Pepsin diffusivity in whey protein gels and its effect on gastric digestion

Food Hydrocolloids

Volumn 66, Issue , 2017, Pages 318-325

  Luo, Qi ^a   Borst, Jan Willem ^a   Westphal, Adrie H ^a   Boom, Remko M ^a   Janssen, Anja E M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Diffusion; FCS; Gastric digestion; GFP; Pepsin; Whey protein gel

Indexed keywords

FLUORESCENCE SPECTROSCOPY; GELS; HYDROLYSIS; MICROSTRUCTURE; PROTEINS; SCANNING ELECTRON MICROSCOPY; SPECTROSCOPIC ANALYSIS;

FLUORESCENCE CORRELATION SPECTROSCOPY; GASTRIC DIGESTIONS; GEL SURFACE; GFP; HUMAN HEALTH; PEPSIN; PROTEIN GEL; WHEY PROTEIN GEL; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

DIFFUSION;

EID: 85007559990     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.11.046     Document Type: Article

References (29)

1. Akkermans, C., Venema, P., van der Goot, A.J., Gruppen, H., Bakx, E.J., Boom, R.M., et al. Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2. Biomacromolecules 9:5 (2008), 1474–1479, 10.1021/bm7014224.
2. Amsden, B., Solute diffusion within hydrogels. mechanisms and models. Macromolecules 31:23 (1998), 8382–8395, 10.1021/ma980765f.
3. Bornhorst, G.M., Chang, L.Q., Rutherfurd, S.M., Moughan, P.J., Singh, R.P., Gastric emptying rate and chyme characteristics for cooked brown and white rice meals in vivo. Journal of the Science of Food and Agriculture, 2013, 10.1002/jsfa.6160.
4. Bornhorst, G.M., Singh, R.P., Gastric digestion in vivo and in vitro: How the structural aspects of food influence the digestion process. Annual Review of Food Science and Technology 5:1 (2014), 111–132, 10.1146/annurev-food-030713-092346.
5. Collins, P.J., Houghton, L.A., Read, N.W., Horowitz, M., Chatterton, B.E., Heddle, R., et al. Role of the proximal and distal stomach in mixed solid and liquid meal emptying. Gut 32:6 (1991), 615–619, 10.1136/gut.32.6.615.
6. Colsenet, R., Söderman, O., Mariette, F., Pulsed field gradient NMR study of poly(ethylene glycol) diffusion in whey protein solutions and gels. Macromolecules 39:3 (2006), 1053–1059, 10.1021/ma0519922.
7. Croguennoc, P., Nicolai, T., Kuil, M.E., Hollander, J.G., Self-diffusion of native proteins and dextran in heat-set globular protein gels. The Journal of Physical Chemistry B 105:24 (2001), 5782–5788, 10.1021/jp0043726.
8. Doi, E., Gels and gelling of globular proteins. Trends in Food Science & Technology 4:1 (1993), 1–5, 10.1016/s0924-2244(05)80003-2.
9. Erickson, H.P., Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biological Procedures Online 11 (2009), 32–51, 10.1007/s12575-009-9008-x.
10. Fersht, A., Structures and mechanisms of selected enzymes. Enzyme structure and mechanism, 2nd ed., 1985, W. H. Freeman & Co, New York, NY, 389–452.
11. Guo, Q., Ye, A., Lad, M., Ferrua, M., Dalgleish, D., Singh, H., Disintegration kinetics of food gels during gastric digestion and its role on gastric emptying: An in vitro analysis. Food & Function 6 (2015), 756–764, 10.1039/c4fo00700j.
12. Inouye, K., Fruton, J.S., Studies on the specificity of pepsin. Biochemistry 6:6 (1967), 1765–1777.
13. Kwaaitaal, M., Schor, M., Hink, M.A., Visser, A.J.W.G., de Vries, S.C., Fluorescence correlation spectroscopy and fluorescence recovery after photobleaching to study receptor kinase mobility in planta. Dissmeyer, N., Schnittger, A., (eds.) Plant kinases, 2011, Humana Press, New York, 225–242, 10.1007/978-1-61779-264-9_13 Retrieved from.
