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Volumn 90, Issue 4, 2010, Pages 658-663

Enhanced water absorption of wheat gluten by hydrothermal treatment followed by microbial transglutaminase reaction

Author keywords

Hydrothermal treatment; Microbial transglutaminase; Water absorption ratio; Wheat gluten

Indexed keywords

GLUTEN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; WATER;

EID: 76749160630     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3864     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 0142075364 scopus 로고    scopus 로고
    • Water as the determinant of food engineering properties
    • Lewicki PP, Water as the determinant of food engineering properties. A review. J Food Eng 61:483-495 (2004).
    • (2004) A Review. J Food Eng , vol.61 , pp. 483-495
    • Lewicki, P.P.1
  • 2
    • 50449088189 scopus 로고    scopus 로고
    • Variations in water absorption capacity and baking performance of barley varieties with different polysaccharide content and composition
    • Holtekjølen AK, Olsen HHR, Færgestad EM, Uhlen AK and Knutsen SH, Variations in water absorption capacity and baking performance of barley varieties with different polysaccharide content and composition. LWT-Food Sci Technol 41:2085-2091 (2008).
    • (2008) Lwt-food Sci Technol , vol.41 , pp. 2085-2091
    • Holtekjølen, A.K.1    Olsen, H.H.R.2    Færgestad, E.M.3    Uhlen, A.K.4    Knutsen, S.H.5
  • 3
    • 33748885488 scopus 로고    scopus 로고
    • Chemistry of gluten proteins
    • Wieser H, Chemistry of gluten proteins. Food Microbiol 24:115-119 (2007).
    • (2007) Food Microbiol , vol.24 , pp. 115-119
    • Wieser, H.1
  • 4
    • 4544384067 scopus 로고    scopus 로고
    • Application of a micro Z-arm mixer to characterize mixing properties and water absorption of wheat flour
    • Haraszi R, Gras PW, Tomoskozi S, Salgo A and Bekes F, Application of a micro Z-arm mixer to characterize mixing properties and water absorption of wheat flour. Cereal Chem 81:555-560 (2004).
    • (2004) Cereal Chem , vol.81 , pp. 555-560
    • Haraszi, R.1    Gras, P.W.2    Tomoskozi, S.3    Salgo, A.4    Bekes, F.5
  • 5
    • 1842435154 scopus 로고    scopus 로고
    • Water dynamics in white bread and starch gels as affected by water and gluten content
    • Wang X, Choi SG and Kerr WL, Water dynamics in white bread and starch gels as affected by water and gluten content. LWT-Food Sci Technol 37:377-384 (2004).
    • (2004) Lwt-food Sci Technol , vol.37 , pp. 377-384
    • Wang, X.1    Choi, S.G.2    Kerr, W.L.3
  • 6
    • 1642577211 scopus 로고    scopus 로고
    • Effects of wheat protein fractions on flour tortilla quality
    • Pascut S, Kelekci N and Waniska RD, Effects of wheat protein fractions on flour tortilla quality. Cereal Chem 81:38-43 (2004).
    • (2004) Cereal Chem , vol.81 , pp. 38-43
    • Pascut, S.1    Kelekci, N.2    Waniska, R.D.3
  • 8
    • 33646345878 scopus 로고    scopus 로고
    • Functional improvement of milk whey proteins induced by high hydrostatic pressure
    • Lopez-Fandino R, Functional improvement of milk whey proteins induced by high hydrostatic pressure. Crit Rev Food Sci Nutr 46:351-363 (2006).
    • (2006) Crit Rev Food Sci Nutr , vol.46 , pp. 351-363
    • Lopez-Fandino, R.1
  • 9
    • 0036188988 scopus 로고    scopus 로고
    • Physicochemical properties of acylated casein micelles in milk
    • Vidal V, Marchesseau S and Cuq JL, Physicochemical properties of acylated casein micelles in milk. J Food Sci 67:42-47 (2002).
    • (2002) J Food Sci , vol.67 , pp. 42-47
    • Vidal, V.1    Marchesseau, S.2    Cuq, J.L.3
  • 10
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
    • Yong YH, Yamaguchi S and Matsumura Y, Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten. J Agric Food Chem 54: 6034-6040 (2006).
    • (2006) J Agric Food Chem , vol.54 , pp. 6034-6040
    • Yong, Y.H.1    Yamaguchi, S.2    Matsumura, Y.3
  • 11
    • 0034301689 scopus 로고    scopus 로고
    • Thermal and mechanical properties and water absorption of guanidine hydrochloride-modified soy protein (11S)
    • Zhong ZK and Sun XS, Thermal and mechanical properties and water absorption of guanidine hydrochloride-modified soy protein (11S). J Appl Polym Sci 78:1063-1070 (2000).
    • (2000) J Appl Polym Sci , vol.78 , pp. 1063-1070
    • Zhong, Z.K.1    Sun, X.S.2
  • 12
    • 0022513002 scopus 로고
    • Water sorption by proteins - milk and whey proteins
    • Kinsella JE and Fox PF, Water sorption by proteins - milk and whey proteins. Crit Rev Food Sci Nutr 24:91-139 (1986).
    • (1986) Crit Rev Food Sci Nutr , vol.24 , pp. 91-139
    • Kinsella, J.E.1    Fox, P.F.2
  • 13
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama K, Nio N and Kikuchi Y, Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol 64:447-454 (2004).
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 14
    • 0000971643 scopus 로고
    • The effect of heat on wheat gluten and the involvement of sulfhydryl-disulfide interchange reactions
