Cited by 82Proteins in Food SystemsProtein Hydrolysis and Bioactive PeptidesFood composition and properties

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The Effect of Gel Microstructure on Simulated Gastric Digestion of Protein Gels

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Opazo-Navarrete, Mauricio, Altenburg, Marte D., Boom, Remko M., Janssen, Anja E. M.·2018·Food Biophysics

Abstract

The objective of this study was to analyse the impact of the gel structure obtained by different heat-induced temperatures on the in vitro gastric digestibility at pH 2. To achieve this, gels were prepared from soy protein, pea protein, albumin from chicken egg white and whey protein isolate at varying temperatures (90, 120 and 140 °C) for 30 min. Gels were characterised prior to digestion via microstructure and SDS-PAGE analysis. Subsequently, the gastric digestion process was followed via the protein hydrolysis and HPSEC analysis up to 180 min. Peptides of different sizes (<5 kDa) were gradually formed during the digestion. Our results showed that gels induced at 140 °C were digested faster. The protein source and gelation temperature had great influence on the in vitro gastric protein digestibility.

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Fig. 1 SDS-PAGE profiles of protein gels: (a) S (soy protein isolate), S90 (soy protein gel made at 90 °C), S120 (soy protein gel made at 120 °C), S140 (soy protein gel made at 140 °C), (b) P (pea protein concentrate), P90 (pea protein gel made at 90 °C), P120 (pea protein gel made at 120 °C), P140 (pea protein gel made at 140 °C), (c) A (albumin from chicken egg white) A90 (albumin from chicken egg white protein gel made at 90 °C), A120 (albumin from chicken egg white protein gel made at 120 °C), A140 (albumin from chicken egg white protein gel made at 140 °C) and (d) W (whey protein isolate), W90 (whey protein gel made at 90 °C), W120 (whey protein gel made at 120 °C), W140 (whey protein gel made at 140 °C)
Fig. 1 SDS-PAGE profiles of protein gels: (a) S (soy protein isolate), S90 (soy protein gel made at 90 °C), S120 (soy protein gel made at 120 °C), S140 (soy protein gel made at 140 °C), (b) P (pea protein concentrate), P90 (pea protein gel made at 90 °C), P120 (pea protein gel made at 120 °C), P140 (pea protein gel made at 140 °C), (c) A (albumin from chicken egg white) A90 (albumin from chicken egg white protein gel made at 90 °C), A120 (albumin from chicken egg white protein gel made at 120 °C), A140 (albumin from chicken egg white protein gel made at 140 °C) and (d) W (whey protein isolate), W90 (whey protein gel made at 90 °C), W120 (whey protein gel made at 120 °C), W140 (whey protein gel made at 140 °C)CC BY · PubMed Central
Fig. 2 SEM images of protein gels made at different temperatures (90, 120 and 140 °C) using different sources. SPI, soy protein isolate; PPC, pea protein concentrate; Alb, albumin from chicken egg white; WPI, whey protein isolate
Fig. 2 SEM images of protein gels made at different temperatures (90, 120 and 140 °C) using different sources. SPI, soy protein isolate; PPC, pea protein concentrate; Alb, albumin from chicken egg white; WPI, whey protein isolateCC BY · PubMed Central
Fig. 3 Hardness prior digestion of the different protein gels. SPI, soy protein isolate; PPC, pea protein concentrate; Albumin, albumin from chicken egg white; WPI, whey protein isolate
Fig. 3 Hardness prior digestion of the different protein gels. SPI, soy protein isolate; PPC, pea protein concentrate; Albumin, albumin from chicken egg white; WPI, whey protein isolateCC BY · PubMed Central
Fig. 4 Hydrolysis profile of proteins solutions (×) and proteins gelled at 90 °C (◆), 120 °C (■) and 140 °C (△). a Soy protein gels, (b) pea protein gels, (c) albumin from chicken egg white gels and (d) whey protein gels
Fig. 4 Hydrolysis profile of proteins solutions (×) and proteins gelled at 90 °C (◆), 120 °C (■) and 140 °C (△). a Soy protein gels, (b) pea protein gels, (c) albumin from chicken egg white gels and (d) whey protein gelsCC BY · PubMed Central
Fig. 5 HPSEC profiles of gastric digestion of soy protein gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °C
Fig. 5 HPSEC profiles of gastric digestion of soy protein gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °CCC BY · PubMed Central
Fig. 6 HPSEC profiles of gastric digestion of pea protein gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °C
Fig. 6 HPSEC profiles of gastric digestion of pea protein gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °CCC BY · PubMed Central
Fig. 7 HPSEC profiles of gastric digestion of albumin from chicken egg white gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °C
Fig. 7 HPSEC profiles of gastric digestion of albumin from chicken egg white gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °CCC BY · PubMed Central
Fig. 8 HPSEC profiles of gastric digestion of whey protein gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °C
Fig. 8 HPSEC profiles of gastric digestion of whey protein gels made at: (a) 90 °C, (b) 120 °C and (c) 140 °CCC BY · PubMed Central
Fig. 9 HPSEC profiles of gastric digestion of different protein sources in solution (5% protein) of: (a) Soy protein isolate (SPI), (b) Pea protein concentrate (PPC), (c) Albumin from chicken egg white; (d) Whey protein isolate (WPI) and (e) Casein
Fig. 9 HPSEC profiles of gastric digestion of different protein sources in solution (5% protein) of: (a) Soy protein isolate (SPI), (b) Pea protein concentrate (PPC), (c) Albumin from chicken egg white; (d) Whey protein isolate (WPI) and (e) CaseinCC BY · PubMed Central

