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Volumn 61, Issue 24, 2013, Pages 5706-5714

Effect of the structural features of hydrochloric acid-deamidated wheat gluten on its susceptibility to enzymatic hydrolysis

Author keywords

Fourier transform infrared spectroscopy (FTIR); hydrochloric acid deamidation; Raman spectra; scanning electron microscope (SEM); susceptibility; wheat gluten

Indexed keywords

DISULFIDE BONDS; FT-IR SPECTRUM; HYDROLYSIS DEGREE; NITROGEN SOLUBILITY; STRUCTURAL FEATURE; SULFHYDRYL GROUPS; UNIFORM PORE; WHEAT GLUTEN;

EID: 84879378668     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf400281v     Document Type: Article
Times cited : (38)

References (30)
  • 2
    • 73349103194 scopus 로고    scopus 로고
    • Effect of acetic acid deamidation-induced modification in functional and nutritional properties and conformation of wheat gluten
    • Liao, L.; Zhao, M. M.; Ren, J. Y.; Zhao, H. F.; Cui, C.; Hu, X. Effect of acetic acid deamidation-induced modification in functional and nutritional properties and conformation of wheat gluten J. Sci. Food Agric. 2009, 90, 409-417
    • (2009) J. Sci. Food Agric. , vol.90 , pp. 409-417
    • Liao, L.1    Zhao, M.M.2    Ren, J.Y.3    Zhao, H.F.4    Cui, C.5    Hu, X.6
  • 3
    • 0036010140 scopus 로고    scopus 로고
    • Cereal seed storage proteins: Structures, properties and role in grain utilization
    • Peter, R.; Nigel, G. Cereal seed storage proteins: structures, properties and role in grain utilization J. Exp. Bot. 2002, 53, 947-958
    • (2002) J. Exp. Bot. , vol.53 , pp. 947-958
    • Peter, R.1    Nigel, G.2
  • 4
    • 78649631576 scopus 로고    scopus 로고
    • Susceptibility of wheat gluten to enzymatic hydrolysis following deamidation with acetic acid and sensory characteristics of the resultant hydrolysates
    • Liao, L.; Qiu, C. Y.; Liu, T. X.; Zhao, M. M.; Ren, J. Y.; Zhao, H. F. Susceptibility of wheat gluten to enzymatic hydrolysis following deamidation with acetic acid and sensory characteristics of the resultant hydrolysates J. Cereal Sci. 2010, 52, 395-403
    • (2010) J. Cereal Sci. , vol.52 , pp. 395-403
    • Liao, L.1    Qiu, C.Y.2    Liu, T.X.3    Zhao, M.M.4    Ren, J.Y.5    Zhao, H.F.6
  • 5
    • 68949214303 scopus 로고    scopus 로고
    • Characteristics of enzymatic hydrolysis of thermal-treatedwheat gluten
    • Wang, J. S.; Wei, Z. Y.; Lu, L.; Bian, K.; Zhao, M. M. Characteristics of enzymatic hydrolysis of thermal-treatedwheat gluten J. Cereal Sci. 2009, 50, 205-209
    • (2009) J. Cereal Sci. , vol.50 , pp. 205-209
    • Wang, J.S.1    Wei, Z.Y.2    Lu, L.3    Bian, K.4    Zhao, M.M.5
  • 6
    • 1542304014 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates
    • Hrckova, M.; Rusnakova, M.; Zemanovic, J. Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates Czech J. Food Sci. 2002, 2, 7-14
    • (2002) Czech J. Food Sci. , vol.2 , pp. 7-14
    • Hrckova, M.1    Rusnakova, M.2    Zemanovic, J.3
  • 8
    • 0015341416 scopus 로고
    • Preparation and isolation of acid-catalyzed hydrolysates from wheat gluten
    • Aranyi, C.; Hawrylewicz, E. J. Preparation and isolation of acid-catalyzed hydrolysates from wheat gluten J. Agric. Food Chem. 1972, 20, 670-675
    • (1972) J. Agric. Food Chem. , vol.20 , pp. 670-675
    • Aranyi, C.1    Hawrylewicz, E.J.2
  • 9
    • 0032850080 scopus 로고    scopus 로고
    • Acid modification of proteins from soymilk residue (okara)
    • Chan, W. M.; Ma, C. Y. Acid modification of proteins from soymilk residue (okara) Food Res. Int. 1999, 32, 119-127
    • (1999) Food Res. Int. , vol.32 , pp. 119-127
    • Chan, W.M.1    Ma, C.Y.2
  • 10
    • 0001407358 scopus 로고
    • Conformational changes and functional properties of acid-modified soy protein
    • Matsudomi, N.; Sasaki, T.; Kato, A.; Kobayashi, K. Conformational changes and functional properties of acid-modified soy protein J. Agric. Biol. Chem. 1985, 49, 1251-1256
    • (1985) J. Agric. Biol. Chem. , vol.49 , pp. 1251-1256
    • Matsudomi, N.1    Sasaki, T.2    Kato, A.3    Kobayashi, K.4
  • 11
    • 0016958589 scopus 로고
