메뉴 건너뛰기




Volumn 239, Issue , 2018, Pages 898-910

Exploring the breakdown of dairy protein gels during in vitro gastric digestion using time-lapse synchrotron deep-UV fluorescence microscopy

Author keywords

Dairy gels; Gastric digestion; Pepsin; Synchrotron deep UV microscopy

Indexed keywords

AMINO ACIDS; BIOLOGICAL MATERIALS; CHEMICAL ANALYSIS; FLUORESCENCE; FLUORESCENCE MICROSCOPY; KINETICS; PROTEINS;

EID: 85023594249     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.07.023     Document Type: Article
Times cited : (49)

References (43)
  • 2
    • 34547336610 scopus 로고    scopus 로고
    • New insights in the interpretation of tryptophan fluorescence: Origin of the fluorescence lifetime and characterization of a new fluorescence parameter in proteins: the emission to excitation ratio
    • Albani, J.R., New insights in the interpretation of tryptophan fluorescence: Origin of the fluorescence lifetime and characterization of a new fluorescence parameter in proteins: the emission to excitation ratio. Journal of Fluorescence 17:4 (2007), 406–417, 10.1007/s10895-007-0183-3.
    • (2007) Journal of Fluorescence , vol.17 , Issue.4 , pp. 406-417
    • Albani, J.R.1
  • 3
    • 84881531287 scopus 로고    scopus 로고
    • Acid and rennet gels exhibit strong differences in the kinetics of milk protein digestion and amino acid bioavailability
    • Barbé, F., Ménard, O., Gouar, Y..Le., Buffière, C., Famelart, M.-H., Laroche, B.,.. Dupont, D., Acid and rennet gels exhibit strong differences in the kinetics of milk protein digestion and amino acid bioavailability. Food Chemistry 143 (2014), 1–8, 10.1016/j.foodchem.2013.07.100.
    • (2014) Food Chemistry , vol.143 , pp. 1-8
    • Barbé, F.1    Ménard, O.2    Gouar, Y.L.3    Buffière, C.4    Famelart, M.-H.5    Laroche, B.6    Dupont, D.7
  • 4
    • 84867898775 scopus 로고    scopus 로고
    • The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids
    • Barbé, F., Ménard, O., Le Gouar, Y., Buffière, C., Famelart, M.-H., Laroche, B.,.. Rémond, D., The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids. Food Chemistry 136:3–4 (2013), 1203–1212, 10.1016/j.foodchem.2012.09.022.
    • (2013) Food Chemistry , vol.136 , Issue.3-4 , pp. 1203-1212
    • Barbé, F.1    Ménard, O.2    Le Gouar, Y.3    Buffière, C.4    Famelart, M.-H.5    Laroche, B.6    Rémond, D.7
  • 5
    • 84959502918 scopus 로고    scopus 로고
    • Engineering digestion: Multiscale processes of food digestion
    • Bornhorst, G.M., Gouseti, O., Wickham, M.S.J., Bakalis, S., Engineering digestion: Multiscale processes of food digestion. Journal of Food Science 81:3 (2016), R534–R543, 10.1111/1750-3841.13216.
    • (2016) Journal of Food Science , vol.81 , Issue.3 , pp. R534-R543
    • Bornhorst, G.M.1    Gouseti, O.2    Wickham, M.S.J.3    Bakalis, S.4
  • 6
    • 84897704473 scopus 로고    scopus 로고
    • Gastric digestion in vivo and in vitro: How the structural aspects of food influence the digestion process
    • 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 (2014), 111–132, 10.1146/annurev-food-030713-092346.
    • (2014) Annual Review of Food Science and Technology , vol.5 , pp. 111-132
    • Bornhorst, G.M.1    Singh, R.P.2
  • 7
    • 84989935115 scopus 로고    scopus 로고
    • Designing dairy desserts for weight management: Structure, physical properties and in vitro gastric digestion
    • Borreani, J., Llorca, E., Quiles, A., Hernando, I., Designing dairy desserts for weight management: Structure, physical properties and in vitro gastric digestion. Food Chemistry 220 (2017), 137–144, 10.1016/j.foodchem.2016.09.202.
    • (2017) Food Chemistry , vol.220 , pp. 137-144
    • Borreani, J.1    Llorca, E.2    Quiles, A.3    Hernando, I.4
  • 8
    • 84956652156 scopus 로고    scopus 로고
    • Impact of gastric pH profiles on the proteolytic digestion of mixed βlg-Xanthan biopolymer gels
    • Dekkers, B.L., Kolodziejczyk, E., Acquistapace, S., Engmann, J., Wooster, T.J., Impact of gastric pH profiles on the proteolytic digestion of mixed βlg-Xanthan biopolymer gels. Food & Function 7:1 (2016), 58–68, 10.1039/c5fo01085c.