14. Lakowicz, J.R., Fluorescence correlation spectroscopy. Principles of fluorescence spectroscopy, 2006, Springer US, New York, 797–840.
15. Luo, Q., Boom, R.M., Janssen, A.E.M., Digestion of protein and protein gels in simulated gastric environment. LWT - Food Science and Technology 63:1 (2015), 161–168, 10.1016/j.lwt.2015.03.087.
16. Nolles, A., Westphal, A.H., de Hoop, J.A., Fokkink, R.G., Kleijn, J.M., van Berkel, W.J.H., et al. Encapsulation of GFP in complex coacervate core micelles. Biomacromolecules 16:5 (2015), 1542–1549, 10.1021/acs.biomac.5b00092.
17. Nyemb-Diop, K., Causeur, D., Jardin, J., Briard-Bion, V., Guérin-Dubiard, C., Rutherfurd, S.M., et al. Investigating the impact of egg white gel structure on peptide kinetics profile during in vitro digestion. Food Research International 88:Part B (2016), 302–309, 10.1016/j.foodres.2016.01.004.
18. Petit, J.-M., Zhu, X.X., Macdonald, P.M., Solute probe diffusion in aqueous solutions of poly(vinyl alcohol) as studied by pulsed-gradient spin-echo NMR spectroscopy. Macromolecules 29:1 (1996), 70–76, 10.1021/ma9510597.
19. Piper, D., Fenton, B.H., pH stability and activity curves of pepsin with special reference to their clinical importance. Gut 6:5 (1965), 506–508.
20. Royant, A., Noirclerc-Savoye, M., Stabilizing role of glutamic acid 222 in the structure of enhanced green fluorescent protein. Journal of Structural Biology 174:2 (2011), 385–390, 10.1016/j.jsb.2011.02.004.
21. Singh, H., Ye, A., Ferrua, M.J., Aspects of food structures in the digestive tract. Current Opinion in Food Science 3 (2015), 85–93, 10.1016/j.cofs.2015.06.007.
22. Skakun, V., Digris, A., Apanasovich, V., Global analysis of autocorrelation functions and photon counting distributions in fluorescence fluctuation spectroscopy. Engelborghs, Y., Visser, A.J.W.G., (eds.) Fluorescence spectroscopy and microscopy, 2014, Humana Press, New York, 719–741.
23. Stylianopoulos, T., Poh, M.-Z., Insin, N., Bawendi, M.G., Fukumura, D., Munn, L.L., et al. Diffusion of particles in the extracellular matrix: The Effect of Repulsive Electrostatic Interactions. Biophysical Journal 99:5 (2010), 1342–1349, 10.1016/j.bpj.2010.06.016.
24. Thorne, R.G., Lakkaraju, A., Rodriguez-Boulan, E., Nicholson, C., In vivo diffusion of lactoferrin in brain extracellular space is regulated by interactions with heparan sulfate. Proceedings of the National Academy of Sciences 105:24 (2008), 8416–8421, 10.1073/pnas.0711345105.
25. Tyn, M.T., Gusek, T.W., Prediction of diffusion coefficients of proteins. Biotechnology and Bioengineering 35:4 (1990), 327–338, 10.1002/bit.260350402.
26. Videcoq, P., Steenkeste, K., Bonnin, E., Garnier, C., A multi-scale study of enzyme diffusion in macromolecular solutions and physical gels of pectin polysaccharides. Soft Matter 9:20 (2013), 5110–5118, 10.1039/c3sm00058c.
27. Walstra, P., Physical chemistry of foods. 2002, CRC Press, Boca Raton, FL.
28. Whitney, E.N., Cataldo, C.B., Sharon, R.R., Understanding normal and clinical nutrition. 5th ed., 1998, Wadsworth Publishing Company, Inc, Belmont, CA.
29. Wöll, D., Fluorescence correlation spectroscopy in polymer science. RSC Advances 4:5 (2013), 2447–2465, 10.1039/c3ra44909b.