    • Schofield JD, Bottomley RC, Timms MF and Booth MR, The effect of heat on wheat gluten and the involvement of sulfhydryl-disulfide interchange reactions. J Cereal Sci 1:241-253 (1983).
    • (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
  • 15
    • 36148950974 scopus 로고    scopus 로고
    • Mechanism of gliadin-glutenin cross-linking during hydrothermal treatment
    • Lagrain B, Thewissen BG, Brijs K and Delcour JA, Mechanism of gliadin-glutenin cross-linking during hydrothermal treatment. Food Chem 107:753-760 (2008).
    • (2008) Food Chem , vol.107 , pp. 753-760
    • Lagrain, B.1    Thewissen, B.G.2    Brijs, K.3    Delcour, J.A.4
  • 16
    • 76549212824 scopus 로고
    • The enzymatic formation of hydroxamic acids from glutamine and asparagine
    • Grossowicz N, Wainfan E, Borek E and Waelsch H, The enzymatic formation of hydroxamic acids from glutamine and asparagine. J Biol Chem 187:111-125 (1950).
    • (1950) J Biol Chem , vol.187 , pp. 111-125
    • Grossowicz, N.1    Wainfan, E.2    Borek, E.3    Waelsch, H.4
  • 17
    • 0015136268 scopus 로고
    • Microchemical determination of organic nitrogen with Nessler reagent
    • Morrison GR, Microchemical determination of organic nitrogen with Nessler reagent. Anal Biochem 43:527-532 (1971).
    • (1971) Anal Biochem , vol.43 , pp. 527-532
    • Morrison, G.R.1
  • 19
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe methods and its correction with surface properties of proteins
    • Kato A and Nakai S, Hydrophobicity determined by a fluorescence probe methods and its correction with surface properties of proteins. Biochim Biophys Acta 624:13-20 (1980).
    • (1980) Biochim Biophys Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 20
    • 44349101790 scopus 로고    scopus 로고
    • Preparation and characterization of modified wheat gluten by enzymatic hydrolysis-ultrafiltration
    • Wang JS, Zhao MM, Bao Y, Hong T and Rosella CM, Preparation and characterization of modified wheat gluten by enzymatic hydrolysis-ultrafiltration. J Food Biochem 32:316-334 (2008).
    • (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
  • 21
    • 67649392930 scopus 로고    scopus 로고
    • SDS Polyacrylamide gel electrophoresis of proteins
    • 2nd edition. Humana Press Inc., Totowa, New Jersey
    • Walker JM, SDS Polyacrylamide gel electrophoresis of proteins, in The Protein Protocols Handbook, 2nd edition. Humana Press Inc., Totowa, New Jersey, pp. 61-67 (2002).
    • (2002) The Protein Protocols Handbook , pp. 61-67
    • Walker, J.M.1
  • 22
    • 33845550183 scopus 로고
    • Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity
    • Nakai S, Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J Agric Food Chem 31:676-683 (1983).
    • (1983) J Agric Food Chem , vol.31 , pp. 676-683
    • Nakai, S.1
  • 23
    • 33750430615 scopus 로고    scopus 로고
    • Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction
    • Wang JS, Zhao MM, Yang XQ, Jiang YM and Chun C, Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction. Food Hydrocolloids 21:174-179 (2007).
    • (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
  • 24
    • 0029114262 scopus 로고
    • Molecular flexibility in wheat gluten proteins submitted to heating
    • Hargreaves J, Popineau Y, Lemeste M and Hemminga MA, Molecular flexibility in wheat gluten proteins submitted to heating. FEBS Lett 372:103-107 (1995).
    • (1995) Febs Lett , vol.372 , pp. 103-107
    • Hargreaves, J.1    Popineau, Y.2    Lemeste, M.3    Hemminga, M.A.4
  • 25
    • 0036261525 scopus 로고    scopus 로고
    • Mechanism of heat and shear mediated aggregation of wheat gluten upon mixing
    • Morel MH, Redl A and Guilbert S, Mechanism of heat and shear mediated aggregation of wheat gluten upon mixing. Biomacromolecules 3:488-497 (2002).
    • (2002) Biomacromolecules , vol.3 , pp. 488-497
    • Morel, M.H.1    Redl, A.2    Guilbert, S.3
  • 26
    • 0242575228 scopus 로고    scopus 로고
    • Studies on effects of microbial transglutaminase on gluten proteins of wheat. I. Biochemical analysis
    • Bauer N, Koehler P, Wieser H and Schieberle P, Studies on effects of microbial transglutaminase on gluten proteins of wheat. I. Biochemical analysis. Cereal Chem 80:781-786 (2003).
    • (2003) Cereal Chem , vol.80 , pp. 781-786
    • Bauer, N.1    Koehler, P.2    Wieser, H.3    Schieberle, P.4
  • 27
    • 0035209417 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking
    • Sharma R, Lorenzen PC and Qvist KB, Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. Int Dairy J 11:785-793 (2001).
    • (2001) Int Dairy J , vol.11 , pp. 785-793
    • Sharma, R.1    Lorenzen, P.C.2    Qvist, K.B.3
  • 28
    • 84954873088 scopus 로고
    • Incorporation of amino acids into food proteins by transglutaminase
    • Ikura K, Yoshikawa M, Sasaki R and Chiba H, Incorporation of amino acids into food proteins by transglutaminase. Agric Biol Chem 45:2587-2592 (1981).
    • (1981) Agric Biol Chem , vol.45 , pp. 2587-2592
    • Ikura, K.1    Yoshikawa, M.2    Sasaki, R.3    Chiba, H.4


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