메뉴 건너뛰기




Volumn 76, Issue 3, 2007, Pages 455-462

Differentiation in improvements of gel strength in chicken and beef sausages induced by transglutaminase

Author keywords

Beef; Breaking strength; Chicken; Crosslinking; Texture; Transglutaminase

Indexed keywords


EID: 34247132589     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2007.01.002     Document Type: Article
Times cited : (57)

References (35)
  • 1
    • 34247138284 scopus 로고    scopus 로고
    • Ahhmed, M. A., Kawahara, S., Soeda, T., & Muguruma, M. (2005). The improvement of gel strength of sausages prepared from three types of meat with microbial transglutaminase. In Proceeding of the 51th international congress of meat science and technology (p. 54). 7-12 August, 2005, Baltimore, Maryland, USA.
  • 3
    • 84882589540 scopus 로고
    • Physical properties of soy bean and board bean 11S globulin gels formed by transglutaminase reaction
    • 493
    • Chanyongvorakul Y., Matsumura Y., Nonaka M., Motoki M., and Mori T. Physical properties of soy bean and board bean 11S globulin gels formed by transglutaminase reaction. Journal of Food Science 60 (1995) 483-488 493
    • (1995) Journal of Food Science , vol.60 , pp. 483-488
    • Chanyongvorakul, Y.1    Matsumura, Y.2    Nonaka, M.3    Motoki, M.4    Mori, T.5
  • 4
    • 18844367780 scopus 로고    scopus 로고
    • Effects of salt and transglutaminase (TG) level and processing conditions on quality characteristics of phosphate-free, cooked, restructured pork shoulder
    • Dimitrakopoulou M.A., Ambrosiadis J.A., Zetou F.K., and Bloukas J.G. Effects of salt and transglutaminase (TG) level and processing conditions on quality characteristics of phosphate-free, cooked, restructured pork shoulder. Meat Science 70 (2005) 743-749
    • (2005) Meat Science , vol.70 , pp. 743-749
    • Dimitrakopoulou, M.A.1    Ambrosiadis, J.A.2    Zetou, F.K.3    Bloukas, J.G.4
  • 6
    • 29544444660 scopus 로고    scopus 로고
    • Effect of existence of exogenous protein on physicochemical properties of heat- and transglutaminase-induced bovine collagen-peptide gel
    • Erwanto Y., Kawahara S., Katayama K., Ahhmed M.A., Yamauchi K., Chin K.B., et al. Effect of existence of exogenous protein on physicochemical properties of heat- and transglutaminase-induced bovine collagen-peptide gel. Journal of Food Science 70 (2005) E505-E509
    • (2005) Journal of Food Science , vol.70
    • Erwanto, Y.1    Kawahara, S.2    Katayama, K.3    Ahhmed, M.A.4    Yamauchi, K.5    Chin, K.B.6
  • 11
    • 0033864267 scopus 로고    scopus 로고
    • Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollack surimi
    • Jiang S.T., Hsieh J.F., Ho M.L., and Chung Y.C. Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollack surimi. Journal of Food Science 65 (2000) 694-699
    • (2000) Journal of Food Science , vol.65 , pp. 694-699
    • Jiang, S.T.1    Hsieh, J.F.2    Ho, M.L.3    Chung, Y.C.4
  • 12
    • 2542500050 scopus 로고    scopus 로고
    • Interactive effects of microbial transglutaminase and recombinant cystatin on the mackerel and hairtail muscle protein
    • Jiang S.T., Hsieh J.F., and Tsai G.J. Interactive effects of microbial transglutaminase and recombinant cystatin on the mackerel and hairtail muscle protein. Journal of Agricultural Food Chemistry 52 (2004) 3617-3625
    • (2004) Journal of Agricultural Food Chemistry , vol.52 , pp. 3617-3625
    • Jiang, S.T.1    Hsieh, J.F.2    Tsai, G.J.3
  • 13
    • 28844441960 scopus 로고    scopus 로고
    • Microbial transglutaminase improves the properties of meat protein and sausages texture manufactured with low-quality pork loin
