메뉴 건너뛰기




Volumn 197, Issue , 2016, Pages 168-174

Effects of partial hydrolysis and subsequent cross-linking on wheat gluten physicochemical properties and structure

Author keywords

Cross linking; Partial hydrolysis; Physicochemical properties; Structure; Wheat gluten

Indexed keywords

AMINO ACIDS; HYDROLYSIS; HYDROPHOBICITY; RHEOLOGY; STRUCTURE (COMPOSITION); THERMODYNAMIC PROPERTIES;

EID: 84945901995     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.10.123     Document Type: Article
Times cited : (137)

References (36)
  • 2
    • 0342804403 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties
    • A.M. Barca, R.A. Ruiz-Salazar, and M.E. Jara-Marini Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties Journal of Food Science 65 2000 246 253
    • (2000) Journal of Food Science , vol.65 , pp. 246-253
    • Barca, A.M.1    Ruiz-Salazar, R.A.2    Jara-Marini, M.E.3
  • 3
    • 35549005384 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates
    • I. Celus, K. Brijs, and J.A. Delcour Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates Journal of Agricultural and Food Chemistry 55 2007 8703 8710
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 8703-8710
    • Celus, I.1    Brijs, K.2    Delcour, J.A.3
  • 4
    • 0003081480 scopus 로고
    • Direct colorimetric assay of free thiol groups and disulfide bonds in suspensions of solubilized and particulate cereal proteins
    • K.Y. Chan, and B.P. Wasserman Direct colorimetric assay of free thiol groups and disulfide bonds in suspensions of solubilized and particulate cereal proteins Cereal Chemistry 70 1993 22
    • (1993) Cereal Chemistry , vol.70 , pp. 22
    • Chan, K.Y.1    Wasserman, B.P.2
  • 5
    • 84856667080 scopus 로고    scopus 로고
    • Comparative study on protein cross-linking and gel enhancing effect of microbial transglutaminase on surimi from different fish
    • S. Chanarat, and S. Benjakul Comparative study on protein cross-linking and gel enhancing effect of microbial transglutaminase on surimi from different fish Journal of the Science of Food and Agriculture 92 2012 844 852
    • (2012) Journal of the Science of Food and Agriculture , vol.92 , pp. 844-852
    • Chanarat, S.1    Benjakul, S.2
  • 7
    • 84879378668 scopus 로고    scopus 로고
    • Effect of the structural features of hydrochloric acid-deamidated wheat gluten on its susceptibility to enzymatic hydrolysis
    • C. Cui, Q. Hu, J. Ren, H. Zhao, L. You, and M. Zhao Effect of the structural features of hydrochloric acid-deamidated wheat gluten on its susceptibility to enzymatic hydrolysis Journal of Agricultural and Food Chemistry 61 2013 5706 5714
    • (2013) Journal of Agricultural and Food Chemistry , vol.61 , pp. 5706-5714
    • Cui, C.1    Hu, Q.2    Ren, J.3    Zhao, H.4    You, L.5    Zhao, M.6
  • 8
    • 84861429878 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate
    • S. Damodaran, and K.K. Agyare Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate Food Hydrocolloids 30 2013 12 18
    • (2013) Food Hydrocolloids , vol.30 , pp. 12-18
    • Damodaran, S.1    Agyare, K.K.2
  • 10
    • 84896137310 scopus 로고    scopus 로고
    • Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions
    • X.L. Feng, H.Z. Liu, A.M. Shi, L. Liu, Q. Wang, and B. Adhikari Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions Food Research International 62 2014 84 90
    • (2014) Food Research International , vol.62 , pp. 84-90
    • Feng, X.L.1    Liu, H.Z.2    Shi, A.M.3    Liu, L.4    Wang, Q.5    Adhikari, B.6
  • 11
    • 33644606321 scopus 로고    scopus 로고
    • Effects of temperature and water content on the secondary structure of wheat gluten studied by FTIR spectroscopy
    • D.M. Georget, and P.S. Belton Effects of temperature and water content on the secondary structure of wheat gluten studied by FTIR spectroscopy Biomacromolecules 7 2006 469 475
    • (2006) Biomacromolecules , vol.7 , pp. 469-475
    • Georget, D.M.1    Belton, P.S.2
  • 12
    • 84928565712 scopus 로고    scopus 로고
    • Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate
    • A.M. Ghribi, I.M. Gafsi, A. Sila, C. Blecker, S. Danthine, and H. Attia S. Besbes Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate Food Chemistry 187 2015 322 330
