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Volumn 84, Issue , 2017, Pages 634-642

Structural changes and functional properties of highly concentrated whey protein isolate-citrus pectin blends after defined, high temperature treatments

Author keywords

Citrus pectin; Emulsion; Heat treatment; Maillard reaction; Whey protein

Indexed keywords

DAIRIES; EMULSIFICATION; EMULSIONS; EXTRUSION; FLUORESCENCE; GLYCOSYLATION; HEAT TREATMENT; PROTEINS; REACTION PRODUCTS; SULFUR COMPOUNDS;

EID: 85021144446     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2017.06.026     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0042161834 scopus 로고    scopus 로고
    • Emulsifying properties of whey protein–dextran conjugates at low pH and different salt concentrations
    • Akhtar, M., Dickinson, E., Emulsifying properties of whey protein–dextran conjugates at low pH and different salt concentrations. Food Colloids, Biopolymers and Materials Special Issue 31:1–4 (2003), 125–132, 10.1016/S0927-7765(03)00049-3.
    • (2003) Food Colloids, Biopolymers and Materials Special Issue , vol.31 , Issue.1-4 , pp. 125-132
    • Akhtar, M.1    Dickinson, E.2
  • 2
    • 0034876817 scopus 로고    scopus 로고
    • Effect of pH and temperature on the formation of volatile compounds in cysteine/reducing sugar/starch mixtures during extrusion cooking
    • Ames, J.M., Guy, R., Kipping, G.J., Effect of pH and temperature on the formation of volatile compounds in cysteine/reducing sugar/starch mixtures during extrusion cooking. Journal of Agricultural and Food Chemistry 49:4 (2001), 1885–1894, 10.1021/jf0012547.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.4 , pp. 1885-1894
    • Ames, J.M.1    Guy, R.2    Kipping, G.J.3
  • 3
    • 0017520457 scopus 로고
    • Effect of dispersed-phase viscosity on the maximum stable drop size for breakup in turbulent flow
    • Arai, K., Konno, M., Matunaga, Y., Saito, S., Effect of dispersed-phase viscosity on the maximum stable drop size for breakup in turbulent flow. Journal of Chemical Engineering of Japan 10:4 (1977), 325–330, 10.1252/jcej.10.325.
    • (1977) Journal of Chemical Engineering of Japan , vol.10 , Issue.4 , pp. 325-330
    • Arai, K.1    Konno, M.2    Matunaga, Y.3    Saito, S.4
  • 5
    • 0003780934 scopus 로고
    • Untersuchungen zum kontinuierlichen Emulgierprozeß in Kolloidmühlen unter Berücksichtigung spezifischer Emulgatoreigenschaften und der Strömungsverhältnisse im Dispergierspalt (Dissertation)
    • Universität Karlsruhe Karlsruhe
    • Armbruster, H., Untersuchungen zum kontinuierlichen Emulgierprozeß in Kolloidmühlen unter Berücksichtigung spezifischer Emulgatoreigenschaften und der Strömungsverhältnisse im Dispergierspalt (Dissertation)., 1990, Universität Karlsruhe, Karlsruhe.
    • (1990)
    • Armbruster, H.1
  • 6
    • 85025546779 scopus 로고
    • The effect of the degree of esterification on the thermal stability and chain conformation of pectins
    • Axelos, M., Branger, M., The effect of the degree of esterification on the thermal stability and chain conformation of pectins. Food Hydrocolloids 7:2 (1993), 91–102, 10.1016/S0268-005X(09)80161-6.
    • (1993) Food Hydrocolloids , vol.7 , Issue.2 , pp. 91-102
    • Axelos, M.1    Branger, M.2
  • 7
    • 0001292240 scopus 로고
    • Maillard browning kinetics in a liquid model system
    • Baisier, W.M., Labuza, T.P., Maillard browning kinetics in a liquid model system. Journal of Agricultural and Food Chemistry 40:5 (1992), 707–713, 10.1021/jf00017a001.
