메뉴 건너뛰기




Volumn 153, Issue , 2017, Pages 253-262

Enhanced ovalbumin stability at oil-water interface by phosphorylation and identification of phosphorylation site using MALDI-TOF mass spectrometry

Author keywords

Interfacial properties; MALDI TOF MS; Ovalbumin; Phosphorylation site

Indexed keywords

CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; EMULSIFICATION; EMULSIONS; MASS SPECTROMETRY; PARTICLE SIZE; PH; PHASE INTERFACES;

EID: 85014446238     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2017.02.027     Document Type: Article
Times cited : (39)

References (56)
  • 1
    • 84962653012 scopus 로고    scopus 로고
    • Effects of coconut (Cocos nucifera L.) protein hydrolysates obtained from enzymatic hydrolysis on the stability and rheological properties of oil–in–water emulsions
    • [1] Thaiphanit, S., Schleining, G., Anprung, P., Effects of coconut (Cocos nucifera L.) protein hydrolysates obtained from enzymatic hydrolysis on the stability and rheological properties of oil–in–water emulsions. Food Hydrocoll. 60 (2016), 252–264.
    • (2016) Food Hydrocoll. , vol.60 , pp. 252-264
    • Thaiphanit, S.1    Schleining, G.2    Anprung, P.3
  • 2
    • 0033828828 scopus 로고    scopus 로고
    • The protein net electric charge determines the surface rheological properties of ovalbumin adsorbed at the air–water interface
    • [2] Pezennec, S., Gauthier, F., Alonso, C., Graner, F., Croguennec, T., Brulé, G., Renault, A., The protein net electric charge determines the surface rheological properties of ovalbumin adsorbed at the air–water interface. Food Hydrocoll. 14 (2000), 463–472.
    • (2000) Food Hydrocoll. , vol.14 , pp. 463-472
    • Pezennec, S.1    Gauthier, F.2    Alonso, C.3    Graner, F.4    Croguennec, T.5    Brulé, G.6    Renault, A.7
  • 3
    • 79952108115 scopus 로고    scopus 로고
    • Rheological properties of ovalbumin hydrogels as affected by surfactants addition
    • [3] Hassan, N., Messina, P.V., Dodero, V.I., Ruso, J.M., Rheological properties of ovalbumin hydrogels as affected by surfactants addition. Int. J. Biol. Macromol. 48 (2011), 495–500.
    • (2011) Int. J. Biol. Macromol. , vol.48 , pp. 495-500
    • Hassan, N.1    Messina, P.V.2    Dodero, V.I.3    Ruso, J.M.4
  • 4
    • 84887042108 scopus 로고    scopus 로고
    • Selenization of ovalbumin by dry-heating in the presence of selenite: effect on protein structure and antioxidant activity
    • [4] Li, C.P., He, Z., Wang, X., Yang, L., Yin, C., Zhang, N., Lin, J., Zhao, H., Selenization of ovalbumin by dry-heating in the presence of selenite: effect on protein structure and antioxidant activity. Food Chem. 148C (2014), 209–217.
    • (2014) Food Chem. , vol.148C , pp. 209-217
    • Li, C.P.1    He, Z.2    Wang, X.3    Yang, L.4    Yin, C.5    Zhang, N.6    Lin, J.7    Zhao, H.8
  • 5
    • 84867694100 scopus 로고    scopus 로고
    • Improvement of functional properties of ovalbumin phosphorylated by dry-heating in the presence of pyrophosphate
    • [5] Lei, L., Chi, Y., Improvement of functional properties of ovalbumin phosphorylated by dry-heating in the presence of pyrophosphate. Eur. Food Res. Technol. 235 (2012), 981–987.
    • (2012) Eur. Food Res. Technol. , vol.235 , pp. 981-987
    • Lei, L.1    Chi, Y.2
  • 6
    • 84891025776 scopus 로고    scopus 로고
    • Ovalbumin–gum arabic interactions: effect of pH, temperature, salt, biopolymers ratio and total concentration
    • [6] Niu, F., Su, Y., Liu, Y., Wang, G., Yang, Z., Yang, Y., Ovalbumin–gum arabic interactions: effect of pH, temperature, salt, biopolymers ratio and total concentration. Colloids Surf. B Biointerfaces 113 (2014), 477–482.
