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Volumn 48, Issue 1, 2008, Pages 33-45

Microstructure, fundamental rheology and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase

Author keywords

Bread; Gluten free; Microstructure; Rheology; Transglutaminase

Indexed keywords

ERAGROSTIS TEF; ZEA MAYS;

EID: 42949105493     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2007.07.011     Document Type: Article
Times cited : (238)

References (47)
  • 2
    • 19044386700 scopus 로고    scopus 로고
    • Sensory, mechanical, and microscopic evaluation of staling in low-protein and gluten-free breads
    • Ahlborn G.J., Pike O.A., Hendrix S.B., Hess W.M., and Clayton S.H. Sensory, mechanical, and microscopic evaluation of staling in low-protein and gluten-free breads. Cereal Chemistry 82 3 (2005) 328-335
    • (2005) Cereal Chemistry , vol.82 , Issue.3 , pp. 328-335
    • Ahlborn, G.J.1    Pike, O.A.2    Hendrix, S.B.3    Hess, W.M.4    Clayton, S.H.5
  • 3
    • 0026682356 scopus 로고
    • Comparison of small and large deformation measurements to characterize the rheology of wheat flour doughs
    • Amemiya J.I., and Menjivar J.A. Comparison of small and large deformation measurements to characterize the rheology of wheat flour doughs. Journal of Food Engineering 16 (1992) 91-108
    • (1992) Journal of Food Engineering , vol.16 , pp. 91-108
    • Amemiya, J.I.1    Menjivar, J.A.2
  • 7
    • 0034255689 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein
    • Babiker E.E. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chemistry 70 (2000) 139-145
    • (2000) Food Chemistry , vol.70 , pp. 139-145
    • Babiker, E.E.1
  • 8
    • 0001187552 scopus 로고    scopus 로고
    • Improvement of the functional properties of sorghum protein by protein-polysaccharide and protein-protein complexes
    • Babiker E.E., and Kato A. Improvement of the functional properties of sorghum protein by protein-polysaccharide and protein-protein complexes. Nahrung 42 5 (1998) S286-S289
    • (1998) Nahrung , vol.42 , Issue.5
    • Babiker, E.E.1    Kato, A.2
  • 9
    • 0035021486 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on the thermoreversible gelation of gelatine
    • Babin H., and Dickinson E. Influence of transglutaminase treatment on the thermoreversible gelation of gelatine. Food Hydrocolloids 15 (2001) 271-276
    • (2001) Food Hydrocolloids , vol.15 , pp. 271-276
    • Babin, H.1    Dickinson, E.2
  • 10
    • 0036751964 scopus 로고    scopus 로고
    • Effects of transglutaminase on SDS-PAGE patterns of wheat, soy and barley proteins and their blends
    • Basman A., Koksel H., and Ng P.K.W. Effects of transglutaminase on SDS-PAGE patterns of wheat, soy and barley proteins and their blends. Journal of Food Science 67 (2002) 2654-2658
    • (2002) Journal of Food Science , vol.67 , pp. 2654-2658
    • Basman, A.1    Koksel, H.2    Ng, P.K.W.3
  • 11
    • 0242569722 scopus 로고    scopus 로고
    • Effects of increasing levels of transglutaminase on the rheological properties and bread quality characteristics of two wheat flours
    • Basman A., Koksel H., and Ng P.K.W. Effects of increasing levels of transglutaminase on the rheological properties and bread quality characteristics of two wheat flours. European Food Research and Technology 215 (2002) 419-424
    • (2002) European Food Research and Technology , vol.215 , pp. 419-424
    • Basman, A.1    Koksel, H.2    Ng, P.K.W.3
  • 12
    • 0002832217 scopus 로고
    • Texture profile analysis
    • 72
    • Bourne M.C. Texture profile analysis. Food Technology 32 (1978) 62-66 72
    • (1978) Food Technology , vol.32 , pp. 62-66
    • Bourne, M.C.1
  • 13
    • 16244393674 scopus 로고    scopus 로고
    • The gluten free diet: How to provide effective education and resources
    • Case S. The gluten free diet: How to provide effective education and resources. Gastroentrology 128 4 (2005) S128-S134
    • (2005) Gastroentrology , vol.128 , Issue.4
    • Case, S.1
  • 16
    • 0026522680 scopus 로고
    • Factors that govern the specificity of transglutaminase-catalysed modification of proteins and peptides
    • Coussons P., Price N.C., Kelly S.M., Smith B., and Sawyer L. Factors that govern the specificity of transglutaminase-catalysed modification of proteins and peptides. Biochemical Journal 282 (1992) 929-930