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Research works printed but not linked: 38

  1. C.D. Munialo, E. van der Linden, K. Ako, H.H.J. de Jong, Food Hydrocoll. 49, 104–117 (2015) · DOI
  2. K. Nyemb, C. Guérin-Dubiard, S. Pézenne, J. Jardin, V. Briard-Bion, C. Cauty, S. Rutherfurd, D. Dupont, F. Nau, Food Hydrocoll. 54, 315–327 (2016) · DOI
  3. J.M.S. Renkema, Formation, structure and rheological properties of soy protein gels. Ph.D. Thesis, Wageningen University, Wageningen, The Netherlands (2001)
  4. A.-M. Hermansson, J. Am. Oil Chem. Soc. 63(5), 658–666 (1986) · DOI
  5. C.-H. Wang, S. Damodaran, J. Agric. Food Chem. 39(3), 433–438 (1991) · DOI
  6. I. Norton, S. Moore, P. Fryer, Obes. Rev. 8(1), 83–88 (2007) · DOI
  7. S. Van Vliet, N.A. Burd, L.J. van Loon, J. Nutr. 145, 1981–1991 (2015) · DOI · Paper page
  8. N. Chen, M. Zhao, W. Sun, Food Chem. 141, 3224–3229 (2013) · DOI
  9. P.J.M. Pelgrom, A.M. Vissers, R.M. Boom, M.A.I. Schutyser, Food Res. Int. 53, 232–239 (2013) · DOI
  10. S.D. Arntfield, E.D. Murray, Can. Inst. Food Sci. Technol. J. 14(4), 289–294 (1981) · DOI
  11. X. Rui, Y. Fu, Q. Zhang, W. Li, F. Zare, X. Chen, M. Jiang, M. Dong, M. LWT-Food Sci. Technol. 71, 234–242 (2016) · DOI
  12. G.M. Bornhorst, M.J. Ferrua, R.P. Singh, J. Food Sci. 80, R924–R934 (2015) · DOI
  13. Q. Guo, A. Ye, M. Lad, D. Dalgleish, H. Singh, Soft Matter 10, 1214–1223 (2014) · DOI
  14. B.L. Dekkers, R. Hamoen, R.M. Boom, A.J. van der Goot, Innov. J. Food Eng. 222, 84–92 (2018) · DOI
  15. B.L. Dekkers, N.V. Constantinos, A.J. van der Goot, Innov. Food Sci. Emerg. 36, 193–200 (2016) · DOI
  16. Q. Luo, R.M. Boom, A.E.M. Janssen, LWT-Food Sci. Technol. 63(1), 161–168 (2015) · DOI
  17. G. Avila, M. Opazo-Navarrete, M. Meurs, M. Minor, G. Sala, M. van Boekel, M. Stieger, A.E.M. Janssen, Food Biophys. 11, 184–197 (2016) · DOI
  18. M.-L. Jalabert-Malbos, A. Mishellany-Dutuor, A. Woda, M.-A. Peyron, Food Qual. Prefer. 18, 803–812 (2007) · DOI
  19. B.E. Casey, K.J. Laidler, J. Am. Chem. Soc. 73, 1455–1457 (1951) · DOI
  20. J. Adler-Nissen, Enzymic Hydrolysis of Food Proteins (Elsevier Applied Science Publishers, New York, 1986), pp. 110–169
  21. I. Crévieu, B. Carré, A.-M. Chagneua, L. Quillien, J. Guéguen, S. Bérot, S.J. Agric, Food Chem. 45, 1295–1300 (1997) · DOI
  22. A.-M. Hermansson, Aggregation and Denaturation Involved in Gel Formation (SHERMAN, P. Food Texture and Rheology. New York: Academic Press, 1979), pp. 265 · DOI · Paper page
  23. J.E. Kinsella, Crit. Rev. Food Sci. Nutr. 21, 197–262 (1984) · DOI
  24. L.G. Phillips, D.M. Whitehead, J.E. Kinsella, Structure Function Properties of Food Proteins (San Diego, Academic Press, 1994), p. 271