    • (2014) Colloids Surf. B Biointerfaces , vol.113 , pp. 477-482
    • Niu, F.1    Su, Y.2    Liu, Y.3    Wang, G.4    Yang, Z.5    Yang, Y.6
  • 7
    • 47749152572 scopus 로고    scopus 로고
    • Biomineralizing synthesis of mesoporous hydroxyapatite–calcium pyrophosphate polycrystal using ovalbumin as biosurfactant
    • [7] Zhao, H., He, W., Wang, Y., Yue, Y., Gao, X., Li, Z., Yan, S., Zhou, W., Zhang, X., Biomineralizing synthesis of mesoporous hydroxyapatite–calcium pyrophosphate polycrystal using ovalbumin as biosurfactant. Mater. Chem. Phys. 111 (2008), 265–270.
    • (2008) Mater. Chem. Phys. , vol.111 , pp. 265-270
    • Zhao, H.1    He, W.2    Wang, Y.3    Yue, Y.4    Gao, X.5    Li, Z.6    Yan, S.7    Zhou, W.8    Zhang, X.9
  • 8
    • 0034011625 scopus 로고    scopus 로고
    • Influence of pH and CaCl 2 on the stability of dilute whey protein stabilized emulsions
    • [8] Kulmyrzaev, A., Chanamai, R., Mcclements, D.J., Influence of pH and CaCl 2 on the stability of dilute whey protein stabilized emulsions. Food Res. Int. 33 (2000), 15–20.
    • (2000) Food Res. Int. , vol.33 , pp. 15-20
    • Kulmyrzaev, A.1    Chanamai, R.2    Mcclements, D.J.3
  • 9
    • 43949119107 scopus 로고    scopus 로고
    • Ions at aqueous interfaces: from water surface to hydrated proteins
    • [9] Jungwirth, P., Winter, B., Ions at aqueous interfaces: from water surface to hydrated proteins. Annu. Rev. Phys. Chem. 59 (2008), 343–366.
    • (2008) Annu. Rev. Phys. Chem. , vol.59 , pp. 343-366
    • Jungwirth, P.1    Winter, B.2
  • 10
    • 4444246784 scopus 로고    scopus 로고
    • Improvement of functional properties of egg white protein through phosphorylation by dry-heating in the presence of pyrophosphate
    • [10] Li, C.-P., Ibrahim, H.R., Sugimoto, Y., Hatta, H., Aoki, T., Improvement of functional properties of egg white protein through phosphorylation by dry-heating in the presence of pyrophosphate. J. Agric. Food Chem. 52 (2004), 5752–5758.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 5752-5758
    • Li, C.-P.1    Ibrahim, H.R.2    Sugimoto, Y.3    Hatta, H.4    Aoki, T.5
  • 11
    • 0242299612 scopus 로고    scopus 로고
    • Phosphorylation of egg white proteins by dry-heating in the presence of phosphate
    • [11] Li, C.P., Salvador, A.S., Ibrahim, H.R., Sugimoto, Y., Aoki, T., Phosphorylation of egg white proteins by dry-heating in the presence of phosphate. J. Agric. Food Chem. 51 (2003), 6808–6815.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 6808-6815
    • Li, C.P.1    Salvador, A.S.2    Ibrahim, H.R.3    Sugimoto, Y.4    Aoki, T.5
  • 12
    • 68149142319 scopus 로고    scopus 로고
    • Glycation and phosphorylation of α-lactalbumin by dry heating: effect on protein structure and physiological functions
    • [12] Enomoto, H., Hayashi, Y., Li, C.P., Ohki, S., Ohtomo, H., Shiokawa, M., Aoki, T., Glycation and phosphorylation of α-lactalbumin by dry heating: effect on protein structure and physiological functions. J. Dairy Sci. 92 (2009), 3057–3068.
