메뉴 건너뛰기




Volumn 52, Issue 11, 2004, Pages 3617-3625

Interactive effects of microbial transglutaminase and recombinant cystatin on the mackerel and hairtail muscle protein

Author keywords

( glutamyl)lysine; Cathepsin; Fish Protein; MTGase; Recombinant Cystatin

Indexed keywords

CYSTATIN; LYSINE DERIVATIVE; MUSCLE PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; RECOMBINANT PROTEIN;

EID: 2542500050     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf035102y     Document Type: Article
Times cited : (8)

References (27)
  • 1
    • 0036812824 scopus 로고    scopus 로고
    • Microbial transglutaminase and recombinant cystatin effects on improving the quality of mackerel surimi
    • Hsieh, J. F.; Tsai, G. J.; Jiang, S. T. Microbial transglutaminase and recombinant cystatin effects on improving the quality of mackerel surimi. J. Food Sci. 2002, 67, 3120-3125.
    • (2002) J. Food Sci. , vol.67 , pp. 3120-3125
    • Hsieh, J.F.1    Tsai, G.J.2    Jiang, S.T.3
  • 2
    • 0030594809 scopus 로고    scopus 로고
    • Transglutaminases: Purification and activity assays
    • Wilhelm, B.; Meinhardt, A.; Seitz, J. Transglutaminases: purification and activity assays. J. Chromatogr. B 1996, 684, 163-177.
    • (1996) J. Chromatogr. B , vol.684 , pp. 163-177
    • Wilhelm, B.1    Meinhardt, A.2    Seitz, J.3
  • 3
    • 85008100751 scopus 로고
    • Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species
    • Asagami, T.; Ogiwara, M.; Wakameda, A.; Noguchi, S. F. Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species. Fish. Sci. 1995, 61, 267-272.
    • (1995) Fish. Sci. , vol.61 , pp. 267-272
    • Asagami, T.1    Ogiwara, M.2    Wakameda, A.3    Noguchi, S.F.4
  • 4
    • 85008002200 scopus 로고
    • Setting of transglutaminase-free actomyosin paste prepared from Alaska pollack surimi
    • Nowsad, A. A.; Kanoh, S.; Niwa, E. Setting of transglutaminase-free actomyosin paste prepared from Alaska pollack surimi. Fish. Sci. 1994, 60, 295-297.
    • (1994) Fish. Sci. , vol.60 , pp. 295-297
    • Nowsad, A.A.1    Kanoh, S.2    Niwa, E.3
  • 5
    • 0036812849 scopus 로고    scopus 로고
    • Improvement of hairtail surimi gel properties by NADPH-sulfite reductase, recombinant cystatin and microbial transglutaminase
    • Hsieh, J. F.; Tsai, G. J.; Jiang, S. T. Improvement of hairtail surimi gel properties by NADPH-sulfite reductase, recombinant cystatin and microbial transglutaminase. J. Food Sci. 2002, 67, 3152-3158.
    • (2002) J. Food Sci. , vol.67 , pp. 3152-3158
    • Hsieh, J.F.1    Tsai, G.J.2    Jiang, S.T.3
  • 6
    • 0027242118 scopus 로고
    • Human cystatin D: cDNA cloning, characterization of the Escherichia coli expressed inhibitor, and identification of the native protein in saliva
    • Freije, J. P.; Balbin, M.; Abrahamson, M.; Velasco, G.; Dalboge, H.; Grubb, A.; Lopez-Otin, C. Human cystatin D: cDNA cloning, characterization of the Escherichia coli expressed inhibitor, and identification of the native protein in saliva. J. Biol. Chem. 1993, 268, 15737-15744.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15737-15744
    • Freije, J.P.1    Balbin, M.2    Abrahamson, M.3    Velasco, G.4    Dalboge, H.5    Grubb, A.6    Lopez-Otin, C.7
  • 7
    • 0032415981 scopus 로고    scopus 로고
    • Molecular cloning, sequence analysis and expression distribution of rainbow trout (Oncorhynchus mykiss) cystatin C
    • Li, F.; An, H.; Seymour, T. A.; Bradford, C. S.; Morrissey, M. T.; Bailey, G. S.; Bames, D. W. Molecular cloning, sequence analysis and expression distribution of rainbow trout (Oncorhynchus mykiss) cystatin C. J. Comp. Biochem. Physiol. B 1998, 121, 135-143.
    • (1998) J. Comp. Biochem. Physiol. B , vol.121 , pp. 135-143
    • Li, F.1    An, H.2    Seymour, T.A.3    Bradford, C.S.4    Morrissey, M.T.5    Bailey, G.S.6    Bames, D.W.7
  • 8
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites for the cysteine proteinase inhibitors human cystatin C and chicken cystatin
    • Abrahamson, M.; Ritonja, A.; Brown, M. A.; Grubb, A.; Machleidt, W.; Barrett, A. J. Identification of the probable inhibitory reactive sites for the cysteine proteinase inhibitors human cystatin C and chicken cystatin. J. Biol. Chem. 1987, 262, 9688-9694.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9688-9694
