메뉴 건너뛰기




Volumn 114, Issue 1, 2009, Pages 180-189

Effects of transglutaminase-induced cross-linking on properties of fish gelatin-nanoclay composite film

Author keywords

Composite; Film; MTGase; Nanoclay; Warm water fish gelatin

Indexed keywords


EID: 58149479586     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.09.057     Document Type: Article
Times cited : (74)

References (48)
  • 1
    • 0141987151 scopus 로고
    • American Society for Testing and Materials, Philadelphia, PA
    • ASTM. Standard methods for water vapour transmission of materials (E 96-80). Annual Book of ASTM Standards (1987), American Society for Testing and Materials, Philadelphia, PA
    • (1987) Annual Book of ASTM Standards
    • ASTM1
  • 2
    • 0141987151 scopus 로고
    • American Society for Testing and Materials, Philadelphia, PA
    • ASTM. Standard methods for tensile properties of thin plastic sheeting (E 882-88). Annual Book of ASTM Standards (1989), American Society for Testing and Materials, Philadelphia, PA
    • (1989) Annual Book of ASTM Standards
    • ASTM1
  • 3
    • 0035021486 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on the thermoreversible gelation of gelatin
    • Babin H., and Dickinson E. Influence of transglutaminase treatment on the thermoreversible gelation of gelatin. Food Hydrocolloid 15 3 (2001) 271-276
    • (2001) Food Hydrocolloid , vol.15 , Issue.3 , pp. 271-276
    • Babin, H.1    Dickinson, E.2
  • 4
    • 58149495012 scopus 로고    scopus 로고
    • Bae, H.J., Byun, Y.J., Hong, S.I., Darby, D.O., Kimmel, R.M., Park, H.J., et al. (2007). Effect of clay content, homogenization RPM, pH, and ultrasonification on mechanical and barrier properties of fish gelatin/montmorillonite nanocomposites. Dissertation, Clemson University.
    • Bae, H.J., Byun, Y.J., Hong, S.I., Darby, D.O., Kimmel, R.M., Park, H.J., et al. (2007). Effect of clay content, homogenization RPM, pH, and ultrasonification on mechanical and barrier properties of fish gelatin/montmorillonite nanocomposites. Dissertation, Clemson University.
  • 5
    • 0242490912 scopus 로고    scopus 로고
    • Suwari gel properties as affected by transglutaminase activator and inhibitors
    • Benjakul S., Visessanguan W., and Pecharat S. Suwari gel properties as affected by transglutaminase activator and inhibitors. Food Chemistry 85 1 (2004) 91-99
    • (2004) Food Chemistry , vol.85 , Issue.1 , pp. 91-99
    • Benjakul, S.1    Visessanguan, W.2    Pecharat, S.3
  • 6
    • 0032401782 scopus 로고    scopus 로고
    • Drawn gelatin films with improved mechanical properties
    • Bigi A., Bracci B., Cojazzi G., Panzavolta S., and Roveri N. Drawn gelatin films with improved mechanical properties. Biomaterials 19 24 (1998) 2335-2340
    • (1998) Biomaterials , vol.19 , Issue.24 , pp. 2335-2340
    • Bigi, A.1    Bracci, B.2    Cojazzi, G.3    Panzavolta, S.4    Roveri, N.5
  • 7
    • 0035122037 scopus 로고    scopus 로고
    • Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking
    • Bigi A., Cojazzi G., Panzavolta S., Rubini K., and Roveri N. Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking. Biomaterials 22 8 (2001) 763
    • (2001) Biomaterials , vol.22 , Issue.8 , pp. 763
    • Bigi, A.1    Cojazzi, G.2    Panzavolta, S.3    Rubini, K.4    Roveri, N.5
  • 8
    • 2542482901 scopus 로고    scopus 로고
    • Relationship between triple-helix content and mechanical properties of gelatin films
    • Bigi A., Panzavolta S., and Rubini K. Relationship between triple-helix content and mechanical properties of gelatin films. Biomaterials 25 25 (2004) 5675-5680