    • (2009) J. Dairy Sci. , vol.92 , pp. 3057-3068
    • Enomoto, H.1    Hayashi, Y.2    Li, C.P.3    Ohki, S.4    Ohtomo, H.5    Shiokawa, M.6    Aoki, T.7
  • 13
    • 29144447015 scopus 로고    scopus 로고
    • Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating
    • [13] Li, C.P., Enomoto, H., Ohki, S., Ohtomo, H., Aoki, T., Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating. J. Dairy Sci. 88 (2005), 4137–4145.
    • (2005) J. Dairy Sci. , vol.88 , pp. 4137-4145
    • Li, C.P.1    Enomoto, H.2    Ohki, S.3    Ohtomo, H.4    Aoki, T.5
  • 14
    • 85014449369 scopus 로고
    • Influence of the Reaction Conditions on the Chemical Phosphorylation of Milk-Proteins
    • [14] Sitohy, M., Sitohy, M., Chobert, J.M., Chobert, J.M., Haertle, T., Haertle, T., Influence of the Reaction Conditions on the Chemical Phosphorylation of Milk-Proteins. 1994.
    • (1994)
    • Sitohy, M.1    Sitohy, M.2    Chobert, J.M.3    Chobert, J.M.4    Haertle, T.5    Haertle, T.6
  • 15
    • 0025917636 scopus 로고
    • Phosphorylation of food proteins with phosphorus oxychloride—improvement of functional and nutritional properties: a review
    • [15] Matheis, G., Phosphorylation of food proteins with phosphorus oxychloride—improvement of functional and nutritional properties: a review. Food Chem. 39 (1991), 13–26.
    • (1991) Food Chem. , vol.39 , pp. 13-26
    • Matheis, G.1
  • 16
    • 34249947523 scopus 로고    scopus 로고
    • Intermolecular interactions in biomolecular systems examined by mass spectrometry
    • [16] Wyttenbach, T., Bowers, M.T., Intermolecular interactions in biomolecular systems examined by mass spectrometry. Annu. Rev. Phys. Chem. 58 (2007), 511–533.
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 511-533
    • Wyttenbach, T.1    Bowers, M.T.2
  • 17
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • [17] Bo, N., Analysis of protein glycosylation by mass spectrometry. Nat. Protoc. 2 (2007), 1585–1602.
    • (2007) Nat. Protoc. , vol.2 , pp. 1585-1602
    • Bo, N.1
  • 18
    • 84891460472 scopus 로고    scopus 로고
    • Synthesis of polydopamine-coated magnetic graphene for Cu(2+) immobilization and application to the enrichment of low-concentration peptides for mass spectrometry analysis
    • [18] Zhao, M., Deng, C., Zhang, X., Synthesis of polydopamine-coated magnetic graphene for Cu(2+) immobilization and application to the enrichment of low-concentration peptides for mass spectrometry analysis. ACS Appl. Mater. Interfaces 5 (2013), 13104–13112.
    • (2013) ACS Appl. Mater. Interfaces , vol.5 , pp. 13104-13112
    • Zhao, M.1    Deng, C.2    Zhang, X.3
  • 20
    • 84926488713 scopus 로고    scopus 로고
    • Mass spectrometry of protein complexes: from origins to applications
    • [20] Mehmood, S., Allison, T.M., Robinson, C.V., Mass spectrometry of protein complexes: from origins to applications. Annu. Rev. Phys. Chem., 66, 2015.
    • (2015) Annu. Rev. Phys. Chem. , vol.66
    • Mehmood, S.1    Allison, T.M.2    Robinson, C.V.3
  • 21
    • 75549083403 scopus 로고    scopus 로고
    • Integrative proteomic analysis of the nucleus accumbens in rhesus monkeys following cocaine self-administration
    • [21] Tannu, N.S., Howell, L.L., Hemby, S.E., Integrative proteomic analysis of the nucleus accumbens in rhesus monkeys following cocaine self-administration. Mol. Psychiatry 15 (2008), 185–203.