    • (1992) Biochemical Journal , vol.282 , pp. 929-930
    • Coussons, P.1    Price, N.C.2    Kelly, S.M.3    Smith, B.4    Sawyer, L.5
  • 17
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic cross-linking as a tool for food colloid rheology control and interfacial solubilization
    • Dickinson E. Enzymic cross-linking as a tool for food colloid rheology control and interfacial solubilization. Trends in Food Science and Technology 8 (1997) 334-339
    • (1997) Trends in Food Science and Technology , vol.8 , pp. 334-339
    • Dickinson, E.1
  • 18
    • 0017680149 scopus 로고
    • The ε-(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminase
    • Folk J.E., and Finlayson J.S. The ε-(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminase. Advances in Protein Chemistry 31 (1977) 1-133
    • (1977) Advances in Protein Chemistry , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 20
    • 0001237811 scopus 로고
    • Gas cell stabilisation and gas retention in wheat bread dough
    • Gan Z., Ellis P.R., and Schofield D.J. Gas cell stabilisation and gas retention in wheat bread dough. Journal of Cereal Science 21 (1995) 215-230
    • (1995) Journal of Cereal Science , vol.21 , pp. 215-230
    • Gan, Z.1    Ellis, P.R.2    Schofield, D.J.3
  • 23
    • 42949163741 scopus 로고    scopus 로고
    • Gottmann, K., Sproessler, B., inventors; Roehm GmbH, assignee, 1992. Backmittel oder Backmehl, sowie verfahren zur herstellung von Bachteigen and Backwaren. Patent EP0492406, 18 January.
    • Gottmann, K., Sproessler, B., inventors; Roehm GmbH, assignee, 1992. Backmittel oder Backmehl, sowie verfahren zur herstellung von Bachteigen and Backwaren. Patent EP0492406, 18 January.
  • 24
    • 1642271550 scopus 로고    scopus 로고
    • Functionality of rice flour modified with a microbial transglutaminase
    • Gujral H.S., and Rosell C.M. Functionality of rice flour modified with a microbial transglutaminase. Journal of Cereal Science 39 (2004) 225-230
    • (2004) Journal of Cereal Science , vol.39 , pp. 225-230
    • Gujral, H.S.1    Rosell, C.M.2
  • 25
  • 27
    • 23044526199 scopus 로고    scopus 로고
    • Grains in relation to celiac disease
    • Kasarda D.D. Grains in relation to celiac disease. Cereal Foods World 46 (2001) 209-210
    • (2001) Cereal Foods World , vol.46 , pp. 209-210
    • Kasarda, D.D.1
  • 28
    • 16244375839 scopus 로고    scopus 로고
    • Dietary guidelines and implementation for celiac disease
    • Kupper C. Dietary guidelines and implementation for celiac disease. Gastroenterology 128 4 (2005) S121-S127
    • (2005) Gastroenterology , vol.128 , Issue.4
    • Kupper, C.1
  • 29
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: its utilization in the food industry
    • Kuraishi C., Yamazaki K., and Susa Y. Transglutaminase: its utilization in the food industry. Food Reviews International 17 (2001) 221-246
    • (2001) Food Reviews International , vol.17 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 30
    • 0003244305 scopus 로고    scopus 로고
    • Hydrated gluten modified by a tranglutaminase
    • Larré C., Deshayes G., Lefebvre J., and Popineau Y. Hydrated gluten modified by a tranglutaminase. Nahrung 42 3/4S (1998) 155-157
    • (1998) Nahrung , vol.42 , Issue.3-4 S , pp. 155-157
    • Larré, C.1    Deshayes, G.2    Lefebvre, J.3    Popineau, Y.4
  • 31
    • 0036686486 scopus 로고    scopus 로고
    • Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yoghurt
    • Lorenzen P.C.H.R., Neve H., Mautner A., and Schlimme E. Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yoghurt. International Journal of Dairy Technology 55 3 (2002) 152-157
    • (2002) International Journal of Dairy Technology , vol.55 , Issue.3 , pp. 152-157
    • Lorenzen, P.C.H.R.1    Neve, H.2    Mautner, A.3    Schlimme, E.4
  • 33
    • 42949173210 scopus 로고    scopus 로고
    • Extraction and electrophoretic characterization of rice proteins
    • Meesook K., and Jeong Y. Extraction and electrophoretic characterization of rice proteins. Nutraceuticals & Food 7 (2002) 437-441
    • (2002) Nutraceuticals & Food , vol.7 , pp. 437-441