    • (1992) Journal of Agricultural and Food Chemistry , vol.40 , Issue.5 , pp. 707-713
    • Baisier, W.M.1    Labuza, T.P.2
  • 8
    • 84876134220 scopus 로고    scopus 로고
    • D-Galacturonic acid as a highly reactive compound in nonenzymatic browning. 1. Formation of browning active degradation products
    • Bornik, M.-A., Kroh, L.W., D-Galacturonic acid as a highly reactive compound in nonenzymatic browning. 1. Formation of browning active degradation products. Journal of Agricultural and Food Chemistry 61:14 (2013), 3494–3500, 10.1021/jf303855s.
    • (2013) Journal of Agricultural and Food Chemistry , vol.61 , Issue.14 , pp. 3494-3500
    • Bornik, M.-A.1    Kroh, L.W.2
  • 9
    • 53149125654 scopus 로고    scopus 로고
    • Effect of extrusion on the emulsifying properties of soybean proteins and pectin mixtures modelled by response surface methodology
    • Bueno, A.S., Pereira, C.M., Menegassi, B., Arêas, J.A.G., Castro, I.A., Effect of extrusion on the emulsifying properties of soybean proteins and pectin mixtures modelled by response surface methodology. Journal of Food Engineering 90:4 (2009), 504–510, 10.1016/j.jfoodeng.2008.07.028.
    • (2009) Journal of Food Engineering , vol.90 , Issue.4 , pp. 504-510
    • Bueno, A.S.1    Pereira, C.M.2    Menegassi, B.3    Arêas, J.A.G.4    Castro, I.A.5
  • 10
    • 0009204554 scopus 로고
    • A possible mechanism for thermal texturization of soybean protein
    • Burgess, L., Stanley, D., A possible mechanism for thermal texturization of soybean protein. Canadian Institute of Food Science and Technology Journal 9:4 (1976), 228–231, 10.1016/S0315-5463(76)73681-2.
    • (1976) Canadian Institute of Food Science and Technology Journal , vol.9 , Issue.4 , pp. 228-231
    • Burgess, L.1    Stanley, D.2
  • 11
    • 0026121899 scopus 로고
    • Protein functionality modification by extrusion cooking
    • Camire, M.E., Protein functionality modification by extrusion cooking. Journal of the American Oil Chemists’ Society 68:3 (1991), 200–205.
    • (1991) Journal of the American Oil Chemists’ Society , vol.68 , Issue.3 , pp. 200-205
    • Camire, M.E.1
  • 12
    • 85021105511 scopus 로고    scopus 로고
    • 5 Amino acids, peptides, and proteins
    • Fennema's food chemistry
    • Damodaran, S., 5 Amino acids, peptides, and proteins. Fennema's food chemistry, 2007.
    • (2007)
    • Damodaran, S.1
  • 13
    • 84879935841 scopus 로고    scopus 로고
    • A holistic approach towards defined product attributes by Maillard-type food processing
    • Davidek, T., Illmann, S., Rytz, A., Blank, I., A holistic approach towards defined product attributes by Maillard-type food processing. Food & Function 4:7 (2013), 1105–1110, 10.1039/C3FO60080G.
    • (2013) Food & Function , vol.4 , Issue.7 , pp. 1105-1110
    • Davidek, T.1    Illmann, S.2    Rytz, A.3    Blank, I.4
  • 14
    • 8644277164 scopus 로고    scopus 로고
    • Formation of milk protein–pectin conjugates with improved emulsifying properties by controlled dry heating
    • Einhorn-Stoll, U., Ulbrich, M., Sever, S., Kunzek, H., Formation of milk protein–pectin conjugates with improved emulsifying properties by controlled dry heating. Food Hydrocolloids 19:2 (2005), 329–340, 10.1016/j.foodhyd.2004.07.005.
    • (2005) Food Hydrocolloids , vol.19 , Issue.2 , pp. 329-340
    • Einhorn-Stoll, U.1    Ulbrich, M.2    Sever, S.3    Kunzek, H.4
  • 15
    • 85008884185 scopus 로고    scopus 로고
    • A mechanistic approach to analyze extrusion processing of biopolymers by numerical, rheological, and optical methods
    • Emin, M.A., Schuchmann, H.P., A mechanistic approach to analyze extrusion processing of biopolymers by numerical, rheological, and optical methods. Trends in Food Science & Technology 60 (2017), 88–95, 10.1016/j.tifs.2016.10.003.