    • Abrahamson, M.1    Ritonja, A.2    Brown, M.A.3    Grubb, A.4    Machleidt, W.5    Barrett, A.J.6
  • 9
    • 0024971526 scopus 로고
    • Chicken egg white cystatin-molecular cloning, nucleotide sequence, and tissue distribution
    • Colella, R.; Sakaguchi, Y.; Nagase, H.; Bird, J. W. C. Chicken egg white cystatin-molecular cloning, nucleotide sequence, and tissue distribution. J. Biol. Chem. 1989, 264, 17164-17169.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17164-17169
    • Colella, R.1    Sakaguchi, Y.2    Nagase, H.3    Bird, J.W.C.4
  • 10
    • 0024810026 scopus 로고
    • The cDNA structure and expression analysis of the genes for the cysteine proteinase inhibitor cystatin C and b2-microglobulin in rat brain
    • Cole, T.; Dickson, P. W.; Esnard, F.; Averill, S.; Risbridger, G. P.; Gauthier, F.; Schreiber, G. The cDNA structure and expression analysis of the genes for the cysteine proteinase inhibitor cystatin C and b2-microglobulin in rat brain. Eur. J. Biochem. 1989, 186, 35-42.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 35-42
    • Cole, T.1    Dickson, P.W.2    Esnard, F.3    Averill, S.4    Risbridger, G.P.5    Gauthier, F.6    Schreiber, G.7
  • 11
    • 0035118185 scopus 로고    scopus 로고
    • High High-level production of recombinant chicken cystatin by Pichia pastoris and its application in mackerel surimi
    • Chen, G. H.; Tang, S. J.; Chen, C. S.; Jiang, S. T. High High-level production of recombinant chicken cystatin by Pichia pastoris and its application in mackerel surimi. J. Agric. Food Chem. 2001, 49, 641-646.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 641-646
    • Chen, G.H.1    Tang, S.J.2    Chen, C.S.3    Jiang, S.T.4
  • 12
    • 0034025580 scopus 로고    scopus 로고
    • Technical approach to simplify the purification method and characterization of microbial transglutaminase produced from St. ladakanum
    • Ho, M. L.; Leu, S. Z.; Hsieh, J. F.; Jiang, S. T. Technical approach to simplify the purification method and characterization of microbial transglutaminase produced from St. ladakanum. J. Food Sci. 2000, 65, 76-80.
    • (2000) J. Food Sci. , vol.65 , pp. 76-80
    • Ho, M.L.1    Leu, S.Z.2    Hsieh, J.F.3    Jiang, S.T.4
  • 13
    • 0000326990 scopus 로고
    • Transglutaminase
    • Tabor, H., Tabor, C. W., Eds.; Academic Press: New York
    • Folk, J. E. Transglutaminase. In Method in Enzymology; Tabor, H., Tabor, C. W., Eds.; Academic Press: New York, 1970; Vol. 17, pp 889-894.
    • (1970) Method in Enzymology , vol.17 , pp. 889-894
    • Folk, J.E.1
  • 14
    • 77957773738 scopus 로고
    • Purification and characterization of proteinases identified as cathepsin L and L-like (58 kDa) from mackerel (Scomber australasics)
    • Lee, J. J.; Chen, H. C.; Jiang, S. T. Purification and characterization of proteinases identified as cathepsin L and L-like (58 kDa) from mackerel (Scomber australasics). Biosci., Biotechnol., Biochem. 1993, 57, 1470-1476.
    • (1993) Biosci., Biotechnol., Biochem. , vol.57 , pp. 1470-1476
    • Lee, J.J.1    Chen, H.C.2    Jiang, S.T.3
  • 15
    • 85007911421 scopus 로고
    • Studies on the control of denaturation of fish muscle proteins during frozen storage
    • Noguchi, S.; Matsumoto, J. J. Studies on the control of denaturation of fish muscle proteins during frozen storage. Nippon Suisan Gakkaishi 1970, 36, 1078-1081.
    • (1970) Nippon Suisan Gakkaishi , vol.36 , pp. 1078-1081
    • Noguchi, S.1    Matsumoto, J.J.2
  • 16
    • 50549198780 scopus 로고
    • A micro-Biuret method for estimating proteins
    • Itzhaki, R. F.; Gill, D. M. A micro-Biuret method for estimating proteins. Anal. Biochem. 1964, 9, 401-410.
    • (1964) Anal. Biochem. , vol.9 , pp. 401-410
    • Itzhaki, R.F.1    Gill, D.M.2
  • 17
    • 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.; Motoki, M. Formation of ε-(γ-glutamyl)lysine cross-link in cured horse mackerel meat induced by drying. J. Food Sci. 1993, 58, 1062-1064.
    • (1993) J. Food Sci. , vol.58 , pp. 1062-1064
    • Kumazawa, Y.1    Seguro, K.2    Takamura, M.3    Motoki, M.4
  • 18
    • 0020362141 scopus 로고
    • High-pressure liqid chromatographic procedure for the determination of ε-(γ-glutamyl)lysine in proteins