    • (2008) Mol. Psychiatry , vol.15 , pp. 185-203
    • Tannu, N.S.1    Howell, L.L.2    Hemby, S.E.3
  • 22
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • [22] Mann, M., Ong, S.E., Grønborg, M., Steen, H., Jensen, O.N., Pandey, A., Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20 (2002), 261–268.
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Grønborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 23
    • 59649110454 scopus 로고    scopus 로고
    • Phosphorylation of proteins by dry-heating in the presence of pyrophosphate and some characteristics of introduced phosphate groups
    • [23] Li, C.P., Hayashi, Y., Enomoto, H., Hu, F., Sawano, Y., Tanokura, M., Aoki, T., Phosphorylation of proteins by dry-heating in the presence of pyrophosphate and some characteristics of introduced phosphate groups. Food Chem. 114 (2009), 1036–1041.
    • (2009) Food Chem. , vol.114 , pp. 1036-1041
    • Li, C.P.1    Hayashi, Y.2    Enomoto, H.3    Hu, F.4    Sawano, Y.5    Tanokura, M.6    Aoki, T.7
  • 24
    • 84862181145 scopus 로고    scopus 로고
    • Co-purification of chicken egg white proteins using polyethylene glycol precipitation and anion-exchange chromatography
    • [24] Fang, G., Huang, Q., Wu, X., Ren, G., Shan, Y., Jin, G., Ma, M., Co-purification of chicken egg white proteins using polyethylene glycol precipitation and anion-exchange chromatography. Sep. Purif. Technol. 96 (2012), 75–80.
    • (2012) Sep. Purif. Technol. , vol.96 , pp. 75-80
    • Fang, G.1    Huang, Q.2    Wu, X.3    Ren, G.4    Shan, Y.5    Jin, G.6    Ma, M.7
  • 25
    • 66149106351 scopus 로고    scopus 로고
    • Sodium caseinates with an altered isoelectric point as emulsifiers in oil/water systems
    • [25] Ma, H.R., Forssell, P., Partanen, R., Seppänen, R., Buchert, J., Boer, H., Sodium caseinates with an altered isoelectric point as emulsifiers in oil/water systems. J. Agric. Food Chem. 57 (2009), 3800–3807.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3800-3807
    • Ma, H.R.1    Forssell, P.2    Partanen, R.3    Seppänen, R.4    Buchert, J.5    Boer, H.6
  • 26
    • 84908393452 scopus 로고    scopus 로고
    • Phase separation behavior and structural analysis of ovalbumin–gum arabic complex coacervation
    • [26] Niu, F., Dong, Y., Shen, F., Wang, J., Liu, Y., Su, Y., Xu, R., Wang, J., Yang, Y., Phase separation behavior and structural analysis of ovalbumin–gum arabic complex coacervation. Food Hydrocoll. 43 (2015), 1–7.
    • (2015) Food Hydrocoll. , vol.43 , pp. 1-7
    • Niu, F.1    Dong, Y.2    Shen, F.3    Wang, J.4    Liu, Y.5    Su, Y.6    Xu, R.7    Wang, J.8    Yang, Y.9
  • 27
    • 84882590818 scopus 로고    scopus 로고
    • Physical and oxidative stability of uncoated and chitosan-coated liposomes containing grape seed extract
    • [27] Gibis, M., Rahn, N., Weiss, J., Physical and oxidative stability of uncoated and chitosan-coated liposomes containing grape seed extract. Pharmaceutics 5 (2013), 421–433.
    • (2013) Pharmaceutics , vol.5 , pp. 421-433
    • Gibis, M.1    Rahn, N.2    Weiss, J.3
  • 28
    • 84904356279 scopus 로고    scopus 로고
    • The influence of thermal processing on emulsion properties of defatted hazelnut flour
    • [28] Turan, D., Altay, F., Capanoğlu, G.E., The influence of thermal processing on emulsion properties of defatted hazelnut flour. Food Chem. 167C (2015), 100–106.