    • Preparation and properties of acidsolubilized gluten conformation
    • Wu, C. H.; Nakai, S.; Powrie, W. D. Preparation and properties of acidsolubilized gluten conformation J. Agric. Food Chem. 1976, 24, 504-510
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 504-510
    • Wu, C.H.1    Nakai, S.2    Powrie, W.D.3
  • 12
    • 0001149620 scopus 로고    scopus 로고
    • Chemical and sensory characterization of hydrolyzed vegetable protein, a savory flavoring
    • Aaslyng, M. D.; Martens, M.; Poll, L.; Nielsen, P. M.; Flyge, H.; Larsen, L. M. Chemical and sensory characterization of hydrolyzed vegetable protein, a savory flavoring J. Agric. Food Chem. 1998, 46, 481-489
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 481-489
    • Aaslyng, M.D.1    Martens, M.2    Poll, L.3    Nielsen, P.M.4    Flyge, H.5    Larsen, L.M.6
  • 13
    • 77952581632 scopus 로고    scopus 로고
    • Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid
    • Liao, L.; Liu, T. X; Zhao, M. M.; Cui, C.; Yuan, B. E.; Tang, S. Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid Food Chem. 2010, 123, 123-130
    • (2010) Food Chem. , vol.123 , pp. 123-130
    • Liao, L.1    Liu, T.X.2    Zhao, M.M.3    Cui, C.4    Yuan, B.E.5    Tang, S.6
  • 14
    • 84861964943 scopus 로고    scopus 로고
    • Investigation of the susceptibility of acid-deamidated wheat gluten to in vitro enzymatic hydrolysis using Raman spectra and free amino acid analysis
    • Liao, L.; Wang, Q.; Zhao, M. M. Investigation of the susceptibility of acid-deamidated wheat gluten to in vitro enzymatic hydrolysis using Raman spectra and free amino acid analysis J. Agric. Food Chem. 2012, 92, 1865-1873
    • (2012) J. Agric. Food Chem. , vol.92 , pp. 1865-1873
    • Liao, L.1    Wang, Q.2    Zhao, M.M.3
  • 15
    • 33748323487 scopus 로고    scopus 로고
    • Enzymatic preparation and functional properties of wheat gluten hydrolysates
    • Kong, X.; Zhou, H.; Qian, H. Enzymatic preparation and functional properties of wheat gluten hydrolysates Food Chem. 2007, 101, 615-620
    • (2007) Food Chem. , vol.101 , pp. 615-620
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 16
    • 68949214303 scopus 로고    scopus 로고
    • Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten
    • Wang, J. S.; Wei, Z. Y.; Li, L.; Bian, K.; Zhao, M. M. Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten J. Cereal Sci. 2009, 50, 205-209
    • (2009) J. Cereal Sci. , vol.50 , pp. 205-209
    • Wang, J.S.1    Wei, Z.Y.2    Li, L.3    Bian, K.4    Zhao, M.M.5
  • 17
    • 0001617099 scopus 로고
    • Evalution of the enzymatic suscepibility of cellulosic substrates using speific hydrolysis rates and enzyme adsorption
    • Lee, D.; Yu, A. H. C.; Wong, K. K. Y.; Saddler, J. N. Evalution of the enzymatic suscepibility of cellulosic substrates using speific hydrolysis rates and enzyme adsorption Appl. Biochem. Biotechnol. 1994, 45, 407-415
    • (1994) Appl. Biochem. Biotechnol. , vol.45 , pp. 407-415
    • Lee, D.1    Yu, A.H.C.2    Wong, K.K.Y.3    Saddler, J.N.4
  • 18
    • 0026792738 scopus 로고
    • Comparison of pretreament methods on the basis of available surface area
    • Thompson, D. N.; Chen, H. C.; Grethlein, H. E. Comparison of pretreament methods on the basis of available surface area Bioresour. Technol. 1992, 39, 155-163
    • (1992) Bioresour. Technol. , vol.39 , pp. 155-163
    • Thompson, D.N.1    Chen, H.C.2    Grethlein, H.E.3
  • 19
    • 52449144865 scopus 로고
    • Effect of structural and physico-chemical features of cellulosic substrates on the efficiency of enzymatic hydrolysis
    • Sinitsyn, A. P.; Gusakov, A. V.; Vlasenko, E. Y.. Effect of structural and physico-chemical features of cellulosic substrates on the efficiency of enzymatic hydrolysis Appl. Biochem. Biotechnol. 1991, 1, 43-59
    • (1991) Appl. Biochem. Biotechnol. , vol.1 , pp. 43-59
    • Sinitsyn, A.P.1    Gusakov, A.V.2    Vlasenko, E.Y.3
  • 21
    • 53949124105 scopus 로고    scopus 로고
    • Raman spectroscopic study of deamidated food proteins
    • Wong, H. W.; Mei, S. C.; Phillips, D. L.; Ma, C. Y. Raman spectroscopic study of deamidated food proteins Food Chem. 2009, 113, 363-370
