메뉴 건너뛰기




Volumn 475, Issue 1, 2015, Pages 69-74

Monitoring of transglutaminase crosslinking reaction by 1H NMR spectroscopy on model substrates

Author keywords

1H NMR; Crosslinking degree; Microbial transglutaminase; Model substrates; ( glutamyl) lysine

Indexed keywords

AMINO ACIDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RESONANCE;

EID: 84930196125     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2014.12.066     Document Type: Article
Times cited : (5)

References (20)
  • 1
    • 0029608871 scopus 로고
    • Microbial transglutaminase - a review of its production and application in food processing
    • Zhu Y., Rinzema A., Tramper J., Bol J. Microbial transglutaminase - a review of its production and application in food processing. Appl. Microbiol. Biotechnol. 1995, 44:277-282.
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 277-282
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4
  • 2
    • 1842454749 scopus 로고    scopus 로고
    • Tissue transglutaminase acylation: proposed role of conserved active site Tyr and Trp residues revealed by molecular modeling of peptide substrate binding
    • Chica R.A., Gagnon P., Keillor J.W., Pelletier J.N. Tissue transglutaminase acylation: proposed role of conserved active site Tyr and Trp residues revealed by molecular modeling of peptide substrate binding. Protein Sci. 2004, 13:979-991.
    • (2004) Protein Sci. , vol.13 , pp. 979-991
    • Chica, R.A.1    Gagnon, P.2    Keillor, J.W.3    Pelletier, J.N.4
  • 3
    • 0014670232 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase: VI. Order of substrate addition
    • Folk J.E. Mechanism of action of guinea pig liver transglutaminase: VI. Order of substrate addition. J. Biol. Chem. 1969, 244:3707-3713.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3707-3713
    • Folk, J.E.1
  • 4
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: nature's biological glues
    • Griffin M., Casadio R., Bergamini C.M. Transglutaminases: nature's biological glues. Biochem. J. 2002, 368:377-396.
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 5
    • 47649091159 scopus 로고    scopus 로고
    • Transglutaminases: widespread cross-linking enzymes in plants
    • Serafini-Fracassini D., Del Duca S. Transglutaminases: widespread cross-linking enzymes in plants. Ann. Bot. 2008, 102:145-152.
    • (2008) Ann. Bot. , vol.102 , pp. 145-152
    • Serafini-Fracassini, D.1    Del Duca, S.2
  • 6
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama K., Nio N., Kikuchi Y. Properties and applications of microbial transglutaminase. Appl. Microbiol. Biotechnol. 2004, 64:447-454.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 7
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: impact on food applications
    • DeJong G.A.H., Koppelman S.J. Transglutaminase catalyzed reactions: impact on food applications. J. Food Sci. 2002, 67:2798-2806.
    • (2002) J. Food Sci. , vol.67 , pp. 2798-2806
    • DeJong, G.A.H.1    Koppelman, S.J.2
  • 8
    • 0000633489 scopus 로고    scopus 로고
    • Recent research trends in transglutaminase technology for food processing
    • Motoki M., Kumazawa Y. Recent research trends in transglutaminase technology for food processing. Food Sci. Technol. Res. 2000, 6:151-160.
    • (2000) Food Sci. Technol. Res. , vol.6 , pp. 151-160
    • Motoki, M.1    Kumazawa, Y.2
  • 9
    • 0032852974 scopus 로고    scopus 로고
    • Rapid, single-step procedure for the identification of transglutaminase-mediated isopeptide crosslinks in amino acid digests
    • Miller M.L., Johnson G.V.W. Rapid, single-step procedure for the identification of transglutaminase-mediated isopeptide crosslinks in amino acid digests. J. Chromatogr. B: Biomed. Sci. Appl. 1999, 732:65-72.
    • (1999) J. Chromatogr. B: Biomed. Sci. Appl. , vol.732 , pp. 65-72
    • Miller, M.L.1    Johnson, G.V.W.2
  • 10
    • 84986467761 scopus 로고