    • (2015) Food Chem. , vol.167C , pp. 100-106
    • Turan, D.1    Altay, F.2    Capanoğlu, G.E.3
  • 29
    • 84962428162 scopus 로고    scopus 로고
    • Preparation of amphiphilic sorbitan monoethers through hydrogenolysis of sorbitan acetals and evaluation as bio-based surfactants
    • [29] Gozlan, C., Deruer, E., Duclos, M.C., Molinier, V., Aubry, J.M., Redl, A., Duguet, N., Lemaire, M., Preparation of amphiphilic sorbitan monoethers through hydrogenolysis of sorbitan acetals and evaluation as bio-based surfactants. Green Chem. 18 (2016), 1994–2004.
    • (2016) Green Chem. , vol.18 , pp. 1994-2004
    • Gozlan, C.1    Deruer, E.2    Duclos, M.C.3    Molinier, V.4    Aubry, J.M.5    Redl, A.6    Duguet, N.7    Lemaire, M.8
  • 31
    • 84907358981 scopus 로고    scopus 로고
    • Binding of (−)-epigallocatechin-3-gallate with thermally-induced bovine serum albumin/L-carrageenan particles
    • [31] Li, J., Wang, X., Binding of (−)-epigallocatechin-3-gallate with thermally-induced bovine serum albumin/L-carrageenan particles. Food Chem. 168C (2015), 566–571.
    • (2015) Food Chem. , vol.168C , pp. 566-571
    • Li, J.1    Wang, X.2
  • 32
    • 84971296093 scopus 로고    scopus 로고
    • Enhanced surface properties of branched polyethersulfone from semi-fluorinated polyhedral oligomeric silsequioxanes
    • [32] Knauer, K.M., Jennings, A.R., Bristol, A.N., Iacono, S.T., Morgan, S.E., Enhanced surface properties of branched polyethersulfone from semi-fluorinated polyhedral oligomeric silsequioxanes. ACS Appl. Mater. Interfaces 8 (2016), 12434–12444.
    • (2016) ACS Appl. Mater. Interfaces , vol.8 , pp. 12434-12444
    • Knauer, K.M.1    Jennings, A.R.2    Bristol, A.N.3    Iacono, S.T.4    Morgan, S.E.5
  • 33
    • 84966297159 scopus 로고    scopus 로고
    • Poly(glycidyl methacrylate-co-2-hydroxyethyl methacrylate) brushes as peptide/protein microarray substrate for improving protein binding and functionality
    • [33] Lei, Z., Gao, J., Liu, X., Liu, D., Wang, Z., Poly(glycidyl methacrylate-co-2-hydroxyethyl methacrylate) brushes as peptide/protein microarray substrate for improving protein binding and functionality. ACS Appl. Mater. Interfaces 8 (2016), 10174–10182.
    • (2016) ACS Appl. Mater. Interfaces , vol.8 , pp. 10174-10182
    • Lei, Z.1    Gao, J.2    Liu, X.3    Liu, D.4    Wang, Z.5
  • 34
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • [34] Shevchenko, A., Wilm, M., Ole Vorm, A., Mann, M., Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68 (1996), 850–858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Ole Vorm, A.3    Mann, M.4
  • 35
    • 0035431586 scopus 로고    scopus 로고
    • Simplified sample preparation method for protein identification by matrix-assisted laser desorption/ionization mass spectrometry: in-gel digestion on the probe surface
    • [35] Stensballe, A., Jensen, O.N., Simplified sample preparation method for protein identification by matrix-assisted laser desorption/ionization mass spectrometry: in-gel digestion on the probe surface. Proteomics 1 (2001), 955–966.
    • (2001) Proteomics , vol.1 , pp. 955-966
    • Stensballe, A.1    Jensen, O.N.2
  • 36
    • 0036186070 scopus 로고    scopus 로고
    • Comparison of gum arabic, modified starch, and whey protein isolate as emulsifiers: influence of pH CaCl 2 and temperature
    • [36] Chanamai, R., Mcclements, D.J., Comparison of gum arabic, modified starch, and whey protein isolate as emulsifiers: influence of pH CaCl 2 and temperature. J. Food Sci. 67 (2002), 120–125.