    • (2017) Trends in Food Science & Technology , vol.60 , pp. 88-95
    • Emin, M.A.1    Schuchmann, H.P.2
  • 16
    • 84855893272 scopus 로고    scopus 로고
    • Extrusion of soy protein with gelatin and sugars at low moisture content
    • Guerrero, P., Beatty, E., Kerry, J.P., Caba, K. de la, Extrusion of soy protein with gelatin and sugars at low moisture content. Journal of Food Engineering 110:1 (2012), 53–59, 10.1016/j.jfoodeng.2011.12.009.
    • (2012) Journal of Food Engineering , vol.110 , Issue.1 , pp. 53-59
    • Guerrero, P.1    Beatty, E.2    Kerry, J.P.3    Caba, K.D.L.4
  • 17
    • 67649411521 scopus 로고    scopus 로고
    • In situ compatibilization of starch–zein blends under shear flow
    • Habeych, E., van der Goot, A.J., Boom, R., In situ compatibilization of starch–zein blends under shear flow. Chemical Engineering Science 64:15 (2009), 3516–3524, 10.1016/j.ces.2009.04.034.
    • (2009) Chemical Engineering Science , vol.64 , Issue.15 , pp. 3516-3524
    • Habeych, E.1    van der Goot, A.J.2    Boom, R.3
  • 18
    • 33947448299 scopus 로고
    • Dehydrated foods, chemistry of browning reactions in model systems
    • Hodge, J.E., Dehydrated foods, chemistry of browning reactions in model systems. Journal of Agricultural and Food Chemistry 1:15 (1953), 928–943, 10.1021/jf60015a004.
    • (1953) Journal of Agricultural and Food Chemistry , vol.1 , Issue.15 , pp. 928-943
    • Hodge, J.E.1
  • 19
    • 84983516282 scopus 로고    scopus 로고
    • Influence of processing conditions on the formation of whey protein-citrus pectin conjugates in extrusion
    • Koch, L., Emin, M.A., Schuchmann, H.P., Influence of processing conditions on the formation of whey protein-citrus pectin conjugates in extrusion. Journal of Food Engineering 193 (2017), 1–9, 10.1016/j.jfoodeng.2016.08.012.
    • (2017) Journal of Food Engineering , vol.193 , pp. 1-9
    • Koch, L.1    Emin, M.A.2    Schuchmann, H.P.3
  • 20
    • 0034779970 scopus 로고    scopus 로고
    • The fluorescence of advanced maillard products is a good indicator of lysine damage during the maillard reaction
    • Leclère, J., Birlouez-Aragon, I., The fluorescence of advanced maillard products is a good indicator of lysine damage during the maillard reaction. Journal of Agricultural and Food Chemistry 49:10 (2001), 4682–4687, 10.1021/jf001433o.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.10 , pp. 4682-4687
    • Leclère, J.1    Birlouez-Aragon, I.2
  • 21
    • 84892883028 scopus 로고    scopus 로고
    • Comparative studies on the physicochemical properties of peanut protein isolate–polysaccharide conjugates prepared by ultrasonic treatment or classical heating
    • Li, C., Xue, H., Chen, Z., Ding, Q., Wang, X., Comparative studies on the physicochemical properties of peanut protein isolate–polysaccharide conjugates prepared by ultrasonic treatment or classical heating. Food Research International 57 (2014), 1–7, 10.1016/j.foodres.2013.12.038.
    • (2014) Food Research International , vol.57 , pp. 1-7
    • Li, C.1    Xue, H.2    Chen, Z.3    Ding, Q.4    Wang, X.5
  • 22
    • 0028565461 scopus 로고
    • Changes in rheological properties of gliadin as a function of temperature and moisture: Development of a state diagram
    • Madeka, H., Kokini, J.L., Changes in rheological properties of gliadin as a function of temperature and moisture: Development of a state diagram. Water in Foods Fundamental Aspects and Their Significance in Relation to Processing of Foods 22:1–4 (1994), 241–252, 10.1016/0260-8774(94)90033-7.