    • (2016) Food & Function , vol.7 , Issue.1 , pp. 58-68
    • Dekkers, B.L.1    Kolodziejczyk, E.2    Acquistapace, S.3    Engmann, J.4    Wooster, T.J.5
  • 9
    • 0030492742 scopus 로고    scopus 로고
    • PH-Induced physicochemical modifications of native phosphocaseinate suspensions: Influence of aqueous phase
    • Famelart, M.H., Lepesant, F., Gaucheron, F., Graet, Y..Le., Schuck, P., PH-Induced physicochemical modifications of native phosphocaseinate suspensions: Influence of aqueous phase. Le Lait 76:5 (1996), 445–460, 10.1051/lait:1996534.
    • (1996) Le Lait , vol.76 , Issue.5 , pp. 445-460
    • Famelart, M.H.1    Lepesant, F.2    Gaucheron, F.3    Graet, Y.L.4    Schuck, P.5
  • 10
    • 84959247713 scopus 로고    scopus 로고
    • Commercial cheeses with different texture have different disintegration and protein/peptide release rates during simulated in vitro digestion
    • Fang, X., Rioux, L.-E., Labrie, S., Turgeon, S.L., Commercial cheeses with different texture have different disintegration and protein/peptide release rates during simulated in vitro digestion. International Dairy Journal 56 (2016), 169–178, 10.1016/j.idairyj.2016.01.023.
    • (2016) International Dairy Journal , vol.56 , pp. 169-178
    • Fang, X.1    Rioux, L.-E.2    Labrie, S.3    Turgeon, S.L.4
  • 13
    • 0041349500 scopus 로고    scopus 로고
    • Fluorescence spectroscopy investigation of acid-or rennet-induced coagulation of milk
    • Herbert, S., Riaublanc, A., Bouchet, B., Gallant, D.J., Dufour, E., Fluorescence spectroscopy investigation of acid-or rennet-induced coagulation of milk. Journal of Dairy Science 82:10 (1999), 2056–2062, 10.3168/jds.S0022-0302(99)75446-9.
    • (1999) Journal of Dairy Science , vol.82 , Issue.10 , pp. 2056-2062
    • Herbert, S.1    Riaublanc, A.2    Bouchet, B.3    Gallant, D.J.4    Dufour, E.5
  • 14
    • 38449090657 scopus 로고    scopus 로고
    • Food, not nutrients, is the fundamental unit in nutrition
    • Jacobs, D.R., Tapsell, L.C., Food, not nutrients, is the fundamental unit in nutrition. Nutrition Reviews 65:10 (2007), 439–450 http://www.ncbi.nlm.nih.gov/pubmed/17972438.
    • (2007) Nutrition Reviews , vol.65 , Issue.10 , pp. 439-450
    • Jacobs, D.R.1    Tapsell, L.C.2
  • 16
    • 84907546143 scopus 로고    scopus 로고
    • Modelling of pepsin digestibility of myofibrillar proteins and of variations due to heating
    • Kondjoyan, A., Daudin, J.-D., Santé-Lhoutellier, V., Modelling of pepsin digestibility of myofibrillar proteins and of variations due to heating. Food Chemistry 172 (2015), 265–271, 10.1016/j.foodchem.2014.08.110.
    • (2015) Food Chemistry , vol.172 , pp. 265-271
    • Kondjoyan, A.1    Daudin, J.-D.2    Santé-Lhoutellier, V.3
  • 17
    • 44949255007 scopus 로고    scopus 로고
    • Disintegration of solid foods in human stomach
    • Kong, F., Singh, R.P., Disintegration of solid foods in human stomach. Journal of Food Science 73:5 (2008), R67–R80, 10.1111/j.1750-3841.2008.00766.x.
    • (2008) Journal of Food Science , vol.73 , Issue.5 , pp. R67-R80
    • Kong, F.1    Singh, R.P.2
  • 18
    • 70450250246 scopus 로고    scopus 로고
    • Digestion of raw and roasted almonds in simulated gastric environment
    • Kong, F., Singh, R.P., Digestion of raw and roasted almonds in simulated gastric environment. Food Biophysics 4:4 (2009), 365–377, 10.1007/s11483-009-9135-6.