    • (2009) Food Chem. , vol.113 , pp. 363-370
    • Wong, H.W.1    Mei, S.C.2    Phillips, D.L.3    Ma, C.Y.4
  • 22
    • 0542391117 scopus 로고
    • Monomeric and Oligomeric Enzymes
    • 2 nd ed. Ellis Horwood: Chichester. U.K
    • Palmer, B. A. Monomeric and Oligomeric Enzymes. In Understanding Enzymes, 2 nd ed.; Ellis Horwood: Chichester. U.K., 1985; Vol. 5, pp 88-96.
    • (1985) Understanding Enzymes , vol.5 , pp. 88-96
    • Palmer, B.A.1
  • 23
    • 0000971643 scopus 로고
    • The effect of heat on wheat gluten and the involvement of sulfhydryl-disulphide interchange reactions
    • Schofield, J. D.; Bottomley, R. C.; Timms, M. F.; Booth, M. R. The effect of heat on wheat gluten and the involvement of sulfhydryl-disulphide interchange reactions J. Cereal Sci. 1983, 1, 241-253
    • (1983) J. Cereal Sci. , vol.1 , pp. 241-253
    • Schofield, J.D.1    Bottomley, R.C.2    Timms, M.F.3    Booth, M.R.4
  • 24
    • 79960723159 scopus 로고    scopus 로고
    • Aggregation behavior of wheat gluten during carboxylic acid deamidation upon hydrothermal treatment
    • Liao, L.; Liu, T. X.; Zhao, M. M.; Cui, C.; Zhao, H. F. Aggregation behavior of wheat gluten during carboxylic acid deamidation upon hydrothermal treatment J. Cereal Sci. 2011, 54, 129-136
    • (2011) J. Cereal Sci. , vol.54 , pp. 129-136
    • Liao, L.1    Liu, T.X.2    Zhao, M.M.3    Cui, C.4    Zhao, H.F.5
  • 25
    • 3242700672 scopus 로고    scopus 로고
    • Effect of surface hydrophobicity distribution on retention of ribonucleases in hydrophobic interaction chromatography
    • Mahn, A.; Lienqueo, M. E.; Asenjo, J. A. Effect of surface hydrophobicity distribution on retention of ribonucleases in hydrophobic interaction chromatography J. Chromatogr., A 2004, 1043, 47-55
    • (2004) J. Chromatogr., A , vol.1043 , pp. 47-55
    • Mahn, A.1    Lienqueo, M.E.2    Asenjo, J.A.3
  • 26
    • 39149108081 scopus 로고    scopus 로고
    • Nano-particle encapsulation of fish oilby spray drying
    • Jafari, S. M.; Assadpoor, E.; Bhandari, B.; He, Y. Nano-particle encapsulation of fish oilby spray drying Food Res. Int. 2008, 41, 172-183
    • (2008) Food Res. Int. , vol.41 , pp. 172-183
    • Jafari, S.M.1    Assadpoor, E.2    Bhandari, B.3    He, Y.4
  • 27
    • 0001121937 scopus 로고
    • Effects of deamidation with Chymotrypsin at pH 10 on the functional properties of proteins
    • Kato, A.; Tanaka, A.; Lee, Y.; Matsudomi, N.; Kobayashi, K. Effects of deamidation with Chymotrypsin at pH 10 on the functional properties of proteins J. Agric. Food Chem. 1987, 35, 285-288
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 285-288
    • Kato, A.1    Tanaka, A.2    Lee, Y.3    Matsudomi, N.4    Kobayashi, K.5
  • 28
    • 0038003146 scopus 로고    scopus 로고
    • Effects of Taiwanese yam (Dioscorea japonica Thunb var. pseudojaponica Yamamoto) on upper gut function and lipid metabolism in Balb/c mice
    • Chen, H. L.; Wang, C. H.; Chang, C. T.; Wang, T. C. Effects of Taiwanese yam (Dioscorea japonica Thunb var. pseudojaponica Yamamoto) on upper gut function and lipid metabolism in Balb/c mice Nutrition 2003, 19, 646-651
    • (2003) Nutrition , vol.19 , pp. 646-651
    • Chen, H.L.1    Wang, C.H.2    Chang, C.T.3    Wang, T.C.4
  • 29
    • 0025769655 scopus 로고
    • Nie SMand Kuck JFR. Near-infrared Fourier transform Raman and conventional Raman studies of calf-crystallins in the lyophilized state and in solution
    • Chen, W. Nie SMand Kuck JFR. Near-infrared Fourier transform Raman and conventional Raman studies of calf-crystallins in the lyophilized state and in solution J. Biophys. 1991, 60, 447-455
    • (1991) J. Biophys. , vol.60 , pp. 447-455
    • Chen, W.1
  • 30
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang, J. S.; Zhao, M. M.; Yang, X. Q. Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration J. Cereal Sci. 2006, 44, 93-100
    • (2006) J. Cereal Sci. , vol.44 , pp. 93-100
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3


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