Role of the bolus degree of structure on the protein digestibility during in vitro digestion of a pea protein-fortified sponge cake chewed by elderly

Journal of Texture Studies

Volumn 51, Issue 1, 2020, Pages 134-143

  Assad Bustillos, Melissa ^a,b,c   Palier, Juliette ^a   Rabesona, Hanitra ^a   Choiset, Yvan ^a   Della Valle, Guy ^a   Feron, Gilles ^b  

^a INRA   (France)

^b CENTRE DES SCIENCES DU GOÛT ET DE L ALIMENTATION   (France)

^c CERELAB   (France)

Author keywords

bolus viscosity; digestibility; INFOGEST; oral processing; proteolysis

Indexed keywords

ELECTROPHORESIS; PROTEOLYSIS; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS; VISCOSITY;

DIGESTIBILITY; IN-VITRO DIGESTIONS; INFOGEST; ORAL PROCESSING; PEA PROTEIN ISOLATES; PRIMARY AMINO GROUPS; PROTEIN DIGESTIBILITY; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS;

PROTEINS;

STARCH;

AGED; CHEMISTRY; DIGESTION; FOOD HANDLING; HUMAN; KINETICS; MASTICATION; METABOLISM; PHYSIOLOGY; PROTEIN DEGRADATION; VISCOSITY;

AGED; DIGESTION; FOOD HANDLING; HUMANS; KINETICS; MASTICATION; PEA PROTEINS; PROTEOLYSIS; STARCH; VISCOSITY;

EID: 85074797080     PISSN: 00224901     EISSN: 17454603     Source Type: Journal    
DOI: 10.1111/jtxs.12486     Document Type: Article

References (46)

