproteins, sodium caseinate and gelatin, their structural stability and the stability of dispersions atdifferent pH values.
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Temel Bulgular & Veri:Wheyproteins undergo thermal denaturation above 68ᵒC, therefore heat-set gelatin was often used for particlepreparation.
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Sonuç & Katkı:This review explained the chemical differences of proteins, preparation ofparticles using different methods, and stability of particles and their dispersions at different conditions.Such differences in protein particles should be carefully investigated before they are used in foodproducts, which could have complex matrix.
🔬Tür:Literatür & Derleme Çalışması
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alan Parametreleri

Abstract

This review focused on the characteristics of protein particles from different sources, namely wheyproteins, sodium caseinate and gelatin, their structural stability and the stability of dispersions atdifferent pH values. To create particles, controlled aggregation and gelation were used in severalmethods. Different chemical structures of the proteins provide different gelation properties. Wheyproteins undergo thermal denaturation above 68ᵒC, therefore heat-set gelatin was often used for particlepreparation. When whey protein particles were prepared at the iso-electric point (IEP) of proteins, theybecame dense and small; whereas at other pH values, particles were soft and spherical due to increasedrepulsive forces between proteins. Such particles could swell when the pH of the aqueous phase wasaway from the IEP. Sodium caseinate is more heat stable compared to whey proteins; however, it is pHsensitive. When sodium caseinate particles were prepared through acidification, particles were stableagainst disintegration only around the IEP of proteins. More stable caseinate particles could be producedusing enzymatic crosslinking. On the other hand, gelatin particles, which were prepared via cold-setgelation, were stable over a wide pH range; however, as they were thermo-sensitive, particlesdisintegrated above 30ᵒC. This review explained the chemical differences of proteins, preparation ofparticles using different methods, and stability of particles and their dispersions at different conditions.Such differences in protein particles should be carefully investigated before they are used in foodproducts, which could have complex matrix.

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Bu Makaleye Atıf Yap

Ocak, B., Coşkun, A. E. İ., Ötleş, S., Ocak, Ö. Ö. (2022). pH-Dependent Behavior and Stability of Protein-Based Particles in Aqueous Media. Celal Bayar Üniversitesi Fen Bilimleri Dergisi, Cilt: 16 - Sayı: 1, 95–102. https://ajindex.com/articles/472127

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Kaynakça (14)

  1. Haug, A, Hostmark, AT, Harstad, OM. 2007. Bovine milk in human nutrition – a review. Lipids in Health and Disease; 6: 25-40
  2. Hammann, F, Schmid, M. 2014. Determination and quantification of molecular interactions in protein films: A review. Materials; 7: 7975-7996
  3. Pelegrine, DHG, Gasparetto, CA. 2005. Whey protein solubility as function of temperature and pH. LWT-Food Science and Technology; 38(1): 77-80
  4. Horne, DS. 2006. Casein micelle structure: Models and muddles. Current Opinion in Colloid and Interface Science; 11: 148-153
  5. Broyard, C, Gaucheron, F. 2015. Modifications of structures and functions of caseins: a scientific and technological challenge. Dairy Science and Technology; 95: 831-862
  6. Thorn, DC, Meehan, S, Sunde, M, Rekas, A, Gras, SL, MacPhee, CE, Dobson, CM, Wilson MR, Carver JA. 2005. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. Biochemistry; 44(51): 17027-36
  7. Braga, ALM, Menossi, M, Cunha, RL. 2006. The effect of the glucono-δ-lactone/caseinate ratio on sodium caseinate gelation. International Dairy Journal; 16: 389-398
  8. Chu, B, Zhou, Z, Wu, G, Farrell Jr, HM. 1995. Laser light scattering of model casein solutions: Effects of high temperature. Journal of Colloid and Interface Science; 170(1): 102-112
  9. Guo, MR, Fox, PF, Flynn, PF, Kindstedt, PS. 1996. Heatinduced modifications of the functional properties of sodium caseinate. International Dairy Journal; 6(5): 473-483
  10. Stanic, D, Monogioudi, E, Dilek, E, Radosavljevic, J, Atanaskovic-Markovic, M, Vuckovic, O, Raija, L, Mattinen, L, Buchert, J, Cirkovic Velickovic, T. 2010. Digestibility and allergenicity assessment of enzymatically crosslinked βcasein. Molecular Nutrition and Food Research; 54: 1273– 1284
  11. O’Kennedy, BT, Mounsey, JS, Murphy, F, Duggan, E, Kelly, PM. 2006. Factors affecting the acid gelation of sodium caseinate. International Dairy Journal; 16(10): 1132-1141
  12. Dickinson, E, Golding, M. 1997. Rheology of sodium caseinate stabilized oil-in-water emulsions. Journal of Colloid and Interface Science; 191(1): 166-176
  13. Gomez-Guillen, MC, Gimenez, B, Lopez-Caballero, ME, Montero, MP. 2011. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids; 25: 1813-1827
  14. Nikoo, M, Benjakul, S, Ocen, D, Yang, N, Xu, B, Zhang, L, Xu, X. 2013. Physical and chemical properties of gelatin from the skin of cultured Am