    • (2009) Food Biophysics , vol.4 , Issue.4 , pp. 365-377
    • Kong, F.1    Singh, R.P.2
  • 19
    • 70350068444 scopus 로고    scopus 로고
    • Modes of disintegration of solid foods in simulated gastric environment
    • Kong, F., Singh, R.P., Modes of disintegration of solid foods in simulated gastric environment. Food Biophysics 4:3 (2009), 180–190, 10.1007/s11483-009-9116-9.
    • (2009) Food Biophysics , vol.4 , Issue.3 , pp. 180-190
    • Kong, F.1    Singh, R.P.2
  • 20
    • 79651473008 scopus 로고    scopus 로고
    • Solid loss of carrots during simulated gastric digestion
    • Kong, F., Singh, R.P., Solid loss of carrots during simulated gastric digestion. Food Biophysics 6:1 (2011), 84–93, 10.1007/s11483-010-9178-8.
    • (2011) Food Biophysics , vol.6 , Issue.1 , pp. 84-93
    • Kong, F.1    Singh, R.P.2
  • 21
    • 84894725094 scopus 로고    scopus 로고
    • Impact of the dairy matrix structure on milk protein digestion kinetics: Mechanistic modelling based on mini-pig in vivo data
    • Le Feunteun, S., Barbé, F., Rémond, D., Ménard, O., Le Gouar, Y., Dupont, D., Laroche, B., Impact of the dairy matrix structure on milk protein digestion kinetics: Mechanistic modelling based on mini-pig in vivo data. Food and Bioprocess Technology 7:4 (2014), 1099–1113, 10.1007/s11947-013-1116-6.
    • (2014) Food and Bioprocess Technology , vol.7 , Issue.4 , pp. 1099-1113
    • Le Feunteun, S.1    Barbé, F.2    Rémond, D.3    Ménard, O.4    Le Gouar, Y.5    Dupont, D.6    Laroche, B.7
  • 22
    • 41749087125 scopus 로고    scopus 로고
    • Effects of acidification with and without rennet on a concentrated casein system: A kinetic NMR probe diffusion study
    • Le Feunteun, S., Mariette, F., Effects of acidification with and without rennet on a concentrated casein system: A kinetic NMR probe diffusion study. Macromolecules 41:6 (2008), 2079–2086, 10.1021/ma702248z.
    • (2008) Macromolecules , vol.41 , Issue.6 , pp. 2079-2086
    • Le Feunteun, S.1    Mariette, F.2
  • 23
    • 0034871048 scopus 로고    scopus 로고
    • Effect of heat treatment on the physical properties of milk gels made with both rennet and acid
    • Lucey, J.A., Tamehana, M., Singh, H., Munro, P.A., Effect of heat treatment on the physical properties of milk gels made with both rennet and acid. Cheese Ripening and Technology 11:4–7 (2001), 559–565, 10.1016/S0958-6946(01)00081-4.
    • (2001) Cheese Ripening and Technology , vol.11 , Issue.4-7 , pp. 559-565
    • Lucey, J.A.1    Tamehana, M.2    Singh, H.3    Munro, P.A.4
  • 24
    • 84928706230 scopus 로고    scopus 로고
    • Digestion of protein and protein gels in simulated gastric environment
    • 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.
    • (2015) LWT – Food Science and Technology , vol.63 , Issue.1 , pp. 161-168
    • Luo, Q.1    Boom, R.M.2    Janssen, A.E.M.3
  • 25
    • 85007559990 scopus 로고    scopus 로고
    • Pepsin diffusivity in whey protein gels and its effect on gastric digestion
    • Luo, Q., Borst, J.W., Westphal, A.H., Boom, R.M., Janssen, A.E.M., Pepsin diffusivity in whey protein gels and its effect on gastric digestion. Food Hydrocolloids 66 (2017), 318–325, 10.1016/j.foodhyd.2016.11.046.
    • (2017) Food Hydrocolloids , vol.66 , pp. 318-325
    • Luo, Q.1    Borst, J.W.2    Westphal, A.H.3    Boom, R.M.4    Janssen, A.E.M.5
  • 26
    • 84861577631 scopus 로고    scopus 로고
    • The effect of gel structure on the kinetics of simulated gastrointestinal digestion of bovine beta-lactoglobulin
    • Macierzanka, A., Boettger, F., Lansonneur, L., Groizard, R., Jean, A.-S., Rigby, N.M.,.. Mackie, A.R., The effect of gel structure on the kinetics of simulated gastrointestinal digestion of bovine beta-lactoglobulin. Food Chemistry 134:4 (2012), 2156–2163, 10.1016/j.foodchem.2012.04.018.