    • (2002) J. Food Sci. , vol.67 , pp. 120-125
    • Chanamai, R.1    Mcclements, D.J.2
  • 37
    • 4444246784 scopus 로고    scopus 로고
    • Improvement of functional properties of egg white protein through phosphorylation by dry-heating in the presence of pyrophosphate
    • [37] Li, C.P., Ibrahim, H.R., Sugimoto, Y., Hatta, H., Aoki, T., Improvement of functional properties of egg white protein through phosphorylation by dry-heating in the presence of pyrophosphate. J. Agric. Food Chem. 52 (2004), 5752–5758.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 5752-5758
    • Li, C.P.1    Ibrahim, H.R.2    Sugimoto, Y.3    Hatta, H.4    Aoki, T.5
  • 38
    • 84973480997 scopus 로고    scopus 로고
    • Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties
    • [38] Dombrowski, J., Johler, F., Warncke, M., Kulozik, U., Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties. Food Hydrocoll. 61 (2016), 318–328.
    • (2016) Food Hydrocoll. , vol.61 , pp. 318-328
    • Dombrowski, J.1    Johler, F.2    Warncke, M.3    Kulozik, U.4
  • 39
    • 84886085745 scopus 로고    scopus 로고
    • The effects of pH and high hydrostatic pressure on the physicochemical properties of a sweet potato protein emulsion
    • [39] Khan, N.M., Mu, T.H., Zhang, M., Arogundade, L.A., The effects of pH and high hydrostatic pressure on the physicochemical properties of a sweet potato protein emulsion. Int. J. Food Sci. Technol. 35 (2014), 209–216.
    • (2014) Int. J. Food Sci. Technol. , vol.35 , pp. 209-216
    • Khan, N.M.1    Mu, T.H.2    Zhang, M.3    Arogundade, L.A.4
  • 40
    • 0036040959 scopus 로고    scopus 로고
    • Effect of dispersing oil phase on the biodegradability of a solid alkane dissolved in non-biodegradable oil
    • [40] Hori, K., Matsuzaki, Y., Tanji, Y., Unno, H., Effect of dispersing oil phase on the biodegradability of a solid alkane dissolved in non-biodegradable oil. Appl. Microbiol. Biotechnol. 59 (2002), 574–579.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 574-579
    • Hori, K.1    Matsuzaki, Y.2    Tanji, Y.3    Unno, H.4
  • 41
    • 84978062658 scopus 로고    scopus 로고
    • Wheat gluten based percolating emulsion gels as simple strategy for structuring liquid oil
    • [41] Liu, X., Chen, X.W., Guo, J., Yin, S.W., Yang, X.Q., Wheat gluten based percolating emulsion gels as simple strategy for structuring liquid oil. Food Hydrocoll. 61 (2016), 747–755.
    • (2016) Food Hydrocoll. , vol.61 , pp. 747-755
    • Liu, X.1    Chen, X.W.2    Guo, J.3    Yin, S.W.4    Yang, X.Q.5
  • 42
    • 84928565712 scopus 로고    scopus 로고
    • Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate
    • [42] Ghribi, A.M., Gafsi, I.M., Sila, A., Blecker, C., Danthine, S., Attia, H., Bougatef, A., Besbes, S., Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate. Food Chem. 187 (2015), 322–330.
    • (2015) Food Chem. , vol.187 , pp. 322-330
    • Ghribi, A.M.1    Gafsi, I.M.2    Sila, A.3    Blecker, C.4    Danthine, S.5    Attia, H.6    Bougatef, A.7    Besbes, S.8
  • 43
    • 58149511931 scopus 로고    scopus 로고
    • Stabilisation of emulsions by using a combination of an oil soluble ionic surfactant and water soluble polyelectrolytes. I: emulsion stabilisation and interfacial tension measurements
    • [43] Stamkulov, N.S., Mussabekov, K.B., Aidarova, S.B., Luckham, P.F., Stabilisation of emulsions by using a combination of an oil soluble ionic surfactant and water soluble polyelectrolytes. I: emulsion stabilisation and interfacial tension measurements. Colloids Surf. A Physicochem. Eng. Asp. 335 (2009), 103–106.
