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Volumn 65, Issue 6, 2017, Pages 1263-1271

Exploring the Relationship between Structural and Air-Water Interfacial Properties of Wheat (Triticum aestivum L.) Gluten Hydrolysates in a Food System Relevant pH Range

Author keywords

air water interface; foam; gluten hydrolysates; interfacial properties; pH; protein conformation

Indexed keywords

AIR; FOAMS; HYDROLYSIS; PH; PROTEINS;

EID: 85013037398     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.6b05062     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 34548822143 scopus 로고    scopus 로고
    • Stabilization of bubbles and foams
    • Murray, B. S. Stabilization of bubbles and foams Curr. Opin. Colloid Interface Sci. 2007, 12, 232-241 10.1016/j.cocis.2007.07.009
    • (2007) Curr. Opin. Colloid Interface Sci. , vol.12 , pp. 232-241
    • Murray, B.S.1
  • 2
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S. Protein stabilization of emulsions and foams J. Food Sci. 2005, 70, R54-R66 10.1111/j.1365-2621.2005.tb07150.x
    • (2005) J. Food Sci. , vol.70 , pp. R54-R66
    • Damodaran, S.1
  • 5
    • 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. 2005, 41, 221-237 10.1016/j.jcs.2004.09.008
    • (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
  • 8
    • 0017024705 scopus 로고
    • Enzymatic hydrolysis of proteins for increased solubility
    • Adler-Nissen, J. Enzymatic hydrolysis of proteins for increased solubility J. Agric. Food Chem. 1976, 24, 1090-1093 10.1021/jf60208a021
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 1090-1093
    • Adler-Nissen, J.1
  • 9
    • 84992305648 scopus 로고    scopus 로고
    • Relevance of the functional properties of enzymatic plant protein hydrolysates in food systems
    • Wouters, A. G. B.; Rombouts, I.; Fierens, E.; Brijs, K.; Delcour, J. A. Relevance of the functional properties of enzymatic plant protein hydrolysates in food systems Compr. Rev. Food Sci. Food Saf. 2016, 15, 786-800 10.1111/1541-4337.12209
    • (2016) Compr. Rev. Food Sci. Food Saf. , vol.15 , pp. 786-800
    • Wouters, A.G.B.1    Rombouts, I.2    Fierens, E.3    Brijs, K.4    Delcour, J.A.5
  • 11
    • 75749122983 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate
    • Jamdar, S. N.; Rajalakshmi, V.; Pednekar, M. D.; Juan, F.; Yardi, V.; Sharma, A. Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate Food Chem. 2010, 121, 178-184 10.1016/j.foodchem.2009.12.027
    • (2010) Food Chem. , vol.121 , pp. 178-184
    • Jamdar, S.N.1    Rajalakshmi, V.2    Pednekar, M.D.3    Juan, F.4    Yardi, V.5    Sharma, A.6
  • 12
    • 38949138414 scopus 로고    scopus 로고
    • Foaming properties of barley protein isolates and hydrolysates
    • Yalcin, E.; Celik, S.; Ibanoglu, E. Foaming properties of barley protein isolates and hydrolysates Eur. Food Res. Technol. 2008, 226, 967-974 10.1007/s00217-007-0618-8
    • (2008) Eur. Food Res. Technol. , vol.226 , pp. 967-974
    • Yalcin, E.1    Celik, S.2    Ibanoglu, E.3
  • 13
    • 0036314589 scopus 로고    scopus 로고
    • Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration
    • Popineau, Y.; Huchet, B.; Larre, C.; Berot, S. Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration J. Cereal Sci. 2002, 35, 327-335 10.1006/jcrs.2001.0437
    • (2002) J. Cereal Sci. , vol.35 , pp. 327-335
    • Popineau, Y.1    Huchet, B.2    Larre, C.3    Berot, S.4
  • 14
    • 0034370011 scopus 로고    scopus 로고
    • Foaming properties of enzymatically hydrolysed wheat gluten
    • Drago, S. R.; González, R. J. Foaming properties of enzymatically hydrolysed wheat gluten Innovative Food Sci. Emerging Technol. 2000, 1, 269-273 10.1016/S1466-8564(00)00034-5