    • Griffin, M.; Wilson, J.; Lorand, L. High-pressure liqid chromatographic procedure for the determination of ε-(γ-glutamyl)lysine in proteins. Anal. Biochem. 1982, 124, 406-413.
    • (1982) Anal. Biochem. , vol.124 , pp. 406-413
    • Griffin, M.1    Wilson, J.2    Lorand, L.3
  • 19
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis of proteins: A Practical Approach
    • Hamer, B. D., Rickwood, D., Eds.; Oxford University Press: New York
    • Hames, B. D. An introduction to polyacrylamide gel electrophoresis of proteins: A Practical Approach. In Gel Electrophoresis of Proteins; Hamer, B. D., Rickwood, D., Eds.; Oxford University Press: New York, 1990; pp 1-91.
    • (1990) Gel Electrophoresis of Proteins , pp. 1-91
    • Hames, B.D.1
  • 20
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, C.; Arold, N.; Taube, D.; Ehrhardt, W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 1988, 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, C.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 21
    • 0000730592 scopus 로고    scopus 로고
    • Cross-linking of mackerel surimi by microbial transglutaminase and ultraviolet irradiation
    • Jiang, S. T.; Leu, S. Z.; Tsai, G. J. Cross-linking of mackerel surimi by microbial transglutaminase and ultraviolet irradiation. J. Agric. Food Chem. 1998, 46, 5278-5282.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 5278-5282
    • Jiang, S.T.1    Leu, S.Z.2    Tsai, G.J.3
  • 22
    • 0001143351 scopus 로고    scopus 로고
    • Effects of mackerel cathepsins L, L-like and calpain on the degradation of mackerel surimi
    • Ho, M. L.; Chen, G. H.; Jiang, S. T. Effects of mackerel cathepsins L, L-like and calpain on the degradation of mackerel surimi. Fish. Sci. 2000, 66, 558-568.
    • (2000) Fish. Sci. , vol.66 , pp. 558-568
    • Ho, M.L.1    Chen, G.H.2    Jiang, S.T.3
  • 23
    • 0033920043 scopus 로고    scopus 로고
    • Factors affecting transglutaminase activity catalysing polyamine conjugation to endogenous substrates in the entire chloroplast
    • Stefano, D. D.; Luca, D.; Massimiliano, D. M.; Paloma, M. R.; Donatella, S. F. Factors affecting transglutaminase activity catalysing polyamine conjugation to endogenous substrates in the entire chloroplast. Plant Physiol. Biochem. 2000, 38, 429-439.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 429-439
    • Stefano, D.D.1    Luca, D.2    Massimiliano, D.M.3    Paloma, M.R.4    Donatella, S.F.5
  • 24
    • 84986467761 scopus 로고
    • ε-(γ-Glutamyl)lysine cross-link distribution in foods as determined by improved method
    • Sakamoto, H.; Kumazawa, Y.; Kawajiri, H.; Motoki, M. ε-(γ -Glutamyl)lysine cross-link distribution in foods as determined by improved method. J. Food Sci. 1995, 60, 416-419.
    • (1995) J. Food Sci. , vol.60 , pp. 416-419
    • Sakamoto, H.1    Kumazawa, Y.2    Kawajiri, H.3    Motoki, M.4
  • 25
    • 0032052262 scopus 로고    scopus 로고
    • Purification, characterization, and gene cloning of transglutaminase from Streptoverticillium cinnamoneum CBS 683.68
    • Duran, R.; Junqua, M.; Schmitter, J. M.; Gancet, C.; Goulas, P. Purification, characterization, and gene cloning of transglutaminase from Streptoverticillium cinnamoneum CBS 683.68. Biochimie 1998, 80, 313-319.
    • (1998) Biochimie , vol.80 , pp. 313-319
    • Duran, R.1    Junqua, M.2    Schmitter, J.M.3    Gancet, C.4    Goulas, P.5
  • 26
    • 84986465415 scopus 로고
    • Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture
    • Sakamoto, H.; Kumazawa, Y.; Toiguchi, S.; Seguro, K.; Soeda, T.; Motoki, M. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. J. Food Sci. 1995, 60, 300-304.
    • (1995) J. Food Sci. , vol.60 , pp. 300-304
    • Sakamoto, H.1    Kumazawa, Y.2    Toiguchi, S.3    Seguro, K.4    Soeda, T.5    Motoki, M.6
  • 27
    • 84986446950 scopus 로고
    • Microbial transglutaminase and ε-(γ-glutamyl)lysine cross-link effects on elastic properties of kamaboko gels
    • Seguro, K.; Kumazawa, Y.; Ohtsuka, T.; Toiguchi, S.; Motoki, M. Microbial transglutaminase and ε-(γ-glutamyl)lysine cross-link effects on elastic properties of kamaboko gels. J. Food Sci. 1995, 60, 305-311.
    • (1995) J. Food Sci. , vol.60 , pp. 305-311
    • Seguro, K.1    Kumazawa, Y.2    Ohtsuka, T.3    Toiguchi, S.4    Motoki, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.