    • (2009) Colloids Surf. A Physicochem. Eng. Asp. , vol.335 , pp. 103-106
    • Stamkulov, N.S.1    Mussabekov, K.B.2    Aidarova, S.B.3    Luckham, P.F.4
  • 44
    • 38049085214 scopus 로고    scopus 로고
    • Changes and roles of secondary structures of whey protein for the formation of protein membrane at soy oil/water interface under high-pressure homogenization
    • [44] Lee, S.H., Lefèvre, T., Subirade, M., Paquin, P., Changes and roles of secondary structures of whey protein for the formation of protein membrane at soy oil/water interface under high-pressure homogenization. J. Agric. Food Chem. 55 (2007), 10924–10931.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 10924-10931
    • Lee, S.H.1    Lefèvre, T.2    Subirade, M.3    Paquin, P.4
  • 45
    • 84884546453 scopus 로고    scopus 로고
    • Oil bulking agents based on polysaccharide gels in meat batters: a Raman spectroscopic study
    • [45] Ruiz-Capillas, C., Carmona, P., Jiménez-Colmenero, F., Herrero, A.M., Oil bulking agents based on polysaccharide gels in meat batters: a Raman spectroscopic study. Food Chem. 141 (2013), 3688–3694.
    • (2013) Food Chem. , vol.141 , pp. 3688-3694
    • Ruiz-Capillas, C.1    Carmona, P.2    Jiménez-Colmenero, F.3    Herrero, A.M.4
  • 46
    • 84939825841 scopus 로고    scopus 로고
    • Ovalbumin/gum arabic-stabilized emulsion: rheology, emulsion characteristics, and Raman spectroscopic study
    • [46] Niu, F., Niu, D., Zhang, H., Chang, C., Gu, L., Su, Y., Yang, Y., Ovalbumin/gum arabic-stabilized emulsion: rheology, emulsion characteristics, and Raman spectroscopic study. Food Hydrocoll. 52 (2016), 607–614.
    • (2016) Food Hydrocoll. , vol.52 , pp. 607-614
    • Niu, F.1    Niu, D.2    Zhang, H.3    Chang, C.4    Gu, L.5    Su, Y.6    Yang, Y.7
  • 47
    • 0030172681 scopus 로고    scopus 로고
    • Raman scattering studies of surfactant association (I) vibrational characteristics of micelles and liquid crystals
    • [47] Ganzuo, L., Ying, L., Lixia, L., YonHai, L., Raman scattering studies of surfactant association (I) vibrational characteristics of micelles and liquid crystals. J. Dispers. Sci. Technol. 17 (1996), 379–389.
    • (1996) J. Dispers. Sci. Technol. , vol.17 , pp. 379-389
    • Ganzuo, L.1    Ying, L.2    Lixia, L.3    YonHai, L.4
  • 48
    • 0344876470 scopus 로고    scopus 로고
    • Studies on egg albumen and whey protein interactions by FT-Raman spectroscopy and rheology
    • [48] Ngarize, S., Adams, A., Howell, N.K., Studies on egg albumen and whey protein interactions by FT-Raman spectroscopy and rheology. Food Hydrocoll. 18 (2004), 49–59.
    • (2004) Food Hydrocoll. , vol.18 , pp. 49-59
    • Ngarize, S.1    Adams, A.2    Howell, N.K.3
  • 49
    • 0034819490 scopus 로고    scopus 로고
    • Elucidation of protein-lipid interactions in a lysozyme-corn oil system by fourier transform Raman spectroscopy
    • [49] Howell, Nazlin K., Herman, Henryk, LiChan, E.C.Y., Elucidation of protein-lipid interactions in a lysozyme-corn oil system by fourier transform Raman spectroscopy. J. Agric. Food Chem. 49 (2001), 1529–1533.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1529-1533
    • Howell, N.K.1    Herman, H.2    LiChan, E.C.Y.3
  • 50
    • 84894134766 scopus 로고    scopus 로고
    • Cellulose nanowhiskers and fiber alignment greatly improve mechanical properties of electrospun prolamin protein fibers
    • [50] Wang, Y., Chen, L., Cellulose nanowhiskers and fiber alignment greatly improve mechanical properties of electrospun prolamin protein fibers. ACS Appl. Mater. Interfaces 6 (2014), 1709–1718.