1. Assad-Bustillos, M., Tournier, C., Feron, G., Guessasma, S., Reguerre, A. L., & Della Valle, G. (2019). Fragmentation of two soft cereal products during oral processing in the elderly: Impact of product properties and oral health status. Food Hydrocolloids, 91, 153–165. https://doi.org/10.1016/j.foodhyd.2019.01.009
2. Assad-Bustillos, M. (2019). Food oral processing and chewing mechanisms in the elderly applied to the development of soft cereal foods fortified with proteins. (PhD Thesis). University of Nantes, 224p.
3. Assad-Bustillos, M., Tournier, C., Septier, C., Della Valle, G., & Feron, G. (2019). Relationships of oral comfort perception and bolus properties in the elderly with salivary flow rate and oral health status for two soft cereal foods. Food Research International, 118, 13–21. https://doi.org/10.1016/j.foodres.2017.11.057
4. Barać, M., Čabrilo, S., Pešić, M., Stanojević, S., Pavlićević, M., Maćej, O., & Ristić, N. (2011). Functional properties of pea (Pisum sativum, L.) protein isolates modified with chymosin. International Journal of Molecular Sciences, 12(12), 8372–8387. https://doi.org/10.3390/ijms12128372
5. Bauer, J., Biolo, G., Cederholm, T., Cesari, M., Cruz-Jentoft, A. J., Morley, J. E., … Boirie, Y. (2013). Evidence-based recommendations for optimal dietary protein intake in older people: A position paper from the PROT-AGE study group. Journal of the American Medical Directors Association, 14(8), 542–559. https://doi.org/10.1016/j.jamda.2013.05.021
6. Bertrand-Harb, C., Nicolas, M.-G., Dalgalarrondo, M., & Chobert, J. M. (1993). Determination of alkylation degree by three colorimetric methods and amino acid analysis: A comparative study. Sciences Des Aliments, 13(3), 577–584.
7. Bohn, T., Carriere, F., Day, L., Deglaire, A., Egger, L., Freitas, D., … Dupont, D. (2018). Correlation between in vitro and in vivo data on food digestion. What can we predict with static in vitro digestion models? Critical Reviews in Food Science and Nutrition, 58(13), 2239–2261. https://doi.org/10.1080/10408398.2017.1315362
8. Boye, J., Zare, F., & Pletch, A. (2010). Pulse proteins: Processing, characterization, functional properties and applications in food and feed. Food Research International, 43(2), 414–431. https://doi.org/10.1016/j.foodres.2009.09.003
9. Church, F. C., Porter, D. H., Catignani, G. L., & Swaisgood, H. E. (1985). An o-phthalaldehyde spectrophotometric assay for proteinases. Analytical Biochemistry, 146(2), 343–348.
10. Dangin, M., Boirie, Y., Guillet, C., & Beaufrère, B. (2002). Influence of the protein digestion rate on protein turnover in Young and elderly subjects. The Journal of Nutrition, 132(10), 3228S–3233S. https://doi.org/10.1093/jn/131.10.3228S
11. Dardevet, D., Remond, D., Peyron, M. A., Papet, I., Savary-Auzeloux, I., & Mosoni, L. (2012). Muscle wasting and resistance of muscle anabolism: The "anabolic threshold concept" for adapted nutritional strategies during sarcopenia. Scientific World Journal, 2012, 1–6. https://doi.org/10.1100/2012/269531
12. De Zorzi, M., Curioni, A., Simonato, B., Giannattasio, M., & Pasini, G. (2007). Effect of pasta drying temperature on gastrointestinal digestibility and allergenicity of durum wheat proteins. Food Chemistry, 104(1), 353–363. https://doi.org/10.1016/J.FOODCHEM.2006.11.057
13. Deutz, N. E. P., Bauer, J. M., Barazzoni, R., Biolo, G., Boirie, Y., Bosy-Westphal, A., … Calder, P. C. (2014). Protein intake and exercise for optimal muscle function with aging: Recommendations from the ESPEN Expert Group. Clinical Nutrition, 33(6), 929–936. https://doi.org/10.1016/J.CLNU.2014.04.007
14. Dewaest, M., Villemejane, C., Berland, S., Michon, C., Verel, A., & Morel, M.-H. (2017). Changes in protein size distribution during wheat flour cake processing. LWT - Food Science and Technology, 79, 333–341. https://doi.org/10.1016/j.lwt.2017.01.036
15. Fennema, O. (2017). In S. Damodaran & K. L. Parkin (Eds.), Fennema's food chemistry (5th ed.). Boca Raton, Florida: CRC Press.
16. Fontana, A., Polverino de Laureto, P., De Filippis, V., Scaramella, E., & Zambonin, M. (1997). Probing the partly folded states of proteins by limited proteolysis. Folding and Design, 2(2), R17–R26. https://doi.org/10.1016/S1359-0278(97)00010-2
17. Freitas, D., Le Feunteun, S., Panouillé, M., & Souchon, I. (2017). The important role of salivary α-amylase in gastric digestion of wheat bread starch. Food & Function, 9, 200–208. https://doi.org/10.1039/C7FO01484H
18. Galanakis, C. (2017). What is the difference between bioavailability bioaccessibility and protein-fortified of food components?| SciTech Connect. Retrieved from http://scitechconnect.elsevier.com/bioavailability-bioaccessibility-bioactivity-food-components/.
19. Gao, J., Lin, S., Jin, X., Wang, Y., Yin, J., Dong, Z., & Zhou, W. (2019). In vitro digestion of bread: How is it influenced by the bolus characteristics? Journal of Texture Studies, 50, 257–268. https://doi.org/10.1111/jtxs.12391
20. Gueguen, J. (1989). Relation between conformation and surface hydrophobicity of pea (Pisum sativum L.) globulins. Journal of Agricultural and Food Chemistry, 37(5), 1236–1241. https://doi.org/10.1021/jf00089a008
21. Gularte, M. A., Gómez, M., & Rosell, C. M. (2012). Impact of legume flours on quality and in vitro digestibility of starch and protein from gluten-free cakes. Food and Bioprocess Technology, 5(8), 3142–3150. https://doi.org/10.1007/s11947-011-0642-3
22. Habiba, R. (2002). Changes in anti-nutrients, protein solubility, digestibility, and HCl-extractability of ash and phosphorus in vegetable peas as affected by cooking methods. Food Chemistry, 77(2), 187–192. https://doi.org/10.1016/S0308-8146(01)00335-1
23. Humphrey, S. P., & Williamson, R. T. (2001). A review of saliva: Normal composition, flow, and function. The Journal of Prosthetic Dentistry, 85(2), 162–169. https://doi.org/10.1067/mpr.2001.113778
24. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685. https://doi.org/10.1038/227680a0
25. Laguna, L., Picouet, P., Guàrdia, M. D., Renard, C. M. G. C., & Sarkar, A. (2017). In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments. LWT - Food Science and Technology, 84, 511–519. https://doi.org/10.1016/j.lwt.2017.06.021
26. Lawrence, A.-M., & Besir, H. (2009). Staining of proteins in gels with Coomassie G-250 without organic solvent and acetic acid. Journal of Visualized Experiments, 30, e1350. https://doi.org/10.3791/1350
27. Leake, J. L., Hawkins, R., & Locker, D. (1994). Social and functional impact of reduced posterior dental units in older adults. Journal of Oral Rehabilitation, 21(1), 1–10. https://doi.org/10.1111/j.1365-2842.1994.tb01119.x
28. Lorieau, L., Halabi, A., Ligneul, A., Hazart, E., Dupont, D., & Floury, J. (2018). Impact of the dairy product structure and protein nature on the proteolysis and amino acid bioaccessiblity during in vitro digestion. Food Hydrocolloids, 82, 399–411. https://doi.org/10.1016/j.foodhyd.2018.04.019
29. Mession, J. L., Sok, N., Assifaoui, A., & Saurel, R. (2013). Thermal denaturation of pea globulins (Pisum sativum L.) - molecular interactions leading to heat-induced protein aggregation. Journal of Agricultural and Food Chemistry, 61(6), 1196–1204. https://doi.org/10.1021/jf303739n
30. Minekus, M., Alminger, M., Alvito, P., Ballance, S., Bohn, T., Bourlieu, C., … Brodkorb, A. (2014). A standardised static in vitro digestion method suitable for food – An international consensus. Food & Function, 5(6), 1113–1124. https://doi.org/10.1039/c3fo60702j
31. Overduin, J., Guérin-Deremaux, L., Wils, D., & Lambers, T. T. (2015). NUTRALYS® pea protein: Characterization of in vitro gastric digestion and in vivo gastrointestinal peptide responses relevant to satiety. Food & Nutrition Research, 59(1), 25622. https://doi.org/10.3402/fnr.v59.25622
32. Pasini, G., Simonato, B., Giannattasio, M., Peruffo, A. D. B., & Curioni, A. (2001). Modifications of wheat flour proteins during in vitro digestion of bread dough, crumb, and crust: An electrophoretic and immunological study. Journal of Agricultural and Food Chemistry, 49(5), 2254–2261. https://doi.org/10.1021/jf0014260
33. Pentikäinen, S., Sozer, N., Närväinen, J., Ylätalo, S., Teppola, P., Jurvelin, J., … Poutanen, K. (2014). Effects of wheat and rye bread structure on mastication process and bolus properties. Food Research International, 66, 356–364. https://doi.org/10.1016/j.foodres.2014.09.034
34. Peyron, M. A., Woda, A., Bourdiol, P., & Hennequin, M. (2017). Age-related changes in mastication. Journal of Oral Rehabilitation, 44(4), 299–312. https://doi.org/10.1111/joor.12478
35. Rémond, D., Machebeuf, M., Yven, C., Buffière, C., Mioche, L., Mosoni, L., & Mirand, P. P. (2007). Postprandial whole-body protein metabolism after a meat meal is influenced by chewing efficiency in elderly subjects. American Journal of Clinical Nutrition, 85(5), 1286–1292. https://doi.org/10.1093/ajcn/85.5.1286
36. Rémond, D., Shahar, D. R., Gille, D., Pinto, P., Kachal, J., Peyron, M.-A., … Vergères, G. (2015). Understanding the gastrointestinal tract of the elderly to develop dietary solutions that prevent malnutrition. Oncotarget, 6(16), 13858–13898. https://doi.org/10.18632/oncotarget.4030
37. Shani-Levi, C., Alvito, P., Andrés, A., Assunção, R., Barberá, R., Blanquet-Diot, S., … Lesmes, U. (2017). Extending in vitro digestion models to specific human populations: Perspectives, practical tools and bio-relevant information. Trends in Food Science & Technology, 60, 52–63. https://doi.org/10.1016/j.tifs.2016.10.017
38. Shewry, P. R., Tatham, A. S., Forde, J., Kreis, M., & Miflin, B. J. (1986). The classification and nomenclature of wheat gluten proteins: A reassessment. Journal of Cereal Science, 4(2), 97–106. https://doi.org/10.1016/S0733-5210(86)80012-1
39. Sommier, A., Dumoulin, E., Douiri, I., & Chipeaux, C. (2012). Characterization of sponge cake baking in an instrumented pilot oven. International Journal of Food Studies, 1, 144–158. https://doi.org/10.7455/ijfs/1.2.2012.a5
40. Spellman, D., McEvoy, E., O'Cuinn, G., & FitzGerald, R. J. (2003). Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis. International Dairy Journal, 13(6), 447–453. https://doi.org/10.1016/S0958-6946(03)00053-0
41. Tzitzikas, E. N., Vincken, J.-P., de Groot, J., Gruppen, H., & Visser, R. G. F. (2006). Genetic variation in pea seed globulin composition. Journal of Agricultural and Food Chemistry, 54(2), 425–433. https://doi.org/10.1021/jf0519008
42. Vandenberghe-Descamps, M., Labouré, H., Prot, A., Septier, C., Tournier, C., Feron, G., & Sulmont-Rossé, C. (2016). Salivary flow decreases in healthy elderly people independently of dental status and drug intake. Journal of Texture Studies, 47(4), 353–360. https://doi.org/10.1111/jtxs.12191
43. Wilderjans, E., Luyts, A., Brijs, K., & Delcour, J. A. (2013). Ingredient functionality in batter type cake making. Trends in Food Science & Technology, 30(1), 6–15. https://doi.org/10.1016/j.tifs.2013.01.001
44. Wilderjans, E., Luyts, A., Goesaert, H., Brijs, K., & Delcour, J. A. (2010). A model approach to starch and protein functionality in a pound cake system. Food Chemistry, 120(1), 44–51. https://doi.org/10.1016/J.FOODCHEM.2009.09.067
45. Young, V. R., & Pellett, P. L. (1994). Plant proteins in relation to human protein and amino acid nutrition. The American Journal of Clinical Nutrition, 59(5), 1203S–1212S. https://doi.org/10.1093/ajcn/59.5.1203S
46. Zhang, Y.-Y., Song, Y., Hu, X.-S., Liao, X.-J., Ni, Y.-Y., & Li, Q.-H. (2012). Effects of sugars in batter formula and baking conditions on 5-hydroxymethylfurfural and furfural formation in sponge cake models. Food Research International, 49(1), 439–445. https://doi.org/10.1016/J.FOODRES.2012.07.012