    • (1994) Water in Foods Fundamental Aspects and Their Significance in Relation to Processing of Foods , vol.22 , Issue.1-4 , pp. 241-252
    • Madeka, H.1    Kokini, J.L.2
  • 23
    • 0029910847 scopus 로고    scopus 로고
    • Effect of glass transition and cross-linking on rheological properties of zein: Development of a preliminary state diagram
    • Madeka, H., Kokini, J., Effect of glass transition and cross-linking on rheological properties of zein: Development of a preliminary state diagram. Cereal Chemistry (USA) 73:4 (1996), 433–438.
    • (1996) Cereal Chemistry (USA) , vol.73 , Issue.4 , pp. 433-438
    • Madeka, H.1    Kokini, J.2
  • 24
    • 0000916315 scopus 로고
    • Action des acides amines sur les sucres. Formation des melanoidins par voie methodiqué
    • Maillard, L.-C., Action des acides amines sur les sucres. Formation des melanoidins par voie methodiqué. Comptes rendus de l'Académie des Sciences 154 (1912), 66–68.
    • (1912) Comptes rendus de l'Académie des Sciences , vol.154 , pp. 66-68
    • Maillard, L.-C.1
  • 25
    • 25844445919 scopus 로고    scopus 로고
    • A critical evaluation of fluorescence as a potential marker for the Maillard reaction
    • Matiacevich, S.B., Pilar Buera, M., A critical evaluation of fluorescence as a potential marker for the Maillard reaction. Food Chemistry 95:3 (2006), 423–430, 10.1016/j.foodchem.2005.01.027.
    • (2006) Food Chemistry , vol.95 , Issue.3 , pp. 423-430
    • Matiacevich, S.B.1    Pilar Buera, M.2
  • 26
    • 0031585402 scopus 로고    scopus 로고
    • A study on advanced Maillard reaction in heated casein/sugar solutions: Fluorescence accumulation
    • Morales, F., van Boekel, M., A study on advanced Maillard reaction in heated casein/sugar solutions: Fluorescence accumulation. International Dairy Journal 7:11 (1997), 675–683, 10.1016/S0958-6946(97)00071-X.
    • (1997) International Dairy Journal , vol.7 , Issue.11 , pp. 675-683
    • Morales, F.1    van Boekel, M.2
  • 27
    • 0027347215 scopus 로고
    • Whey protein concentrates and isolates: Processing and functional properties
    • Morr, C.V., Ha, E.Y.W., Whey protein concentrates and isolates: Processing and functional properties. Critical Reviews in Food Science and Nutrition 33:6 (1993), 431–476, 10.1080/10408399309527643.
    • (1993) Critical Reviews in Food Science and Nutrition , vol.33 , Issue.6 , pp. 431-476
    • Morr, C.V.1    Ha, E.Y.W.2
  • 28
    • 0036604780 scopus 로고    scopus 로고
    • A hydrodynamic study of the depolymerisation of a high methoxy pectin at elevated temperatures
    • Morris, G., Foster, T., Harding, S., A hydrodynamic study of the depolymerisation of a high methoxy pectin at elevated temperatures. Carbohydrate Polymers 48:4 (2002), 361–367, 10.1016/S0144-8617(01)00270-3.
    • (2002) Carbohydrate Polymers , vol.48 , Issue.4 , pp. 361-367
    • Morris, G.1    Foster, T.2    Harding, S.3
  • 30
    • 4043107026 scopus 로고    scopus 로고
    • Improved emulsion stabilizing properties of whey protein isolate by conjugation with pectins
    • Neirynck, N., Van der Meeren, P., Bayarri Gorbe, S., Dierckx, S., Dewettinck, K., Improved emulsion stabilizing properties of whey protein isolate by conjugation with pectins. Food Hydrocolloids 18:6 (2004), 949–957, 10.1016/j.foodhyd.2004.03.004.