    • (2014) ACS Appl. Mater. Interfaces , vol.6 , pp. 1709-1718
    • Wang, Y.1    Chen, L.2
  • 51
    • 84892847760 scopus 로고    scopus 로고
    • Contribution of Raman spectroscopy to in situ monitoring of a high-impact polystyrene process
    • [51] Brun, N., Chevrel, M.C., Falk, L., Hoppe, S., Durand, A., Chapron, D., Bourson, P., Contribution of Raman spectroscopy to in situ monitoring of a high-impact polystyrene process. Chem. Eng. Technol. 37 (2014), 275–282.
    • (2014) Chem. Eng. Technol. , vol.37 , pp. 275-282
    • Brun, N.1    Chevrel, M.C.2    Falk, L.3    Hoppe, S.4    Durand, A.5    Chapron, D.6    Bourson, P.7
  • 52
    • 18144385496 scopus 로고    scopus 로고
    • Composition of bone and apatitic biomaterials as revealed by intravital Raman microspectroscopy
    • [52] Penel, G., Delfosse, C., Descamps, M., Leroy, G., Composition of bone and apatitic biomaterials as revealed by intravital Raman microspectroscopy. Bone 36 (2005), 893–901.
    • (2005) Bone , vol.36 , pp. 893-901
    • Penel, G.1    Delfosse, C.2    Descamps, M.3    Leroy, G.4
  • 53
    • 33644875542 scopus 로고    scopus 로고
    • Chemical modification of chitosan by phosphorylation: an XPS, FT-IR and SEM study
    • [53] Amaral, I.F., Granja, P.L., Barbosa, M.A., Chemical modification of chitosan by phosphorylation: an XPS, FT-IR and SEM study. J. Biomater. Sci. Polym. Ed. 16 (2005), 1575–1593.
    • (2005) J. Biomater. Sci. Polym. Ed. , vol.16 , pp. 1575-1593
    • Amaral, I.F.1    Granja, P.L.2    Barbosa, M.A.3
  • 54
    • 84965032410 scopus 로고    scopus 로고
    • Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment
    • [54] Wang, H., Tu, Z.C., Liu, G.X., Zhang, L., Chen, Y., Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment. Food Chem. 210 (2016), 141–147.
    • (2016) Food Chem. , vol.210 , pp. 141-147
    • Wang, H.1    Tu, Z.C.2    Liu, G.X.3    Zhang, L.4    Chen, Y.5
  • 55
    • 84903183509 scopus 로고    scopus 로고
    • Probing the conformational changes of ovalbumin after glycation using HDX-MS
    • [55] Huang, X., Tu, Z., Hui, W., Zhang, Q., Yuan, C., Yan, S., Hui, X., Probing the conformational changes of ovalbumin after glycation using HDX-MS. Food Chem. 166 (2015), 62–67.
    • (2015) Food Chem. , vol.166 , pp. 62-67
    • Huang, X.1    Tu, Z.2    Hui, W.3    Zhang, Q.4    Yuan, C.5    Yan, S.6    Hui, X.7
  • 56
    • 84874893500 scopus 로고    scopus 로고
    • Increase of ovalbumin glycation by the maillard reaction after disruption of the disulfide bridge evaluated by liquid chromatography and high resolution mass spectrometry
    • [56] Huang, X., Tu, Z., Wang, H., Zhang, Q., Shi, Y., Xiao, H., Increase of ovalbumin glycation by the maillard reaction after disruption of the disulfide bridge evaluated by liquid chromatography and high resolution mass spectrometry. J. Agric. Food Chem. 61 (2013), 2253–2262.
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 2253-2262
    • Huang, X.1    Tu, Z.2    Wang, H.3    Zhang, Q.4    Shi, Y.5    Xiao, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.