    • Katayama K., Chin K.B., Yoshihara S., and Muguruma M. Microbial transglutaminase improves the properties of meat protein and sausages texture manufactured with low-quality pork loin. Asian-Australian Journal of Animal Science 19 (2006) 102-108
    • (2006) Asian-Australian Journal of Animal Science , vol.19 , pp. 102-108
    • Katayama, K.1    Chin, K.B.2    Yoshihara, S.3    Muguruma, M.4
  • 15
    • 84893758056 scopus 로고
    • Formation of ε-(γ-glutamyl)lysine cross-link in cured horse mackerel meat induced by drying
    • Kumazawa Y., Seguro K., Takamura M., and Motoki M. Formation of ε-(γ-glutamyl)lysine cross-link in cured horse mackerel meat induced by drying. Journal of Food Science 58 (1993) 1062-1064
    • (1993) Journal of Food Science , vol.58 , pp. 1062-1064
    • Kumazawa, Y.1    Seguro, K.2    Takamura, M.3    Motoki, M.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 17
    • 84986522809 scopus 로고
    • A review: Enzymatic cross-linking of proteins applicable to food
    • Matheis G., and Whitaker J. A review: Enzymatic cross-linking of proteins applicable to food. Journal of Food Biochemistry 11 (1987) 309-327
    • (1987) Journal of Food Biochemistry , vol.11 , pp. 309-327
    • Matheis, G.1    Whitaker, J.2
  • 18
    • 21544478512 scopus 로고    scopus 로고
    • Technomic Publishing Company, Pennsylvania, USA pp. xi-xiv
    • Mazza G. Functional foods (1998), Technomic Publishing Company, Pennsylvania, USA pp. xi-xiv
    • (1998) Functional foods
    • Mazza, G.1
  • 19
    • 0002434049 scopus 로고
    • Muscle differentiation and meat quality
    • Ralston L. (Ed), Elsevier applied science, London, UK
    • Monin G., and Ouali A. Muscle differentiation and meat quality. In: Ralston L. (Ed). developments in meat science-5 (1991), Elsevier applied science, London, UK 89-157
    • (1991) developments in meat science-5 , pp. 89-157
    • Monin, G.1    Ouali, A.2
  • 20
    • 0000927288 scopus 로고
    • Crosslinking between different food proteins by transglutaminase
    • Motoki M., and Nio N. Crosslinking between different food proteins by transglutaminase. Journal of Food Science 48 (1983) 5615-5666
    • (1983) Journal of Food Science , vol.48 , pp. 5615-5666
    • Motoki, M.1    Nio, N.2
  • 21
    • 34247106176 scopus 로고    scopus 로고
    • Muguruma, M., Tsuruoka, K., Fujino, H., Kawahara, S., Yamauchi, K., Matsumura, S. & Soeda, T. (1999). Gel strength enhancement of sausages by treating with microbial transglutaminase. In Proceeding of the 45th international congress of meat science and technology (pp. 138-139). 1-6 August, 1999, Yokohama, Japan.
  • 22
    • 0037207551 scopus 로고    scopus 로고
    • Soybean and milk protein modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate
    • Muguruma M., Tsuruoka K., Katayama K., Erwanto Y., Kawahara S., Yamauchi K., et al. Soybean and milk protein modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Science 63 (2003) 191-197
    • (2003) Meat Science , vol.63 , pp. 191-197
    • Muguruma, M.1    Tsuruoka, K.2    Katayama, K.3    Erwanto, Y.4    Kawahara, S.5    Yamauchi, K.6
  • 23
    • 0003028825 scopus 로고
    • Humectants improve myosin extractability and water activity of raw, cured intermediate moisture meats
    • Muguruma M., Nishimura T., Umetsu R., Goto I., and Yamauchi M. Humectants improve myosin extractability and water activity of raw, cured intermediate moisture meats. Meat Science 20 (1987) 179-194
    • (1987) Meat Science , vol.20 , pp. 179-194
    • Muguruma, M.1    Nishimura, T.2    Umetsu, R.3    Goto, I.4    Yamauchi, M.5
  • 24
    • 0012797736 scopus 로고
    • The technology of cooked cured products
    • Müller W.D. The technology of cooked cured products. Fleischwirtschaft 69 (1989) 1425-1428
