메뉴 건너뛰기




Volumn 83, Issue 1, 2006, Pages 28-36

Network formation in gluten-free bread with application of transglutaminase

Author keywords

[No Author keywords available]

Indexed keywords

CROSSLINKING; FOOD PRODUCTS; IMAGE TEXTURE; QUALITY CONTROL; STARCH;

EID: 30844474169     PISSN: 00090352     EISSN: None     Source Type: Journal    
DOI: 10.1094/CC-83-0028     Document Type: Article
Times cited : (248)

References (36)
  • 2
    • 0242569722 scopus 로고    scopus 로고
    • Effects of increasing levels of transglutaminase on the Theological properties and bread quality characteristics of two wheat flours
    • Basman, A., Köksel, H., and Ng, P. K. W. 2002. Effects of increasing levels of transglutaminase on the Theological properties and bread quality characteristics of two wheat flours. Eur. Food Res. Technol. 215:419-424.
    • (2002) Eur. Food Res. Technol. , vol.215 , pp. 419-424
    • Basman, A.1    Köksel, H.2    Ng, P.K.W.3
  • 3
    • 30944452690 scopus 로고    scopus 로고
    • Studies on the effects of microbial transglutaminase on gluten proteins of wheat
    • AACC International: St. Paul, MN
    • Bauer, N., Koehler, P., Wieser, H., and Schieberle, P. 2003. Studies on the effects of microbial transglutaminase on gluten proteins of wheat. Pages 107-113 in: Recent Advances in Enzymes in Grain Processing. AACC International: St. Paul, MN.
    • (2003) Recent Advances in Enzymes in Grain Processing , pp. 107-113
    • Bauer, N.1    Koehler, P.2    Wieser, H.3    Schieberle, P.4
  • 4
    • 0003895440 scopus 로고
    • Springer Verlag: New York
    • Belitz, H. D., and Grosch, W. 1987. Pages 379-388, 395-396, 403-412, and 536-538 in: Food Chemistry. Springer Verlag: New York.
    • (1987) Food Chemistry , pp. 379-388
    • Belitz, H.D.1    Grosch, W.2
  • 5
    • 1542780385 scopus 로고    scopus 로고
    • The effect of storage time on textural and crumb grain characteristics of sourdough wheat bread
    • Crowley, P., Schober, T. J., Clarke, C. I., and Arendt, E. K. 2002. The effect of storage time on textural and crumb grain characteristics of sourdough wheat bread. Eur. Food Res. Technol. 214:489-496.
    • (2002) Eur. Food Res. Technol. , vol.214 , pp. 489-496
    • Crowley, P.1    Schober, T.J.2    Clarke, C.I.3    Arendt, E.K.4
  • 6
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food application
    • De Jong, G. A. H., and Koppelmann, S. J. 2002. Transglutaminase catalyzed reactions: Impact on food application. J. Food Sci. 67:2798-2805.
    • (2002) J. Food Sci. , vol.67 , pp. 2798-2805
    • De Jong, G.A.H.1    Koppelmann, S.J.2
  • 7
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic cross-linking as a tool for food colloid rheology control and interfacial stabilization
    • Dickinson, E. 1997. Enzymic cross-linking as a tool for food colloid rheology control and interfacial stabilization. Trends Food Sci. Technol. 8:334-339.
    • (1997) Trends Food Sci. Technol. , vol.8 , pp. 334-339
    • Dickinson, E.1
  • 8
    • 0036236205 scopus 로고    scopus 로고
    • Transglutaminase in baking applications
    • Diez Poza, O. 2002. Transglutaminase in baking applications. Cereal Foods World 47:93-95.
    • (2002) Cereal Foods World , vol.47 , pp. 93-95
    • Diez Poza, O.1
  • 9
    • 0033600430 scopus 로고    scopus 로고
    • Fortnightly review. Celiac Disease
    • Feighery, C. 1999. Fortnightly review. Celiac Disease. Brit. Med. J. 319:236-239.
    • (1999) Brit. Med. J. , vol.319 , pp. 236-239
    • Feighery, C.1
  • 10
    • 1542350800 scopus 로고    scopus 로고
    • Recent advances in the formulation of gluten-free cereal-based products
    • Gallagher, E., Gormley, T. R., and Arendt, E. K. 2003. Recent advances in the formulation of gluten-free cereal-based products. Trends Food Sci. Technol. 15:143-152.
    • (2003) Trends Food Sci. Technol. , vol.15 , pp. 143-152
    • Gallagher, E.1    Gormley, T.R.2    Arendt, E.K.3
  • 11
    • 0037290293 scopus 로고    scopus 로고
    • Crust and crumb characteristics of gluten-free breads