    • (2000) Innovative Food Sci. Emerging Technol. , vol.1 , pp. 269-273
    • Drago, S.R.1    González, R.J.2
  • 15
    • 44349101790 scopus 로고    scopus 로고
    • Preparation and characterization of modified wheat gluten by enzymatic hydrolysis-ultrafiltration
    • Wang, J. S.; Zhao, M. M.; Bao, Y.; Hong, T.; Rosella, C. M. Preparation and characterization of modified wheat gluten by enzymatic hydrolysis-ultrafiltration J. Food Biochem. 2008, 32, 316-334 10.1111/j.1745-4514.2008.00157.x
    • (2008) J. Food Biochem. , vol.32 , pp. 316-334
    • Wang, J.S.1    Zhao, M.M.2    Bao, Y.3    Hong, T.4    Rosella, C.M.5
  • 16
    • 84905589954 scopus 로고    scopus 로고
    • Structural and functional properties of hemp seed protein products
    • Malomo, S. A.; He, R.; Aluko, R. E. Structural and functional properties of hemp seed protein products J. Food Sci. 2014, 79, C1512-C1521 10.1111/1750-3841.12537
    • (2014) J. Food Sci. , vol.79 , pp. C1512-C1521
    • Malomo, S.A.1    He, R.2    Aluko, R.E.3
  • 17
    • 84929578956 scopus 로고    scopus 로고
    • Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer
    • Jarpa-Parra, M.; Bamdad, F.; Tian, Z.; Zeng, H. B.; Temelli, F.; Chen, L. Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer Colloids Surf., B 2015, 132, 45-53 10.1016/j.colsurfb.2015.04.065
    • (2015) Colloids Surf., B , vol.132 , pp. 45-53
    • Jarpa-Parra, M.1    Bamdad, F.2    Tian, Z.3    Zeng, H.B.4    Temelli, F.5    Chen, L.6
  • 19
    • 79955604476 scopus 로고    scopus 로고
    • Foaming properties of tryptic gliadin hydrolysate peptide fractions
    • Thewissen, B. G.; Celus, I.; Brijs, K.; Delcour, J. A. Foaming properties of tryptic gliadin hydrolysate peptide fractions Food Chem. 2011, 128, 606-612 10.1016/j.foodchem.2011.03.007
    • (2011) Food Chem. , vol.128 , pp. 606-612
    • Thewissen, B.G.1    Celus, I.2    Brijs, K.3    Delcour, J.A.4
  • 20
    • 0006544980 scopus 로고
    • AOAC. Association of Official Analytical Chemists: Washington, DC, USA, Method 990.03
    • AOAC. Official Methods of Analysis; Association of Official Analytical Chemists: Washington, DC, USA, 1995; Method 990.03.
    • (1995) Official Methods of Analysis
  • 22
    • 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. 1990, 190, 516-520 10.1007/BF01214073
    • (1990) Z. Lebensm.-Unters. Forsch. , vol.190 , pp. 516-520
    • Diermayr, P.1    Dehne, L.2
  • 23
    • 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. 2001, 66, 642-646 10.1111/j.1365-2621.2001.tb04614.x
    • (2001) J. Food Sci. , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 24
    • 0000050670 scopus 로고    scopus 로고
    • Plasmin hydrolysis of beta-casein: Foaming and emulsifying properties of the fractionated hydrolysate
    • Caessens, P. W. J. R.; Gruppen, H.; Visser, S.; van Aken, G. A.; Voragen, A. G. J. Plasmin hydrolysis of beta-casein: foaming and emulsifying properties of the fractionated hydrolysate J. Agric. Food Chem. 1997, 45, 2935-2941 10.1021/jf9700889
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2935-2941
    • Caessens, P.W.J.R.1    Gruppen, H.2    Visser, S.3    Van Aken, G.A.4    Voragen, A.G.J.5
  • 25
    • 78751706080 scopus 로고    scopus 로고
    • Rheological properties of protein films
    • Murray, B. S. Rheological properties of protein films Curr. Opin. Colloid Interface Sci. 2011, 16, 27-35 10.1016/j.cocis.2010.06.005
    • (2011) Curr. Opin. Colloid Interface Sci. , vol.16 , pp. 27-35
    • Murray, B.S.1
  • 26
    • 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 2016, 55, 155-162 10.1016/j.foodhyd.2015.11.017
    • (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
  • 27
    • 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, Proteins Proteomics 2007, 1774, 403-411 10.1016/j.bbapap.2007.01.002