    • (2004) Biomaterials , vol.25 , Issue.25 , pp. 5675-5680
    • Bigi, A.1    Panzavolta, S.2    Rubini, K.3
  • 9
    • 0038417840 scopus 로고    scopus 로고
    • Enzyme-catalyzed gel formation of gelatin and chitosan: Potential for in situ applications
    • Chen T., Embree H., Brown E., Taylor M., and Payne G. Enzyme-catalyzed gel formation of gelatin and chitosan: Potential for in situ applications. Biomaterials 24 17 (2003) 2831-2841
    • (2003) Biomaterials , vol.24 , Issue.17 , pp. 2831-2841
    • Chen, T.1    Embree, H.2    Brown, E.3    Taylor, M.4    Payne, G.5
  • 10
    • 3042541063 scopus 로고    scopus 로고
    • Characterization of gelatin based films modified with transglutaminase, glyoxal, and formaldehyde
    • De Carvalho R.A., and Grosso C.R.F. Characterization of gelatin based films modified with transglutaminase, glyoxal, and formaldehyde. Food Hydrocolloid 18 5 (2004) 717
    • (2004) Food Hydrocolloid , vol.18 , Issue.5 , pp. 717
    • De Carvalho, R.A.1    Grosso, C.R.F.2
  • 12
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization
    • Dickinson E. Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization. Trends in Food Science and Technology 8 10 (1997) 334-339
    • (1997) Trends in Food Science and Technology , vol.8 , Issue.10 , pp. 334-339
    • Dickinson, E.1
  • 13
    • 0000432286 scopus 로고
    • The adsorption of proteins by montmorillonitic clays
    • Ensminger L.E., and Gieseking J.E. The adsorption of proteins by montmorillonitic clays. Soil Science 48 (1939) 467-471
    • (1939) Soil Science , vol.48 , pp. 467-471
    • Ensminger, L.E.1    Gieseking, J.E.2
  • 14
    • 0001516396 scopus 로고
    • The adsorption of proteins by montmorillonitic clays and its effect on base-exchange capacity
    • Ensminger L.E., and Gieseking J.E. The adsorption of proteins by montmorillonitic clays and its effect on base-exchange capacity. Soil Science 51 (1941) 125-132
    • (1941) Soil Science , vol.51 , pp. 125-132
    • Ensminger, L.E.1    Gieseking, J.E.2
  • 15
    • 0034934084 scopus 로고    scopus 로고
    • Gel properties of collagens from skins of cod (Gadus morhua) and hake (Merluccius merluccius) and their modification by the coenhancers magnesium sulphate, glycerol, and transglutaminase
    • Fernandez-Diaz M., Montero P., and Gomez-Guillen M. Gel properties of collagens from skins of cod (Gadus morhua) and hake (Merluccius merluccius) and their modification by the coenhancers magnesium sulphate, glycerol, and transglutaminase. Food Chemistry 74 2 (2001) 161-167
    • (2001) Food Chemistry , vol.74 , Issue.2 , pp. 161-167
    • Fernandez-Diaz, M.1    Montero, P.2    Gomez-Guillen, M.3
  • 16
    • 12344309474 scopus 로고    scopus 로고
    • Effect of the thermal treatment of the filmogenic solution on the mechanical properties, colour and opacity of films based on muscle proteins of two varieties of tilapia
    • Garcia F.T., and Sobral P. Effect of the thermal treatment of the filmogenic solution on the mechanical properties, colour and opacity of films based on muscle proteins of two varieties of tilapia. Food Science and Technology 38 3 (2005) 289-296
    • (2005) Food Science and Technology , vol.38 , Issue.3 , pp. 289-296
    • Garcia, F.T.1    Sobral, P.2
  • 17
    • 0002140547 scopus 로고
    • Edible films and coatings from wheat and corn proteins
    • Gennadios A., and Weller C.L. Edible films and coatings from wheat and corn proteins. Food Technology 44 10 (1990) 63-69
    • (1990) Food Technology , vol.44 , Issue.10 , pp. 63-69