    • (1989) Fleischwirtschaft , vol.69 , pp. 1425-1428
    • Müller, W.D.1
  • 26
  • 27
    • 0037207560 scopus 로고    scopus 로고
    • Binding and textural puppetries of beef gels processed with κ-carrageenan, egg albumin and microbial transglutaminase
    • Pietrasik Z. Binding and textural puppetries of beef gels processed with κ-carrageenan, egg albumin and microbial transglutaminase. Meat Science 63 (2003) 317-324
    • (2003) Meat Science , vol.63 , pp. 317-324
    • Pietrasik, Z.1
  • 28
    • 84987312149 scopus 로고
    • Effects of salt levels in prerigor blends and cooked sausages on water binding, released fat and pH
    • Poulanne E.J., and Terrell R.N. Effects of salt levels in prerigor blends and cooked sausages on water binding, released fat and pH. Journal of Food Science 48 (1983) 1022-1024
    • (1983) Journal of Food Science , vol.48 , pp. 1022-1024
    • Poulanne, E.J.1    Terrell, R.N.2
  • 29
    • 9644296525 scopus 로고
    • Cookery of muscle food
    • Kinsman D.M., Kotula A.W., and Breidenstein B.C. (Eds), Chapman & Hall, Inc., New York, USA
    • Resurreccion A.V.A. Cookery of muscle food. In: Kinsman D.M., Kotula A.W., and Breidenstein B.C. (Eds). Muscle foods (1994), Chapman & Hall, Inc., New York, USA 406-429
    • (1994) Muscle foods , pp. 406-429
    • Resurreccion, A.V.A.1
  • 30
    • 0036216086 scopus 로고    scopus 로고
    • Emulsion stability and water uptake ability of chicken breast muscle proteins as affected by microbial transglutaminase
    • Ruiz-Carrascal J., and Regenstein J. Emulsion stability and water uptake ability of chicken breast muscle proteins as affected by microbial transglutaminase. Journal of Food Science 67 (2002) 734-739
    • (2002) Journal of Food Science , vol.67 , pp. 734-739
    • Ruiz-Carrascal, J.1    Regenstein, J.2
  • 31
    • 84986465415 scopus 로고
    • Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture
    • Sakamoto H., Kumazawa Y., Seguro K., Soeda T., and Motoki M. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. Journal of Food Science 60 (1995) 300-304
    • (1995) Journal of Food Science , vol.60 , pp. 300-304
    • Sakamoto, H.1    Kumazawa, Y.2    Seguro, K.3    Soeda, T.4    Motoki, M.5
  • 32
    • 17144368764 scopus 로고    scopus 로고
    • Identification and quantification of ε-(γ-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS)
    • Schafer C., Schott M., Brandle F., Neidhart S., and Carle R. Identification and quantification of ε-(γ-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS). Journal of Agricultural Food Chemistry 53 (2005) 2830-2837
    • (2005) Journal of Agricultural Food Chemistry , vol.53 , pp. 2830-2837
    • Schafer, C.1    Schott, M.2    Brandle, F.3    Neidhart, S.4    Carle, R.5
  • 33
    • 0034413312 scopus 로고    scopus 로고
    • Evaluation of transglutaminase on the quality of low-salt chicken meat-balls
    • Tseng T.F., Liu D.C., and Chen M.T. Evaluation of transglutaminase on the quality of low-salt chicken meat-balls. Meat Science 55 (2000) 427-431
    • (2000) Meat Science , vol.55 , pp. 427-431
    • Tseng, T.F.1    Liu, D.C.2    Chen, M.T.3
  • 34
    • 84893592478 scopus 로고
    • ε-(γ-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25 °C
    • Tsukamasa Y., Sato K., Shimizu Y., Imai C., Sugiyama S., Minegishi Y., et al. ε-(γ-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25 °C. Journal of Food Science 58 (1993) 785-787
    • (1993) Journal of Food Science , vol.58 , pp. 785-787
    • Tsukamasa, Y.1    Sato, K.2    Shimizu, Y.3    Imai, C.4    Sugiyama, S.5    Minegishi, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.