    • (2007) Biochim. Biophys. Acta, Proteins Proteomics , vol.1774 , pp. 403-411
    • Gasymov, O.K.1    Glasgow, B.J.2
  • 28
    • 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. 2000, 48, 328-334 10.1021/jf990393p
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 30
    • 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. 2014, 15, 22518-22538 10.3390/ijms151222518
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 22518-22538
    • Ghisaidoobe, A.1    Chung, S.2
  • 31
    • 67649243772 scopus 로고    scopus 로고
    • β-Lactoglobulin aggregates in foam films: Correlation between foam films and foaming properties
    • Rullier, B.; Axelos, M. A. V.; Langevin, D.; Novales, B. β-Lactoglobulin aggregates in foam films: correlation between foam films and foaming properties J. Colloid Interface Sci. 2009, 336, 750-755 10.1016/j.jcis.2009.04.034
    • (2009) J. Colloid Interface Sci. , vol.336 , pp. 750-755
    • Rullier, B.1    Axelos, M.A.V.2    Langevin, D.3    Novales, B.4
  • 32
    • 54149089640 scopus 로고    scopus 로고
    • Effect of protein aggregates on foaming properties of β-lactoglobulin
    • Rullier, B.; Novales, B.; Axelos, M. A. V. Effect of protein aggregates on foaming properties of β-lactoglobulin Colloids Surf., A 2008, 330, 96-102 10.1016/j.colsurfa.2008.07.040
    • (2008) Colloids Surf., A , vol.330 , pp. 96-102
    • Rullier, B.1    Novales, B.2    Axelos, M.A.V.3
  • 33
    • 84901250363 scopus 로고    scopus 로고
    • Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0
    • Liang, H.-N.; Tang, C.-h. Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0 LWT-Food Sci. Technol. 2014, 58, 463-469 10.1016/j.lwt.2014.03.023
    • (2014) LWT-Food Sci. Technol. , vol.58 , pp. 463-469
    • Liang, H.-N.1    Tang, C.-H.2
  • 34
    • 84929179343 scopus 로고    scopus 로고
    • Foaming characteristics of commercial soy protein isolate as influenced by heat-induced aggregation
    • He, Z. Y.; Li, W. W.; Guo, F. X.; Li, W. Y.; Zeng, M. M.; Chen, J. Foaming characteristics of commercial soy protein isolate as influenced by heat-induced aggregation Int. J. Food Prop. 2015, 18, 1817-1828 10.1080/10942912.2014.946046
    • (2015) Int. J. Food Prop. , vol.18 , pp. 1817-1828
    • He, Z.Y.1    Li, W.W.2    Guo, F.X.3    Li, W.Y.4    Zeng, M.M.5    Chen, J.6
  • 37
    • 0036267602 scopus 로고    scopus 로고
    • Particles as surfactants - Similarities and differences
    • Binks, B. P. Particles as surfactants-similarities and differences Curr. Opin. Colloid Interface Sci. 2002, 7, 21-41 10.1016/S1359-0294(02)00008-0
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 21-41
    • Binks, B.P.1
  • 38
    • 84989810308 scopus 로고    scopus 로고
    • Recent advances on food-grade particles stabilized Pickering emulsions: Fabrication, characterization and research trends
    • Xiao, J.; Li, Y.; Huang, Q. Recent advances on food-grade particles stabilized Pickering emulsions: fabrication, characterization and research trends Trends Food Sci. Technol. 2016, 55, 48-60 10.1016/j.tifs.2016.05.010
    • (2016) Trends Food Sci. Technol. , vol.55 , pp. 48-60
    • Xiao, J.1    Li, Y.2    Huang, Q.3
  • 39
    • 84914665340 scopus 로고    scopus 로고
    • Pickering stabilization of foams and emulsions with particles of biological origin
    • Lam, S.; Velikov, K. P.; Velev, O. D. Pickering stabilization of foams and emulsions with particles of biological origin Curr. Opin. Colloid Interface Sci. 2014, 19, 490-500 10.1016/j.cocis.2014.07.003
    • (2014) Curr. Opin. Colloid Interface Sci. , vol.19 , pp. 490-500
    • Lam, S.1    Velikov, K.P.2    Velev, O.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.