    • Meesook, K.1    Jeong, Y.2
  • 34
    • 72449130043 scopus 로고
    • Chromatographic determination of amino acids by the use of automatic recording equipment
    • Moore S., and Stein W.H. Chromatographic determination of amino acids by the use of automatic recording equipment. Methods in Enzymology 6 (1963) 819-831
    • (1963) Methods in Enzymology , vol.6 , pp. 819-831
    • Moore, S.1    Stein, W.H.2
  • 35
    • 4544249254 scopus 로고    scopus 로고
    • Textural comparison of gluten-free and wheat based doughs, batters and breads
    • Moore M.M., Schober T.J., Dockery P., and Arendt E.K. Textural comparison of gluten-free and wheat based doughs, batters and breads. Cereal Chemistry 81 (2004) 567-575
    • (2004) Cereal Chemistry , vol.81 , pp. 567-575
    • Moore, M.M.1    Schober, T.J.2    Dockery, P.3    Arendt, E.K.4
  • 38
    • 84954942298 scopus 로고
    • Functional properties of food proteins polymerized by transglutaminase
    • Motoki M., Nio N., and Takinami K. Functional properties of food proteins polymerized by transglutaminase. Agricultural and Biological Chemistry 48 (1984) 1257-1261
    • (1984) Agricultural and Biological Chemistry , vol.48 , pp. 1257-1261
    • Motoki, M.1    Nio, N.2    Takinami, K.3
  • 39
    • 0037165563 scopus 로고    scopus 로고
    • Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase
    • Nai-Chi Siu, Ching-Yung Ma, Wai-Yin Mock, and Yoshinori Mine. Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase. Journal of Agricultural and Food Chemistry 50 (2002) 2666-2672
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 2666-2672
    • Nai-Chi Siu1    Ching-Yung Ma2    Wai-Yin Mock3    Yoshinori Mine4
  • 40
    • 0037165562 scopus 로고    scopus 로고
    • Physicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminase
    • Nai-Chi Siu, Ching-Yung Ma, and Yoshinori Mine. Physicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminase. Journal of Agricultural and Food Chemistry 50 (2002) 2660-2665
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 2660-2665
    • Nai-Chi Siu1    Ching-Yung Ma2    Yoshinori Mine3
  • 42
    • 14644394500 scopus 로고
    • Changes in nitrogen and carbohydrate fractions in developing oat groats
    • Peterson D.M., and Smith D. Changes in nitrogen and carbohydrate fractions in developing oat groats. Crop Science 16 (1976) 67-71
    • (1976) Crop Science , vol.16 , pp. 67-71
    • Peterson, D.M.1    Smith, D.2
  • 43
    • 4444320892 scopus 로고    scopus 로고
    • Effects of gluten and transglutaminase on microstructure, sensory characteristics and instrumental texture of oat bread
    • Salmenkallio-Marttila M., Roininen K., Autio K., and Lähteenmäki L. Effects of gluten and transglutaminase on microstructure, sensory characteristics and instrumental texture of oat bread. Agricultural and Food Science 13 (2004) 138-150
    • (2004) Agricultural and Food Science , vol.13 , pp. 138-150
    • Salmenkallio-Marttila, M.1    Roininen, K.2    Autio, K.3    Lähteenmäki, L.4
  • 45
    • 85025569807 scopus 로고
    • Functional properties of proteins and role of protein-polysaccharide interaction
    • Tolstoguzov V.B. Functional properties of proteins and role of protein-polysaccharide interaction. Food Hydrocolloids 4 (1991) 429-468
    • (1991) Food Hydrocolloids , vol.4 , pp. 429-468
    • Tolstoguzov, V.B.1
  • 46
    • 42949135186 scopus 로고    scopus 로고
    • Wijngaards, G., Zhu, Y., Maagd, J. M., Bol, J., 1997. Transglutaminase as a potential tool in developing new protein ingredients and foods. Medical Faculty Landbouww, University of Gent 62, 1381-1383.
    • Wijngaards, G., Zhu, Y., Maagd, J. M., Bol, J., 1997. Transglutaminase as a potential tool in developing new protein ingredients and foods. Medical Faculty Landbouww, University of Gent 62, 1381-1383.
  • 47
    • 0000336639 scopus 로고    scopus 로고
    • Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase
    • Xiao-Qing Han, and Srinivasan Damodaran. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. Journal of Agricultural and Food Chemistry 44 (1996) 1211-1217
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 1211-1217
    • Xiao-Qing Han1    Srinivasan Damodaran2


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