    • Gallagher, E., Gormley, T. R., and Arendt, E. K. 2004. Crust and crumb characteristics of gluten-free breads. J. Food Eng. 56:153-161.
    • (2004) J. Food Eng. , vol.56 , pp. 153-161
    • Gallagher, E.1    Gormley, T.R.2    Arendt, E.K.3
  • 12
    • 0036980061 scopus 로고    scopus 로고
    • Protein-protein crosslinking in food: Methods, consequences, applications
    • Gerrard, J. A. 2002. Protein-protein crosslinking in food: Methods, consequences, applications. Trends Food Sci. Technol. 13:391-399.
    • (2002) Trends Food Sci. Technol. , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 13
    • 0031832353 scopus 로고    scopus 로고
    • The effect of microbial transglutaminase on dough properties and crumb strength of white pan bread
    • Gerrard, J. A., Fayle, S. E., Wilson, A. J., Newberry, M. P., Ross, M., and Kavale, S. 1998. The effect of microbial transglutaminase on dough properties and crumb strength of white pan bread. J. Food Sci. 63:472-475.
    • (1998) J. Food Sci. , vol.63 , pp. 472-475
    • Gerrard, J.A.1    Fayle, S.E.2    Wilson, A.J.3    Newberry, M.P.4    Ross, M.5    Kavale, S.6
  • 15
    • 1042301085 scopus 로고    scopus 로고
    • Different hydrocolloids as bread improvers and antistaling agents
    • Guarda, A., Rosell, C. M., Benedito, C., and Galotto, M. J. 2003. Different hydrocolloids as bread improvers and antistaling agents. Food Hydrocolloids 18:241-247.
    • (2003) Food Hydrocolloids , vol.18 , pp. 241-247
    • Guarda, A.1    Rosell, C.M.2    Benedito, C.3    Galotto, M.J.4
  • 16
    • 0000336639 scopus 로고    scopus 로고
    • Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase
    • Han, X.-Q., and Damodaran, S. 1996. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. J. Agric. Food Chem. 44:1211-1217.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 1211-1217
    • Han, X.-Q.1    Damodaran, S.2
  • 17
    • 0033978216 scopus 로고    scopus 로고
    • Effects of commercial hydrolytic enzyme additives on Canadian short process bread properties and processing characteristics
    • Harada, O., Lysenko, E. D., and Preston, K. R. 2000. Effects of commercial hydrolytic enzyme additives on Canadian short process bread properties and processing characteristics. Cereal Chem. 77:70-76.
    • (2000) Cereal Chem. , vol.77 , pp. 70-76
    • Harada, O.1    Lysenko, E.D.2    Preston, K.R.3
  • 19
    • 0001261464 scopus 로고
    • Enthalpy of denaturation and surface functional properties of heated egg white proteins in the dry state
    • Kato, A., Ibrahim, H., Watanabe, H., Honma, K., and Kobayashi, K. 1990. Enthalpy of denaturation and surface functional properties of heated egg white proteins in the dry state. J. Food Sci. 55:1280-1282.
    • (1990) J. Food Sci. , vol.55 , pp. 1280-1282
    • Kato, A.1    Ibrahim, H.2    Watanabe, H.3    Honma, K.4    Kobayashi, K.5
  • 20
    • 0002332254 scopus 로고    scopus 로고
    • The usefulness of transglutaminase for food processing
    • Oxford University Press: Oxford, UK
    • Kuraishi, C., Sakamoto, J., and Soeda, T. 1996. The usefulness of transglutaminase for food processing. Pages 29-38 in: Biotechnology for Improved Foods and Flavours. Oxford University Press: Oxford, UK.
    • (1996) Biotechnology for Improved Foods and Flavours , pp. 29-38
    • Kuraishi, C.1    Sakamoto, J.2    Soeda, T.3
  • 21
    • 0003244305 scopus 로고    scopus 로고
    • Hydrated gluten modified by transglutaminase
    • Larré, C., Deshayes, G., Lefebevre, J., and Popineau, Y. 1998. Hydrated gluten modified by transglutaminase. Nahrung 42:155-157.
    • (1998) Nahrung , vol.42 , pp. 155-157
    • Larré, C.1    Deshayes, G.2    Lefebevre, J.3    Popineau, Y.4
  • 23
    • 0002217453 scopus 로고
    • Confocal microscopy
    • Lichtman, J. W. 1994. Confocal microscopy. Sci. Am. 271:40-45.
    • (1994) Sci. Am. , vol.271 , pp. 40-45
    • Lichtman, J.W.1
  • 24
    • 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. 2004. Textural comparison of gluten-free and wheat based doughs, batters and breads. Cereal Chem. 81:567-575.