  25. T. Furukawa, S. Ohta, A. Yamamoto, J. Texture Stu. 10, 333–346 (1979) · DOI
  26. T. Furukawa, S. Ohta, J. Texture Stu. 13(1), 59–69 (1982) · DOI
  27. C.Y. Ma, J. Holme, J. Food Sci. 47, 1454–1459 (1982) · DOI
  28. J.M. Aguilera, Food Technol. 49, 83–89 (1995)
  29. V.K. Gupta, H. Reuter, Neth. Milk Dairy J. 46, 89–100 (1992)
  30. F.J. Monahan, J.B. German, J.E. Kinsella, J. Agric. Food Chem. 43, 46–52 (1995) · DOI
  31. M. McSwiney, H. Singh, O.H. Campanella, Food Hydrocoll. 8, 441–453 (1994) · DOI
  32. R.H. Schmidt, in Protein functionality in foods, ed. by J. P. Cherry. Gelation and coagulation (ACS, Washington, 1981), pp. 131–147 · DOI
  33. L. Marciani, P.A. Gowland, R.C. Spiller, P. Manoj, R.J. Moore, P. Young, A.J. Fillery-Travis, Am. J. Physiol. Gastrointest. Liver Physiol. 280(6), G1227–G1233 (2001) · DOI · Paper page
  34. Q. Guo, A. Ye, M. Lad, M. Ferrua, D. Dalgleish, H. Singh, Food Funct. 6, 756–764 (2015) · DOI
  35. T. Lambers, W. van de Bosch, S. de Jong, Food Dig. 4, 1–6 (2013) · DOI
  36. K. Tsumura, T. Saito, W. Kugimiya, K. Inouye, J. Food Sci. 69, 363–367 (2004) · DOI
  37. N. Chen, Q. Zhao, W. Sun, M. Zhao, J. Agric. Food Chem. 61, 12139–12145 (2013) · DOI
  38. L. Laguna, P. Picouet, M.D. Guardia, C.M.G.C. Renard, A. Sarkar, LWT-Food Sci. Technol. 84, 511–519 (2017) · DOI

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Metadata

Authors
Opazo-Navarrete, M., Altenburg, M. D., Boom, R. M., & Janssen, A. E. M.
Affiliations
Wageningen University & Research (NL)
Corresponding author
Janssen, Anja E. M.
Venue
Food Biophysics
Published
2018-03-05
Volume
13
Issue
2
Pages
124-138
ISSN
  • 1557-1858 (ISSN-L)
  • 1557-1866
OpenAlex
W2791903335
Cited by
82
References
4
Citations by year
2026: 8 · 2025: 13 · 2024: 11 · 2023: 12 · 2022: 10 · 2021: 12 · 2020: 6 · 2019: 9 · 2018: 1
FWCI
5.27
Type
journal article
Language
en
Open access
Locations
  • Food Biophysics (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, other-oa)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Socio-Environmental Systems Modeling (acceptedVersion, cc-by)
  • Data Archiving and Networked Services (DANS) (submittedVersion, cc-by)
Funders
Wageningen University
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
  • Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
Keywords
gel microstructure, in vitro gastric digestion, protein gels, heat-induced gelation, gelation temperature, soy protein, pea protein, egg white albumin, whey protein isolate, proteolysis, peptide formation, protein digestibility

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