    • (2004) Food Hydrocolloids , vol.18 , Issue.6 , pp. 949-957
    • Neirynck, N.1    Van der Meeren, P.2    Bayarri Gorbe, S.3    Dierckx, S.4    Dewettinck, K.5
  • 31
    • 4444226270 scopus 로고    scopus 로고
    • Aggregation and degradation of plasticized wheat gluten during thermo-mechanical treatments, as monitored by rheological and biochemical changes
    • Pommet, M., Morel, M.-H., Redl, A., Guilbert, S., Aggregation and degradation of plasticized wheat gluten during thermo-mechanical treatments, as monitored by rheological and biochemical changes. Polymer 45:20 (2004), 6853–6860, 10.1016/j.polymer.2004.07.076.
    • (2004) Polymer , vol.45 , Issue.20 , pp. 6853-6860
    • Pommet, M.1    Morel, M.-H.2    Redl, A.3    Guilbert, S.4
  • 32
    • 84949192865 scopus 로고    scopus 로고
    • Influence of the degree of esterification on the emulsifying performance of conjugates formed between whey protein isolate and citrus pectin
    • Schmidt, U.S., Pietsch, V.L., Rentschler, C., Kurz, T., Endreß, H.-U., Schuchmann, H.P., Influence of the degree of esterification on the emulsifying performance of conjugates formed between whey protein isolate and citrus pectin. Food Hydrocolloids 56 (2016), 1–8, 10.1016/j.foodhyd.2015.11.015.
    • (2016) Food Hydrocolloids , vol.56 , pp. 1-8
    • Schmidt, U.S.1    Pietsch, V.L.2    Rentschler, C.3    Kurz, T.4    Endreß, H.-U.5    Schuchmann, H.P.6
  • 33
    • 0037624879 scopus 로고    scopus 로고
    • The chemical structure of pectins
    • G.B. Seymour J.P. Knox Blackwell; Published in U.S. and Canada only by CRC Press Oxford, Boca Raton, FL
    • Schols, H.A., Voragen, A.G.J., The chemical structure of pectins. Seymour, G.B., Knox, J.P., (eds.) Sheffield biological sciences. Pectins and their manipulation, 2002, Blackwell; Published in U.S. and Canada only by CRC Press, Oxford, Boca Raton, FL.
    • (2002) Sheffield biological sciences. Pectins and their manipulation
    • Schols, H.A.1    Voragen, A.G.J.2
  • 34
    • 0014141297 scopus 로고
    • Ultraviolet spectrophotometric determination of hexoses, pentoses, and uronic acids after their reactions with concentrated sulfuric acid
    • Scott, R.W., Moore, W.E., Effland, M.J., Millett, M.A., Ultraviolet spectrophotometric determination of hexoses, pentoses, and uronic acids after their reactions with concentrated sulfuric acid. Analytical Biochemistry 21:1 (1967), 68–80, 10.1016/0003-2697(67)90084-X.
    • (1967) Analytical Biochemistry , vol.21 , Issue.1 , pp. 68-80
    • Scott, R.W.1    Moore, W.E.2    Effland, M.J.3    Millett, M.A.4
  • 35
    • 79955638399 scopus 로고    scopus 로고
    • Properties of whey protein isolate–dextran conjugate prepared using pulsed electric field
    • Sun, W.-W., Yu, S.-j., Zeng, X.-A., Yang, X.-Q., Jia, X., Properties of whey protein isolate–dextran conjugate prepared using pulsed electric field. Food Research International 44:4 (2011), 1052–1058, 10.1016/j.foodres.2011.03.020.
    • (2011) Food Research International , vol.44 , Issue.4 , pp. 1052-1058
    • Sun, W.-W.1    Yu, S.-J.2    Zeng, X.-A.3    Yang, X.-Q.4    Jia, X.5
  • 36
    • 0001985208 scopus 로고
    • Comparison of the structural features of apple and citrus pectic substances
    • Vries, J. A. de, Rombouts, F.M., Voragen, A., Pilnik, W., Comparison of the structural features of apple and citrus pectic substances. Carbohydrate Polymers 4:2 (1984), 89–101, 10.1016/0144-8617(84)90016-X.
    • (1984) Carbohydrate Polymers , vol.4 , Issue.2 , pp. 89-101
    • Vries, J.A.D.1    Rombouts, F.M.2    Voragen, A.3    Pilnik, W.4


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