    • Gennadios, A.1    Weller, C.L.2
  • 18
    • 0000257069 scopus 로고
    • Edible films and coatings from soy milk and soy protein
    • Gennadios A., and Weller C.L. Edible films and coatings from soy milk and soy protein. Cereal Foods World 36 12 (1991) 1004-1009
    • (1991) Cereal Foods World , vol.36 , Issue.12 , pp. 1004-1009
    • Gennadios, A.1    Weller, C.L.2
  • 19
    • 0342502122 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on the functional properties of megrim (Lepidorhombus boscii) skin gelatin
    • Gomez-Guillen M.C., Sarabia A.I., Solas M.T., and Montero P. Effect of microbial transglutaminase on the functional properties of megrim (Lepidorhombus boscii) skin gelatin. Journal of the Science of Food and Agriculture 81 7 (2001) 665-673
    • (2001) Journal of the Science of Food and Agriculture , vol.81 , Issue.7 , pp. 665-673
    • Gomez-Guillen, M.C.1    Sarabia, A.I.2    Solas, M.T.3    Montero, P.4
  • 21
    • 2042546711 scopus 로고    scopus 로고
    • Physical behavior of fish gelatin-kappa-carrageenan mixtures
    • Haug I.J., Draget K.I., and Smidsrod A. Physical behavior of fish gelatin-kappa-carrageenan mixtures. Carbohydrate Polymers 56 1 (2004) 11-19
    • (2004) Carbohydrate Polymers , vol.56 , Issue.1 , pp. 11-19
    • Haug, I.J.1    Draget, K.I.2    Smidsrod, A.3
  • 22
    • 58149506742 scopus 로고    scopus 로고
    • Hunter Lab applications note (1996). September 1-15, Vol. 8, No. 11.
    • Hunter Lab applications note (1996). September 1-15, Vol. 8, No. 11.
  • 23
    • 0002314075 scopus 로고
    • Edible films and coatings - a review
    • Kester J.J., and Fennema O.R. Edible films and coatings - a review. Food Technology 40 12 (1986) 47-59
    • (1986) Food Technology , vol.40 , Issue.12 , pp. 47-59
    • Kester, J.J.1    Fennema, O.R.2
  • 25
    • 1442360981 scopus 로고    scopus 로고
    • Modification of the properties of gelatin from skins of Balticcod (Gadusmorhua) with transglutaminase
    • Kolodzlejska I., Kaczorowski K., Piotrowska B., and Sadowska M. Modification of the properties of gelatin from skins of Balticcod (Gadusmorhua) with transglutaminase. Food Chemistry 86 2 (2004) 203-209
    • (2004) Food Chemistry , vol.86 , Issue.2 , pp. 203-209
    • Kolodzlejska, I.1    Kaczorowski, K.2    Piotrowska, B.3    Sadowska, M.4
  • 26
    • 14744297808 scopus 로고    scopus 로고
    • The influence of salts and temperature on enzymatic activity of microbial transglutaminase
    • Kutemeyer C., Froeck M., Werlein H., and Watkinson B. The influence of salts and temperature on enzymatic activity of microbial transglutaminase. Food Control 16 8 (2005) 735-737
    • (2005) Food Control , vol.16 , Issue.8 , pp. 735-737
    • Kutemeyer, C.1    Froeck, M.2    Werlein, H.3    Watkinson, B.4
  • 27
    • 0032858668 scopus 로고    scopus 로고
    • Barrier and tensile properties of transglutaminase crosslinked gelatin films as affected by relative humidity, temperature, and glycerol content
    • Lim L., Mine Y., and Tung M. Barrier and tensile properties of transglutaminase crosslinked gelatin films as affected by relative humidity, temperature, and glycerol content. Journal of Food Science 64 4 (1999) 616-622
    • (1999) Journal of Food Science , vol.64 , Issue.4 , pp. 616-622
    • Lim, L.1    Mine, Y.2    Tung, M.3
  • 28
    • 0037464436 scopus 로고    scopus 로고
    • Preparation and mechanical properties of edible pectin-soy flour films obtained in the absence or presence of transglutaminase
