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Volumn 529, Issue , 2017, Pages 659-667

Impact of ethanol on the air-water interfacial properties of enzymatically hydrolyzed wheat gluten

Author keywords

Air water interfacial properties; Ethanol; Foam; Gluten; Hydrolysates

Indexed keywords

AIR; ETHANOL; FOAMS; FOOD PRODUCTS; HYDROLYSIS; PROTEINS;

EID: 85021261041     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2017.06.013     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 84879883569 scopus 로고    scopus 로고
    • Proteins from land plants −potential resources for human nutrition and food security
    • Day, L., Proteins from land plants −potential resources for human nutrition and food security. Trends Food Sci. Technol. 32 (2013), 25–42.
    • (2013) Trends Food Sci. Technol. , vol.32 , pp. 25-42
    • Day, L.1
  • 3
    • 15744378146 scopus 로고    scopus 로고
    • Fractionation of wheat and wheat flour into starch and gluten: overview of the main processes and the factors involved
    • Van Der Borght, A., Goesaert, H., Veraverbeke, W.S., Delcour, J.A., Fractionation of wheat and wheat flour into starch and gluten: overview of the main processes and the factors involved. J. Cereal Sci. 41 (2005), 221–237.
    • (2005) J. Cereal Sci. , vol.41 , pp. 221-237
    • Van Der Borght, A.1    Goesaert, H.2    Veraverbeke, W.S.3    Delcour, J.A.4
  • 5
    • 0029999609 scopus 로고    scopus 로고
    • Biopolymers – giant proteins with flour power
    • Wrigley, C.W., Biopolymers – giant proteins with flour power. Nature 381 (1996), 738–739.
    • (1996) Nature , vol.381 , pp. 738-739
    • Wrigley, C.W.1
  • 6
    • 0017024705 scopus 로고
    • Enzymatic hydrolysis of proteins for increased solubility
    • Adler-Nissen, J., Enzymatic hydrolysis of proteins for increased solubility. J. Agric. Food Chem. 24 (1976), 1090–1093.
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 1090-1093
    • Adler-Nissen, J.1
  • 7
    • 84947928397 scopus 로고    scopus 로고
    • Air-water interfacial properties of enzymatic wheat gluten hydrolyzates determine their foaming behavior
    • Wouters, A.G.B., Rombouts, I., Legein, M., Fierens, E., Brijs, K., Blecker, C., Delcour, J.A., Air-water interfacial properties of enzymatic wheat gluten hydrolyzates determine their foaming behavior. Food Hydrocolloids 55 (2016), 155–162.
    • (2016) Food Hydrocolloids , vol.55 , pp. 155-162
    • Wouters, A.G.B.1    Rombouts, I.2    Legein, M.3    Fierens, E.4    Brijs, K.5    Blecker, C.6    Delcour, J.A.7
  • 8
    • 25844500998 scopus 로고    scopus 로고
    • Factors determining the physical properties of protein foams
    • Foegeding, E.A., Luck, P.J., Davis, J.P., Factors determining the physical properties of protein foams. Food Hydrocolloids 20 (2006), 284–292.
    • (2006) Food Hydrocolloids , vol.20 , pp. 284-292
    • Foegeding, E.A.1    Luck, P.J.2    Davis, J.P.3
  • 9
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S., Protein stabilization of emulsions and foams. J. Food Sci. 70 (2005), R54–R66.
    • (2005) J. Food Sci. , vol.70 , pp. R54-R66
    • Damodaran, S.1
  • 12
    • 0036867705 scopus 로고    scopus 로고
    • Interfacial rheology of food emulsifiers and proteins
    • Murray, B.S., Interfacial rheology of food emulsifiers and proteins. Curr. Opin. Colloid Interface Sci. 7 (2002), 426–431.
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 426-431
    • Murray, B.S.1
  • 13
    • 78751706080 scopus 로고    scopus 로고
    • Rheological properties of protein films
    • Murray, B.S., Rheological properties of protein films. Curr. Opin. Colloid Interface Sci. 16 (2011), 27–35.
    • (2011) Curr. Opin. Colloid Interface Sci. , vol.16 , pp. 27-35
    • Murray, B.S.1
  • 15
    • 84989830782 scopus 로고    scopus 로고
    • Corrigendum to air-water interfacial properties of enzymatic wheat gluten hydrolyzates determine their foaming behavior [food hydrocoll. 55c (2016) 155–162]
    • Wouters, A.G.B., Rombouts, I., Legein, M., Fierens, E., Brijs, K., Blecker, C., Delcour, J.A., Corrigendum to air-water interfacial properties of enzymatic wheat gluten hydrolyzates determine their foaming behavior [food hydrocoll. 55c (2016) 155–162]. Food Hydrocolloids 61 (2016), 956–957.
    • (2016) Food Hydrocolloids , vol.61 , pp. 956-957
    • Wouters, A.G.B.1    Rombouts, I.2    Legein, M.3    Fierens, E.4    Brijs, K.5    Blecker, C.6    Delcour, J.A.7