    • ε-(γ-Glutamyl)lysine crosslink distribution in foods as determined by improved method
    • Sakamoto H., Kumazawa Y., Kawajiri H., Motoki M. ε-(γ-Glutamyl)lysine crosslink distribution in foods as determined by improved method. J. Food Sci. 1995, 60:416-420.
    • (1995) J. Food Sci. , vol.60 , pp. 416-420
    • Sakamoto, H.1    Kumazawa, Y.2    Kawajiri, H.3    Motoki, M.4
  • 11
    • 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., Brandl F., Neidhart S., 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). J. Agric. Food Chem. 2005, 53:2830-2837.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 2830-2837
    • Schafer, C.1    Schott, M.2    Brandl, F.3    Neidhart, S.4    Carle, R.5
  • 12
    • 0037062850 scopus 로고    scopus 로고
    • Physicochemical study of k- and β-casein dispersions and the effect of cross-linking by transglutaminase
    • De Kruif C.G., Tuinier R., Holt C., Timmins P.A., Rollema H.S. Physicochemical study of k- and β-casein dispersions and the effect of cross-linking by transglutaminase. Langmuir 2002, 18:4885-4891.
    • (2002) Langmuir , vol.18 , pp. 4885-4891
    • De Kruif, C.G.1    Tuinier, R.2    Holt, C.3    Timmins, P.A.4    Rollema, H.S.5
  • 14
    • 0036348648 scopus 로고    scopus 로고
    • Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein
    • Dinnella C., Gargaro M.T., Rossano R., Monteleone E. Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein. Food Chem. 2002, 78:363-368.
    • (2002) Food Chem. , vol.78 , pp. 363-368
    • Dinnella, C.1    Gargaro, M.T.2    Rossano, R.3    Monteleone, E.4
  • 15
    • 0034567635 scopus 로고    scopus 로고
    • Comparison of substrate specificities of transglutaminases using synthetic peptides as acyl donors
    • Ohtsuka T., Ota M., Nio N., Motoki M. Comparison of substrate specificities of transglutaminases using synthetic peptides as acyl donors. Biosci. Biotechnol. Biochem. 2000, 64:2608-2613.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2608-2613
    • Ohtsuka, T.1    Ota, M.2    Nio, N.3    Motoki, M.4
  • 16
    • 0029147474 scopus 로고
    • Substrate requirements for transglutaminases: influence of the amino acid residue preceding the amine donor lysine in a native protein
    • Grootjans J.J., Groenen P.J.T.A., de Jong W.W. Substrate requirements for transglutaminases: influence of the amino acid residue preceding the amine donor lysine in a native protein. J. Biol. Chem. 1995, 270:22855-22858.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22855-22858
    • Grootjans, J.J.1    Groenen, P.J.T.A.2    de Jong, W.W.3
  • 17
    • 78651168687 scopus 로고
    • Structural requirements of specific substrates for guinea pig liver transglutaminase
    • Folk J.E., Cole P.W. Structural requirements of specific substrates for guinea pig liver transglutaminase. J. Biol. Chem. 1965, 240:2951-2960.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2951-2960
    • Folk, J.E.1    Cole, P.W.2
  • 18
    • 0014011698 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase: I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity
    • Folk J.E., Cole P.W. Mechanism of action of guinea pig liver transglutaminase: I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. J. Biol. Chem. 1966, 241:5518-5525.
    • (1966) J. Biol. Chem. , vol.241 , pp. 5518-5525
    • Folk, J.E.1    Cole, P.W.2
  • 20
    • 62549155305 scopus 로고    scopus 로고
    • Assessment of cross-linking in combined cross-linked soy protein isolate gels by microbial transglutaminase and maillard reaction
    • Gan C.Y., Cheng L.H., Easa A.M. Assessment of cross-linking in combined cross-linked soy protein isolate gels by microbial transglutaminase and maillard reaction. J. Food Sci. 2009, 74:C141-C146.
    • (2009) J. Food Sci. , vol.74 , pp. C141-C146
    • Gan, C.Y.1    Cheng, L.H.2    Easa, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.