    • (2015) Food Chemistry , 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    Besbes, S.7
  • 13
    • 80051713269 scopus 로고    scopus 로고
    • Effects of microfluidization treatment and transglutaminase cross-linking on physicochemical, functional, and conformational properties of peanut protein isolate
    • X. Hu, M. Zhao, W. Sun, G. Zhao, and J. Ren Effects of microfluidization treatment and transglutaminase cross-linking on physicochemical, functional, and conformational properties of peanut protein isolate Journal of Agricultural and Food Chemistry 59 2011 8886 8894
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 8886-8894
    • Hu, X.1    Zhao, M.2    Sun, W.3    Zhao, G.4    Ren, J.5
  • 14
    • 67649205136 scopus 로고    scopus 로고
    • Endogenous redox agents and enzymes that affect protein network formation during breadmaking-a review
    • I.J. Joye, B. Lagrain, and J.A. Delcour Endogenous redox agents and enzymes that affect protein network formation during breadmaking-a review Journal of Cereal Science 50 2009 1 10
    • (2009) Journal of Cereal Science , vol.50 , pp. 1-10
    • Joye, I.J.1    Lagrain, B.2    Delcour, J.A.3
  • 15
    • 0002643154 scopus 로고
    • Glutenin structure in relation to wheat quality
    • D.D. Kasarda Glutenin structure in relation to wheat quality Wheat is Unique 1989 277 302
    • (1989) Wheat Is Unique , pp. 277-302
    • Kasarda, D.D.1
  • 16
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • A. Kato, and S. Nakai Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins Biochimica et Biophysica Acta (BBA)-Protein Structure 624 1980 13 20
    • (1980) Biochimica et Biophysica Acta (BBA)-Protein Structure , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 78649631576 scopus 로고    scopus 로고
    • Susceptibility of wheat gluten to enzymatic hydrolysis following deamidation with acetic acid and sensory characteristics of the resultant hydrolysates
    • L. Liao, C.Y. Qiu, T.X. Liu, M.M. Zhao, J.Y. Ren, and H.F. Zhao Susceptibility of wheat gluten to enzymatic hydrolysis following deamidation with acetic acid and sensory characteristics of the resultant hydrolysates Journal of Cereal Science 52 2010 395 403
    • (2010) Journal of Cereal Science , 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
  • 21
    • 0033502450 scopus 로고    scopus 로고
    • The glutenin macropolymer of wheat flour doughs: Structure-function perspectives
    • M.P. Lindsay, and J.H. Skerritt The glutenin macropolymer of wheat flour doughs: Structure-function perspectives Trends in Food Science & Technology 10 1999 247 253
    • (1999) Trends in Food Science & Technology , vol.10 , pp. 247-253
    • Lindsay, M.P.1    Skerritt, J.H.2
  • 22
    • 12344251713 scopus 로고    scopus 로고
    • Effect of limited hydrolysis of sunflower protein on the interactions with polysaccharides in foams
    • K.D. Martinez, R.I. Baeza, F. Millan, and A.M.R. Pilosof Effect of limited hydrolysis of sunflower protein on the interactions with polysaccharides in foams Food Hydrocolloids 19 2005 361 369
    • (2005) Food Hydrocolloids , vol.19 , pp. 361-369
    • Martinez, K.D.1    Baeza, R.I.2    Millan, F.3    Pilosof, A.M.R.4
  • 24
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • J.K. Myers, C. Nick Pace, and J. Martin Scholtz Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding Protein Science 4 1995 2138 2148
    • (1995) Protein Science , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Nick Pace, C.2    Martin Scholtz, J.3
  • 25
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • I. Pallarès, J. Vendrell, F.X. Avilés, and S. Ventura Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin Journal of Molecular Biology 342 2004 321 331
    • (2004) Journal of Molecular Biology , vol.342 , pp. 321-331
    • Pallarès, I.1    Vendrell, J.2    Avilés, F.X.3    Ventura, S.4
  • 26
    • 84867708075 scopus 로고    scopus 로고
    • Effect of combined treatment of hydrolysis and polymerization with transglutaminase on β-lactoglobulin antigenicity