    • (2012) Food Chemistry , vol.134 , Issue.4 , pp. 2156-2163
    • Macierzanka, A.1    Boettger, F.2    Lansonneur, L.3    Groizard, R.4    Jean, A.-S.5    Rigby, N.M.6    Mackie, A.R.7
  • 27
    • 0034247906 scopus 로고    scopus 로고
    • Structure and scaling behavior of aging rennet-induced casein gels examined by confocal microscopy and permeametry
    • Mellema, M., Heesakkers, J.W.M., van Opheusden, J.H.J., van Vliet, T., Structure and scaling behavior of aging rennet-induced casein gels examined by confocal microscopy and permeametry. Langmuir 16:17 (2000), 6847–6854, 10.1021/la000135i.
    • (2000) Langmuir , vol.16 , Issue.17 , pp. 6847-6854
    • Mellema, M.1    Heesakkers, J.W.M.2    van Opheusden, J.H.J.3    van Vliet, T.4
  • 28
    • 0037177375 scopus 로고    scopus 로고
    • Effects of structural rearrangements on the rheology of rennet-induced casein particle gels
    • Mellema, M., Walstra, P., van Opheusden, J.H.J., van Vliet, T., Effects of structural rearrangements on the rheology of rennet-induced casein particle gels. Advances in Colloid and Interface Science 98:1 (2002), 25–50, 10.1016/S0001-8686(01)00089-6.
    • (2002) Advances in Colloid and Interface Science , vol.98 , Issue.1 , pp. 25-50
    • Mellema, M.1    Walstra, P.2    van Opheusden, J.H.J.3    van Vliet, T.4
  • 29
    • 84901667773 scopus 로고    scopus 로고
    • A standardised static in vitro digestion method suitable for food – An international consensus
    • Minekus, M., Alminger, M., Alvito, P., Ballance, S., Bohn, T., Bourlieu, C.,.. Brodkorb, A., A standardised static in vitro digestion method suitable for food – An international consensus. Food & Function 5:6 (2014), 1113–1124, 10.1039/C3FO60702J.
    • (2014) Food & Function , vol.5 , Issue.6 , pp. 1113-1124
    • Minekus, M.1    Alminger, M.2    Alvito, P.3    Ballance, S.4    Bohn, T.5    Bourlieu, C.6    Brodkorb, A.7
  • 30
    • 42149100435 scopus 로고    scopus 로고
    • Microscopy, microstructure and displacement of proteins from interfaces: Implications for food quality and digestion
    • Morris, V.J., Gunning, A.P., Microscopy, microstructure and displacement of proteins from interfaces: Implications for food quality and digestion. Soft Matter 4:5 (2008), 943–951, 10.1039/B718904D.
    • (2008) Soft Matter , vol.4 , Issue.5 , pp. 943-951
    • Morris, V.J.1    Gunning, A.P.2
  • 32
    • 84896108126 scopus 로고    scopus 로고
    • The extent of ovalbumin in vitro digestion and the nature of generated peptides are modulated by the morphology of protein aggregates
    • Nyemb, K., Guérin-Dubiard, C., Dupont, D., Jardin, J., Rutherfurd, S.M., Nau, F., The extent of ovalbumin in vitro digestion and the nature of generated peptides are modulated by the morphology of protein aggregates. Food Chemistry 157 (2014), 429–438, 10.1016/j.foodchem.2014.02.048.
    • (2014) Food Chemistry , vol.157 , pp. 429-438
    • Nyemb, K.1    Guérin-Dubiard, C.2    Dupont, D.3    Jardin, J.4    Rutherfurd, S.M.5    Nau, F.6
  • 33
    • 84946201445 scopus 로고    scopus 로고
    • The structural properties of egg white gels impact the extent of in vitro protein digestion and the nature of peptides generated
    • Nyemb, K., Guérin-Dubiard, C., Pézennec, S., Jardin, J., Briard-Bion, V., Cauty, C.,.. Nau, F., The structural properties of egg white gels impact the extent of in vitro protein digestion and the nature of peptides generated. Food Hydrocolloids 54:Part B (2016), 315–327, 10.1016/j.foodhyd.2015.10.011.
    • (2016) Food Hydrocolloids , vol.54 , pp. 315-327
    • Nyemb, K.1    Guérin-Dubiard, C.2    Pézennec, S.3    Jardin, J.4    Briard-Bion, V.5    Cauty, C.6    Nau, F.7
  • 35
    • 0013806544 scopus 로고
    • PH stability and activity curves of pepsin with special reference to their clinical importance
    • Piper, D.W., Fenton, B.H., PH stability and activity curves of pepsin with special reference to their clinical importance. Gut 6:5 (1965), 506–508, 10.1136/gut.6.5.506.