    • Mariniello L., Di Pierro P., Esposito C., Sorrentino A., Masi P., and Porta R. Preparation and mechanical properties of edible pectin-soy flour films obtained in the absence or presence of transglutaminase. Journal of Biotechnology 102 2 (2003) 191-198
    • (2003) Journal of Biotechnology , vol.102 , Issue.2 , pp. 191-198
    • Mariniello, L.1    Di Pierro, P.2    Esposito, C.3    Sorrentino, A.4    Masi, P.5    Porta, R.6
  • 29
    • 4143088311 scopus 로고    scopus 로고
    • Mechanical properties of biomimetic tissue adhesive based on the microbial transglutaminase-catalyzed crosslinking of gelatin
    • McDermott M., Chen T., Williams C., Markley K., and Payne G. Mechanical properties of biomimetic tissue adhesive based on the microbial transglutaminase-catalyzed crosslinking of gelatin. Biomacromolecules 5 4 (2004) 1270-1279
    • (2004) Biomacromolecules , vol.5 , Issue.4 , pp. 1270-1279
    • McDermott, M.1    Chen, T.2    Williams, C.3    Markley, K.4    Payne, G.5
  • 30
    • 5844240927 scopus 로고
    • Hydrophillic edible films: Modified procedure for water vapour permeability and explanation of thickness effects
    • Mchugh T.H., Avena-Bustillos R., and Krochta J.M. Hydrophillic edible films: Modified procedure for water vapour permeability and explanation of thickness effects. Journal of Food Science 58 (1993) 899-903
    • (1993) Journal of Food Science , vol.58 , pp. 899-903
    • Mchugh, T.H.1    Avena-Bustillos, R.2    Krochta, J.M.3
  • 31
    • 0031690193 scopus 로고    scopus 로고
    • Transglutaminase and its use for food processing
    • Motoki M., and Seguro K. Transglutaminase and its use for food processing. Trends in Food Science and Technology 9 5 (1998) 204-210
    • (1998) Trends in Food Science and Technology , vol.9 , Issue.5 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 32
    • 0000428509 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on thermal gelation of carp actomyosin sol
    • Ni S., Nozawa H., and Seki N. Effect of microbial transglutaminase on thermal gelation of carp actomyosin sol. Fisheries Science 64 3 (1998) 434-438
    • (1998) Fisheries Science , vol.64 , Issue.3 , pp. 434-438
    • Ni, S.1    Nozawa, H.2    Seki, N.3
  • 37
    • 0036320050 scopus 로고    scopus 로고
    • Using salt and microbial transglutaminase as binding agents in restructured fish products resembling hams
    • Ramirez J., Uresti R., Tellex S., and Vazquez M. Using salt and microbial transglutaminase as binding agents in restructured fish products resembling hams. Journal of Food Science 67 5 (2002) 1778-1784
    • (2002) Journal of Food Science , vol.67 , Issue.5 , pp. 1778-1784
    • Ramirez, J.1    Uresti, R.2    Tellex, S.3    Vazquez, M.4
  • 38
    • 34547838221 scopus 로고    scopus 로고
    • Gelatin-clay nanocomposites of improved properties
    • Rao Y. Gelatin-clay nanocomposites of improved properties. Polymer 48 (2007) 5369-5375
    • (2007) Polymer , vol.48 , pp. 5369-5375
    • Rao, Y.1
  • 39
    • 84986446950 scopus 로고
    • Microbial transglutaminase and epsilon-(gamma-glutamyl) lysine cross-link effects on elastic properties of kamaboko gels
    • Seguro K., Kumazawa Y., Ohtsuka T., Toiguchi S., and Motoki M. Microbial transglutaminase and epsilon-(gamma-glutamyl) lysine cross-link effects on elastic properties of kamaboko gels. Journal of Food Science 60 2 (1995) 305-311
    • (1995) Journal of Food Science , vol.60 , Issue.2 , pp. 305-311
    • Seguro, K.1    Kumazawa, Y.2    Ohtsuka, T.3    Toiguchi, S.4    Motoki, M.5
  • 40
    • 0036995672 scopus 로고    scopus 로고
    • Susceptibility of an industrial alpha-lactalbumin concentrate to cross-linking by microbial transglutaminase