  • 17
    • 0036731234 scopus 로고    scopus 로고
    • Modulation of globular protein functionality by weakly interacting cosolvents
    • McClements, D.J., Modulation of globular protein functionality by weakly interacting cosolvents. Crit. Rev. Food Sci. Nutr. 42 (2002), 417–471.
    • (2002) Crit. Rev. Food Sci. Nutr. , vol.42 , pp. 417-471
    • McClements, D.J.1
  • 19
    • 84862127163 scopus 로고    scopus 로고
    • Density, viscosity, and surface tension of water+ethanol mixtures from 293 to 323k
    • Khattab, I.S., Bandarkar, F., Fakhree, M.A.A., Jouyban, A., Density, viscosity, and surface tension of water+ethanol mixtures from 293 to 323k. Korean J. Chem. Eng. 29 (2012), 812–817.
    • (2012) Korean J. Chem. Eng. , vol.29 , pp. 812-817
    • Khattab, I.S.1    Bandarkar, F.2    Fakhree, M.A.A.3    Jouyban, A.4
  • 20
    • 0031374169 scopus 로고    scopus 로고
    • Molecular diffusion and drainage of thin liquid films stabilized by bovine serum albumin tween 20 mixtures in aqueous solutions of ethanol and sucrose
    • Wilde, P.J., Nino, M.R.R., Clark, D.C., Patino, J.M.R., Molecular diffusion and drainage of thin liquid films stabilized by bovine serum albumin tween 20 mixtures in aqueous solutions of ethanol and sucrose. Langmuir 13 (1997), 7151–7157.
    • (1997) Langmuir , vol.13 , pp. 7151-7157
    • Wilde, P.J.1    Nino, M.R.R.2    Clark, D.C.3    Patino, J.M.R.4
  • 22
    • 0025460569 scopus 로고
    • Effect of ethanol on the foaming of aqueous protein solutions
    • Ahmed, M., Dickinson, E., Effect of ethanol on the foaming of aqueous protein solutions. Colloids Surf. 47 (1990), 353–365.
    • (1990) Colloids Surf. , vol.47 , pp. 353-365
    • Ahmed, M.1    Dickinson, E.2
  • 23
    • 0037139161 scopus 로고    scopus 로고
    • Effect of the aqueous phase composition on the adsorption of bovine serum albumin to the air-water interface
    • Rodríguez Niño, M.R., Rodríguez Patino, J.M., Effect of the aqueous phase composition on the adsorption of bovine serum albumin to the air-water interface. Ind. Eng. Chem. Res. 41 (2002), 1489–1495.
    • (2002) Ind. Eng. Chem. Res. , vol.41 , pp. 1489-1495
    • Rodríguez Niño, M.R.1    Rodríguez Patino, J.M.2
  • 24
    • 0642316706 scopus 로고    scopus 로고
    • Rheokinetic analysis of protein films at the air-aqueous phase interface. 1. Bovine serum albumin adsorption on ethanol aqueous solutions
    • Rodríguez Niño, M.R., Wilde, P.J., Clark, D.C., Husband, F.A., Rodríguez Patino, J.M., Rheokinetic analysis of protein films at the air-aqueous phase interface. 1. Bovine serum albumin adsorption on ethanol aqueous solutions. J. Agric. Food Chem. 45 (1997), 3010–3015.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3010-3015
    • Rodríguez Niño, M.R.1    Wilde, P.J.2    Clark, D.C.3    Husband, F.A.4    Rodríguez Patino, J.M.5
  • 25
    • 0004081112 scopus 로고
    • Official Methods of Analysis. Method 990.03
    • Association of Official Analytical Chemists Washington, DC, USA
    • AOAC, Official Methods of Analysis. Method 990.03. 1995, Association of Official Analytical Chemists, Washington, DC, USA.
    • (1995)
    • AOAC1
  • 26
    • 0003737812 scopus 로고
    • Enzymic Hydrolysis of Food Proteins
    • Elsevier Applied Science Publishers New York, USA
    • Adler-Nissen, J., Enzymic Hydrolysis of Food Proteins. 1985, Elsevier Applied Science Publishers, New York, USA.
    • (1985)
    • Adler-Nissen, J.1
  • 27
    • 0025440874 scopus 로고
    • Controlled enzymatic hydrolysis of proteins at low ph values.1. Experiments with bovine serum-albumin
    • Diermayr, P., Dehne, L., Controlled enzymatic hydrolysis of proteins at low ph values.1. Experiments with bovine serum-albumin. Z. Lebensm. Unters. Forsch. 190 (1990), 516–520.
    • (1990) Z. Lebensm. Unters. Forsch. , vol.190 , pp. 516-520
    • Diermayr, P.1    Dehne, L.2
  • 28
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen, P.M., Petersen, D., Dambmann, C., Improved method for determining food protein degree of hydrolysis. J. Food Sci. 66 (2001), 642–646.
    • (2001) J. Food Sci. , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 30
    • 0001889833 scopus 로고
    • Interfacial viscoelasticity in emulsions and foams
    • Lucassen-Reynders, E.H., Wasan, D.T., Interfacial viscoelasticity in emulsions and foams. Food Struct. 12 (1993), 1–12.