    • I.S. Sabadin, M.B. Villas-Boas, R. de Lima Zollner, and F.M. Netto Effect of combined treatment of hydrolysis and polymerization with transglutaminase on β-lactoglobulin antigenicity European Food Research and Technology 235 2012 801 809
    • (2012) European Food Research and Technology , vol.235 , pp. 801-809
    • Sabadin, I.S.1    Villas-Boas, M.B.2    De Lima Zollner, R.3    Netto, F.M.4
  • 27
    • 84901271451 scopus 로고    scopus 로고
    • Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase
    • C.L. Song, and X.H. Zhao Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase Food Chemistry 163 2014 114 119
    • (2014) Food Chemistry , vol.163 , pp. 114-119
    • Song, C.L.1    Zhao, X.H.2
  • 28
    • 84901802353 scopus 로고    scopus 로고
    • Relationship between secondary structure and surface hydrophobicity of soybean protein isolate subjected to heat treatment
    • Z. Wang, Y. Li, L. Jiang, B. Qi, and L. Zhou Relationship between secondary structure and surface hydrophobicity of soybean protein isolate subjected to heat treatment Journal of Chemistry 2014
    • (2014) Journal of Chemistry
    • Wang, Z.1    Li, Y.2    Jiang, L.3    Qi, B.4    Zhou, L.5
  • 29
    • 84886310365 scopus 로고    scopus 로고
    • Effect of frozen storage on the conformational, thermal and microscopic properties of gluten: Comparative studies on gluten-, glutenin-and gliadin-rich fractions
    • P. Wang, L. Xu, M. Nikoo, D. Ocen, F. Wu, and N. Yang X. Xu Effect of frozen storage on the conformational, thermal and microscopic properties of gluten: Comparative studies on gluten-, glutenin-and gliadin-rich fractions Food Hydrocolloids 35 2014 238 246
    • (2014) Food Hydrocolloids , vol.35 , pp. 238-246
    • Wang, P.1    Xu, L.2    Nikoo, M.3    Ocen, D.4    Wu, F.5    Yang, N.6    Xu, X.7
  • 30
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • J. Wang, M. Zhao, X. Yang, and Y. Jiang Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration Journal of Cereal Science 44 2006 93 100
    • (2006) Journal of Cereal Science , vol.44 , pp. 93-100
    • Wang, J.1    Zhao, M.2    Yang, X.3    Jiang, Y.4
  • 31
    • 33750430615 scopus 로고    scopus 로고
    • Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction
    • J.S. Wang, M.M. Zhao, X.Q. Yang, Y.M. Jiang, and C. Chun Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction Food Hydrocolloids 21 2007 174 179
    • (2007) Food Hydrocolloids , vol.21 , pp. 174-179
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3    Jiang, Y.M.4    Chun, C.5
  • 32
    • 33748885488 scopus 로고    scopus 로고
    • Chemistry of gluten proteins
    • H. Wieser Chemistry of gluten proteins Food Microbiology 24 2007 115 119
    • (2007) Food Microbiology , vol.24 , pp. 115-119
    • Wieser, H.1
  • 33
    • 34548487814 scopus 로고    scopus 로고
    • Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate
    • S.W. Yin, C.H. Tang, J.S. Cao, E.K. Hu, Q.B. Wen, and X.Q. Yang Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate Food Chemistry 106 2008 1004 1013
    • (2008) Food Chemistry , vol.106 , pp. 1004-1013
    • Yin, S.W.1    Tang, C.H.2    Cao, J.S.3    Hu, E.K.4    Wen, Q.B.5    Yang, X.Q.6
  • 35
    • 84901234161 scopus 로고    scopus 로고
    • Effects of maltodextrin glycosylation following limited enzymatic hydrolysis on the functional and conformational properties of soybean protein isolate
    • Y. Zhang, C. Tan, X. Zhang, S. Xia, C. Jia, and K. Eric F. Zhong Effects of maltodextrin glycosylation following limited enzymatic hydrolysis on the functional and conformational properties of soybean protein isolate European Food Research and Technology 238 2014 957 968
    • (2014) European Food Research and Technology , vol.238 , pp. 957-968
    • Zhang, Y.1    Tan, C.2    Zhang, X.3    Xia, S.4    Jia, C.5    Eric, K.6    Zhong, F.7
  • 36
    • 79953203868 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate
    • G. Zhao, Y. Liu, M. Zhao, J. Ren, and B. Yang Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate Food Chemistry 127 2011 1438 1443
    • (2011) Food Chemistry , vol.127 , pp. 1438-1443
    • Zhao, G.1    Liu, Y.2    Zhao, M.3    Ren, J.4    Yang, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.