    • (1965) Gut , vol.6 , Issue.5 , pp. 506-508
    • Piper, D.W.1    Fenton, B.H.2
  • 36
    • 84858954599 scopus 로고    scopus 로고
    • Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of α(S)- and β-casein
    • Post, A.E., Arnold, B., Weiss, J., Hinrichs, J., Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of α(S)- and β-casein. Journal of Dairy Science 95:4 (2012), 1603–1616, 10.3168/jds.2011-4641.
    • (2012) Journal of Dairy Science , vol.95 , Issue.4 , pp. 1603-1616
    • Post, A.E.1    Arnold, B.2    Weiss, J.3    Hinrichs, J.4
  • 37
    • 0000475382 scopus 로고
    • Preliminary note on the change in casein micelles caused by acidification [skim milk]
    • Retrieved from
    • Roefs, S.P.F.M., Walstra, P., Dalgleish, D.G., Horne, D.S., Preliminary note on the change in casein micelles caused by acidification [skim milk]. Netherlands Milk and Dairy Journal (Netherlands) 39 (1985), 119–122 Retrieved from http://agris.fao.org/agris-search/search.do?recordID=NL8582416.
    • (1985) Netherlands Milk and Dairy Journal (Netherlands) , vol.39 , pp. 119-122
    • Roefs, S.P.F.M.1    Walstra, P.2    Dalgleish, D.G.3    Horne, D.S.4
  • 39
    • 79952146837 scopus 로고    scopus 로고
    • In situ tracking of enzymatic breakdown of starch granules by synchrotron UV fluorescence microscopy
    • Tawil, G., Jamme, F., Réfrégiers, M., Viksø-Nielsen, A., Colonna, P., Buléon, A., In situ tracking of enzymatic breakdown of starch granules by synchrotron UV fluorescence microscopy. Analytical Chemistry 83:3 (2011), 989–993, 10.1021/ac1027512.
    • (2011) Analytical Chemistry , vol.83 , Issue.3 , pp. 989-993
    • Tawil, G.1    Jamme, F.2    Réfrégiers, M.3    Viksø-Nielsen, A.4    Colonna, P.5    Buléon, A.6
  • 40
    • 85006790648 scopus 로고    scopus 로고
    • Pepsin diffusion in dairy gels depends on casein concentration and microstructure
    • Thévenot, J., Cauty, C., Legland, D., Dupont, D., Floury, J., Pepsin diffusion in dairy gels depends on casein concentration and microstructure. Food Chemistry 223 (2017), 54–61, 10.1016/j.foodchem.2016.12.014.
    • (2017) Food Chemistry , vol.223 , pp. 54-61
    • Thévenot, J.1    Cauty, C.2    Legland, D.3    Dupont, D.4    Floury, J.5
  • 41
    • 84942855575 scopus 로고    scopus 로고
    • Mathematical models of food degradation in the human stomach
    • M. Boland M. Golding H. Singh Academic Press, Elsevier USA
    • Van Wey, A.S., Shorten, P.R., Mathematical models of food degradation in the human stomach. Boland, M., Golding, M., Singh, H., (eds.) Food structures, digestion and health, 2014, Academic Press, Elsevier, USA, 172–245.
    • (2014) Food structures, digestion and health , pp. 172-245
    • Van Wey, A.S.1    Shorten, P.R.2
  • 42
    • 0000892233 scopus 로고
    • The syneresis of curd
    • P.F. Fox Springer, US Boston, MA Retrieved from
    • Walstra, P., The syneresis of curd. Fox, P.F., (eds.) Cheese: Chemistry, physics and microbiology, 1993, Springer, US, Boston, MA, 141–191 Retrieved from http://link.springer.com/10.1007/978-1-4615-2650-6_5.
    • (1993) Cheese: Chemistry, physics and microbiology , pp. 141-191
    • Walstra, P.1
  • 43
    • 84938810641 scopus 로고    scopus 로고
    • Formation of a structured clot during the gastric digestion of milk: Impact on the rate of protein hydrolysis
    • Ye, A., Cui, J., Dalgleish, D., Singh, H., Formation of a structured clot during the gastric digestion of milk: Impact on the rate of protein hydrolysis. Food Hydrocolloids 52 (2016), 478–486, 10.1016/j.foodhyd.2015.07.023.
    • (2016) Food Hydrocolloids , vol.52 , pp. 478-486
    • Ye, A.1    Cui, J.2    Dalgleish, D.3    Singh, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.