    • (1993) Food Struct. , vol.12 , pp. 1-12
    • Lucassen-Reynders, E.H.1    Wasan, D.T.2
  • 31
    • 84979523597 scopus 로고    scopus 로고
    • Amyloid-like aggregation of ovalbumin: effect of disulfide reduction and other egg white proteins
    • Jansens, K.J.A., Brijs, K., Delcour, J.A., Scanlon, M.G., Amyloid-like aggregation of ovalbumin: effect of disulfide reduction and other egg white proteins. Food Hydrocolloids 61 (2016), 914–922.
    • (2016) Food Hydrocolloids , vol.61 , pp. 914-922
    • Jansens, K.J.A.1    Brijs, K.2    Delcour, J.A.3    Scanlon, M.G.4
  • 32
    • 85013037398 scopus 로고    scopus 로고
    • Exploring the relationship between structural and air-water interfacial properties of wheat (triticum aestivum l.) gluten hydrolysates in a food system relevant ph range
    • Wouters, A.G.B., Fierens, E., Rombouts, I., Brijs, K., Joye, I.J., Delcour, J.A., Exploring the relationship between structural and air-water interfacial properties of wheat (triticum aestivum l.) gluten hydrolysates in a food system relevant ph range. J. Agric. Food Chem. 65 (2017), 1263–1271.
    • (2017) J. Agric. Food Chem. , vol.65 , pp. 1263-1271
    • Wouters, A.G.B.1    Fierens, E.2    Rombouts, I.3    Brijs, K.4    Joye, I.J.5    Delcour, J.A.6
  • 33
    • 79961031305 scopus 로고    scopus 로고
    • Food protein functionality: a comprehensive approach
    • Foegeding, E.A., Davis, J.P., Food protein functionality: a comprehensive approach. Food Hydrocolloids 25 (2011), 1853–1864.
    • (2011) Food Hydrocolloids , vol.25 , pp. 1853-1864
    • Foegeding, E.A.1    Davis, J.P.2
  • 34
    • 0002123958 scopus 로고
    • Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: concentration dependence, mass-transfer considerations, and adsorption kinetics
    • Tripp, B.C., Magda, J.J., Andrade, J.D., Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: concentration dependence, mass-transfer considerations, and adsorption kinetics. J. Colloid Interface Sci. 173 (1995), 16–27.
    • (1995) J. Colloid Interface Sci. , vol.173 , pp. 16-27
    • Tripp, B.C.1    Magda, J.J.2    Andrade, J.D.3
  • 35
    • 84956640138 scopus 로고    scopus 로고
    • Denaturation and covalent network formation of wheat gluten, globular proteins and mixtures thereof in aqueous ethanol and water
    • Lambrecht, M.A., Rombouts, I., Delcour, J.A., Denaturation and covalent network formation of wheat gluten, globular proteins and mixtures thereof in aqueous ethanol and water. Food Hydrocolloids 57 (2016), 122–131.
    • (2016) Food Hydrocolloids , vol.57 , pp. 122-131
    • Lambrecht, M.A.1    Rombouts, I.2    Delcour, J.A.3
  • 36
    • 78650656384 scopus 로고    scopus 로고
    • Counter effect of sucrose on ethanol-induced aggregation of protein
    • Yadav, J.K., Chandani, N., Prajakt, P.R.P., Chauhan, J.B., Counter effect of sucrose on ethanol-induced aggregation of protein. Protein Pept. Lett. 17 (2010), 1542–1546.
    • (2010) Protein Pept. Lett. , vol.17 , pp. 1542-1546
    • Yadav, J.K.1    Chandani, N.2    Prajakt, P.R.P.3    Chauhan, J.B.4
  • 37
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various ph values using three different fluorescent probes
    • Alizadeh-Pasdar, N., Li-Chan, E.C.Y., Comparison of protein surface hydrophobicity measured at various ph values using three different fluorescent probes. J. Agric. Food Chem. 48 (2000), 328–334.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 38
    • 33847659962 scopus 로고    scopus 로고
    • Ans fluorescence: potential to augment the identification of the external binding sites of proteins
    • Gasymov, O.K., Glasgow, B.J., Ans fluorescence: potential to augment the identification of the external binding sites of proteins. Biochim. Biophys. Acta 1774 (2007), 403–411.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 403-411
    • Gasymov, O.K.1    Glasgow, B.J.2
  • 39
    • 84937605198 scopus 로고    scopus 로고
    • Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on förster resonance energy transfer techniques
    • Ghisaidoobe, A., Chung, S., Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on förster resonance energy transfer techniques. Int. J. Mol. Sci. 15 (2014), 22518–22538.
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 22518-22538
    • Ghisaidoobe, A.1    Chung, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.