    • (2004) Cereal Chem. , vol.81 , pp. 567-575
    • Moore, M.M.1    Schober, T.J.2    Dockery, P.3    Arendt, E.K.4
  • 25
    • 0000633489 scopus 로고    scopus 로고
    • Recent research trends in transglutaminase technology for food processing
    • Motoki, M., and Kumazawa, Y. 2000. Recent research trends in transglutaminase technology for food processing. Food Sci. Tech. Res. 6:151-160.
    • (2000) Food Sci. Tech. Res. , vol.6 , pp. 151-160
    • Motoki, M.1    Kumazawa, Y.2
  • 26
    • 0031690193 scopus 로고    scopus 로고
    • Transglutaminase and its use for food processing
    • Motoki, M., and Seguro, K. 1998. Transglutaminase and its use for food processing. Trends Food Sci. Technol. 9:204-210.
    • (1998) Trends Food Sci. Technol. , vol.9 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 27
    • 0037207551 scopus 로고    scopus 로고
    • Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate
    • Murguruma, M., Tsuruoka, K., Katayama, K., Erwanto, Y., Kawahara, S., Yamauchi, K., Sathe, S. K., and Soeda, T. 2003. Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Sci. 63:191-197.
    • (2003) Meat Sci. , vol.63 , pp. 191-197
    • Murguruma, M.1    Tsuruoka, K.2    Katayama, K.3    Erwanto, Y.4    Kawahara, S.5    Yamauchi, K.6    Sathe, S.K.7    Soeda, T.8
  • 28
    • 85025323198 scopus 로고
    • Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels
    • Nonaka, M., Toiguchi, S., Sakamoto, H., Kawajiri, H., Soeda, T., and Motoki, M. 1994. Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels. Food Hydrocolloids 8:1-8.
    • (1994) Food Hydrocolloids , vol.8 , pp. 1-8
    • Nonaka, M.1    Toiguchi, S.2    Sakamoto, H.3    Kawajiri, H.4    Soeda, T.5    Motoki, M.6
  • 30
    • 30944449350 scopus 로고    scopus 로고
    • Evaluation of the effect of different ingredients on the rheological properties of gluten-free pizza doughs
    • AACC International: St. Paul. MN
    • O'Brien, C. M., Schober, T., Arendt, E. K. 2002b. Evaluation of the effect of different ingredients on the rheological properties of gluten-free pizza doughs. Abstr. 2002 AACC Annual Meeting. Published online at http://www.scisoc.org/aacc/meeting/2002/abstracts/. AACC International: St. Paul. MN.
    • (2002) Abstr. 2002 AACC Annual Meeting
    • O'Brien, C.M.1    Schober, T.2    Arendt, E.K.3
  • 31
    • 0028139777 scopus 로고
    • Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions
    • Sakamoto, H., Kumazawa, Y., and Motoki, M. 1994. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59:866-871.
    • (1994) J. Food Sci. , vol.59 , pp. 866-871
    • Sakamoto, H.1    Kumazawa, Y.2    Motoki, M.3
  • 34
    • 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, P. C., and Qvist, K. B. 2001. 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) Int. Dairy J. , vol.11 , pp. 785-793
    • Sharma, R.1    Lorenzen, P.C.2    Qvist, K.B.3
  • 35
    • 0000227970 scopus 로고
    • Formulation of gluten-free pocket-type flat breads: Optimization of methylcellulose, gum arabic, and egg albumen levels by response surface methodology
    • Toufeili, I., Dagher, S., Shadarevian, S., Noureddine, A., Sarakbi, M., and Farran, M. T. 1994. Formulation of gluten-free pocket-type flat breads: Optimization of methylcellulose, gum arabic, and egg albumen levels by response surface methodology. Cereal Chem. 71:594-601.
    • (1994) Cereal Chem. , vol.71 , pp. 594-601
    • Toufeili, I.1    Dagher, S.2    Shadarevian, S.3    Noureddine, A.4    Sarakbi, M.5    Farran, M.T.6
  • 36
    • 33751390858 scopus 로고
    • Cross-linking activity of placental F XIIIa on whey proteins and caseins
    • Traoré, F., and Meunier, J.-C. 1980. Cross-linking activity of placental F XIIIa on whey proteins and caseins. J Agric. Food Chem. 40:399-402.
    • (1980) J Agric. Food Chem. , vol.40 , pp. 399-402
    • Traoré, F.1    Meunier, J.-C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.