    • Sharma R., Zakora M., and Qvist K. Susceptibility of an industrial alpha-lactalbumin concentrate to cross-linking by microbial transglutaminase. International Dairy Journal 12 12 (2002) 1005-1012
    • (2002) International Dairy Journal , vol.12 , Issue.12 , pp. 1005-1012
    • Sharma, R.1    Zakora, M.2    Qvist, K.3
  • 41
    • 0037165610 scopus 로고    scopus 로고
    • Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site
    • Shimba N., Shinohara M., Yokoyama K., Kashiwagi T., Ishikawa K., Ejima D., et al. Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Letters 517 1-3 (2002) 175-179
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , pp. 175-179
    • Shimba, N.1    Shinohara, M.2    Yokoyama, K.3    Kashiwagi, T.4    Ishikawa, K.5    Ejima, D.6
  • 42
    • 85007857382 scopus 로고
    • The functionalities of microbial transglutaminase for food application. 1. The effect of transglutaminase on texture of tofu
    • Soeda T., Ishii T., Yamazaki K., and Murase K. The functionalities of microbial transglutaminase for food application. 1. The effect of transglutaminase on texture of tofu. Journal of the Japanese Society for Food Science and Technology 42 4 (1995) 254-261
    • (1995) Journal of the Japanese Society for Food Science and Technology , vol.42 , Issue.4 , pp. 254-261
    • Soeda, T.1    Ishii, T.2    Yamazaki, K.3    Murase, K.4
  • 43
    • 0035037433 scopus 로고    scopus 로고
    • Influence of plasticizers on the properties of edible films prepared from fish water-soluble proteins
    • Tanaka M., Iwata K., Sanguandeekul R., Handa A., and Ishizaki S. Influence of plasticizers on the properties of edible films prepared from fish water-soluble proteins. Fisheries Science 67 2 (2001) 346-351
    • (2001) Fisheries Science , vol.67 , Issue.2 , pp. 346-351
    • Tanaka, M.1    Iwata, K.2    Sanguandeekul, R.3    Handa, A.4    Ishizaki, S.5
  • 46
    • 0037388170 scopus 로고    scopus 로고
    • Negative effect of combining microbial transglutaminase with low methoxyl pectins on the mechanical properties and colour attributes of fish gels
    • Uresti R., Ramirez J., Lopez-Arias N., and Vazquez M. Negative effect of combining microbial transglutaminase with low methoxyl pectins on the mechanical properties and colour attributes of fish gels. Food Chemistry 80 4 (2003) 551-556
    • (2003) Food Chemistry , vol.80 , Issue.4 , pp. 551-556
    • Uresti, R.1    Ramirez, J.2    Lopez-Arias, N.3    Vazquez, M.4
  • 47
    • 33845430799 scopus 로고    scopus 로고
    • Influence of transglutaminase-induced cross-linking on properties of fish gelatin films
    • Yi J.B., Kim Y.T., Bae H.J., Whiteside W.S., and Park H.J. Influence of transglutaminase-induced cross-linking on properties of fish gelatin films. Journal of Food Science 71 9 (2006) 376-383
    • (2006) Journal of Food Science , vol.71 , Issue.9 , pp. 376-383
    • Yi, J.B.1    Kim, Y.T.2    Bae, H.J.3    Whiteside, W.S.4    Park, H.J.5
  • 48
    • 34547596219 scopus 로고    scopus 로고
    • Influence of molecular architecture and melt rheological characteristic on the optical properties of LDPE blown films
    • Zhu H.J., Wang Y.F., Zhang X.Q., Su Y.F., Dong X., Chen Q.K., et al. Influence of molecular architecture and melt rheological characteristic on the optical properties of LDPE blown films. Polymer 48 17 (2007) 5098-5106
    • (2007) Polymer , vol.48 , Issue.17 , pp. 5098-5106
    • Zhu, H.J.1    Wang, Y.F.2    Zhang, X.Q.3    Su, Y.F.4    Dong, X.5    Chen, Q.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.