메뉴 건너뛰기




Volumn 2, Issue 4, 2007, Pages 462-468

Modification of β-lactoglobulin by microbial transglutaminase under high hydrostatic pressure Localization of reactive glutamine residues

Author keywords

Lactoglobulin milk protiens; Denaturation; Glutamine; High pressure treatment

Indexed keywords

BETA LACTOGLOBULIN; GLUTAMINE; PEPTIDE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRIGLYCINE; TRYPSIN;

EID: 34248390919     PISSN: 18606768     EISSN: None     Source Type: Journal    
DOI: 10.1002/biot.200600226     Document Type: Article
Times cited : (13)

References (23)
  • 1
    • 33645726443 scopus 로고    scopus 로고
    • Transglutaminase in dairy products: Chemistry, physics, applications
    • Jaros, D., Partschefeld, C., Henle, T., Rohm, H., Transglutaminase in dairy products: Chemistry, physics, applications. J. Texture Stud. 2006, 37, 113-156.
    • (2006) J. Texture Stud , vol.37 , pp. 113-156
    • Jaros, D.1    Partschefeld, C.2    Henle, T.3    Rohm, H.4
  • 2
    • 0001299553 scopus 로고    scopus 로고
    • Relationship between the crosslinking of caseins by transglutammase and the gel strength of yoghurt
    • Lauber, S., Henle, T., Klostermeyer, H., Relationship between the crosslinking of caseins by transglutammase and the gel strength of yoghurt. Eur. Food Res. Technol. 2000, 210, 305-309.
    • (2000) Eur. Food Res. Technol , vol.210 , pp. 305-309
    • Lauber, S.1    Henle, T.2    Klostermeyer, H.3
  • 3
    • 0036686486 scopus 로고    scopus 로고
    • Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yogurt
    • Lorenzen, P. C., Neve, H., Mautner, A., Schlimme, E., Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yogurt. Int. J. Dairy Technol. 2002, 55, 152-157.
    • (2002) Int. J. Dairy Technol , vol.55 , pp. 152-157
    • Lorenzen, P.C.1    Neve, H.2    Mautner, A.3    Schlimme, E.4
  • 5
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • Kuraishi, C., Yamazaki, K., Susa, Y., Transglutaminase: Its utilization in the food industry. Food Rev. Int. 2001, 17, 221-246.
    • (2001) Food Rev. Int , vol.17 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 6
    • 0041048223 scopus 로고    scopus 로고
    • Effect of enzymic crosslinking of milk proteins on the resulting properties of yogurt products
    • Lorenzen, P. C., Mautner, A., Schlimme, E., Effect of enzymic crosslinking of milk proteins on the resulting properties of yogurt products. Kieler Milchwirtsch. Forschungsber. 1999, 51, 89-97.
    • (1999) Kieler Milchwirtsch. Forschungsber , vol.51 , pp. 89-97
    • Lorenzen, P.C.1    Mautner, A.2    Schlimme, E.3
  • 7
    • 0035209417 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment of skim milk on the formation of epsilon-(gamma-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking
    • Sharma, R., Lorenzen, P. C., Qvist, K. B., Influence of transglutaminase treatment of skim milk on the formation of epsilon-(gamma-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. Int. Dairy J. 2001, 11, 785-793.
    • (2001) Int. Dairy J , vol.11 , pp. 785-793
    • Sharma, R.1    Lorenzen, P.C.2    Qvist, K.B.3
  • 8
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food applications
    • Da Jong, 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
    • Da Jong, G.A.H.1    Koppelman, S.J.2
  • 9
    • 33745609556 scopus 로고    scopus 로고
    • Enzymatic cross-linking of beta-lactoglobulin: Conformational properties using FTIR spectroscopy
    • Eissa, A. S., Pull, C., Kadla, J. F., Khan, S. A., Enzymatic cross-linking of beta-lactoglobulin: Conformational properties using FTIR spectroscopy. Biomacromolecules 2006, 7, 1707-1713.
    • (2006) Biomacromolecules , vol.7 , pp. 1707-1713
    • Eissa, A.S.1    Pull, C.2    Kadla, J.F.3    Khan, S.A.4
  • 10
    • 0142170734 scopus 로고    scopus 로고
    • Oligomerization of beta-lactoglobulin by microbial transglutaminase during high pressure treatment
    • Lauber, S., Noack, I., Klostermeyer, H., Henle, T., Oligomerization of beta-lactoglobulin by microbial transglutaminase during high pressure treatment. Eur. Food Res. Technol. 2001, 213, 246-247.
    • (2001) Eur. Food Res. Technol , vol.213 , pp. 246-247
    • Lauber, S.1    Noack, I.2    Klostermeyer, H.3    Henle, T.4
  • 11
    • 1542434817 scopus 로고    scopus 로고
    • Stability of microbial transglutaminase to high pressure treatment
    • Lauber, S., Noack, I., Klostermeyer, H., Henle, T., Stability of microbial transglutaminase to high pressure treatment. Eur. Food Res. Technol. 2001, 213, 273-276.
    • (2001) Eur. Food Res. Technol , vol.213 , pp. 273-276
    • Lauber, S.1    Noack, I.2    Klostermeyer, H.3    Henle, T.4
  • 12
    • 33645456647 scopus 로고    scopus 로고
    • Structural changes of microbial transglutaminase during thermal and high-pressure treatment
    • Menendez, O., Rawel, H., Schwarzenbolz, U., Henle, T., Structural changes of microbial transglutaminase during thermal and high-pressure treatment. J. Agric. Food Chem. 2006, 54, 1716-1721.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 1716-1721
    • Menendez, O.1    Rawel, H.2    Schwarzenbolz, U.3    Henle, T.4
  • 13
    • 0037114005 scopus 로고    scopus 로고
    • Crystal structure of microbial transglutaminase from Straptoverticillium mobaraense
    • Kashiwagi, T., Yokoyama, K., Ishikawa, K., Ono, K. et al., Crystal structure of microbial transglutaminase from Straptoverticillium mobaraense. J. Biol. Chem. 2002, 277, 44252-44260.
    • (2002) J. Biol. Chem , vol.277 , pp. 44252-44260
    • Kashiwagi, T.1    Yokoyama, K.2    Ishikawa, K.3    Ono, K.4
  • 14
    • 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
    • 0021774490 scopus 로고
    • In vitro introduction of glycosyl units at glutamines in beta-casein using transglutaminase
    • Yan, S. B., Wold, F., Neoglycoproteins: In vitro introduction of glycosyl units at glutamines in beta-casein using transglutaminase. Biochem. 1984, 23, 3759-3765.
    • (1984) Biochem , vol.23 , pp. 3759-3765
    • Yan, S.1    Wold, B.2    Neoglycoproteins, F.3
  • 17
    • 0242522959 scopus 로고    scopus 로고
    • Modification of glutamine and lysine residues in holo and apo alpha-lactalbumin with microbial transglutaminase
    • Nieuwenhuizen, W. F., Dekker, H. L., da Koning, L. J., Gröneveld, T. et al., Modification of glutamine and lysine residues in holo and apo alpha-lactalbumin with microbial transglutaminase. J. Agric. Food Chem. 2003, 51, 7132-7139.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 7132-7139
    • Nieuwenhuizen, W.F.1    Dekker, H.L.2    da Koning, L.J.3    Gröneveld, T.4
  • 18
    • 0037021366 scopus 로고    scopus 로고
    • Identification of the epsilon-(gamma-glutamyl)lysine cross-linking sites in alpha-lactalbumin polymerized by mammalian and microbial transglutaminases
    • Lee, D.-S., Matsumoto, S., Matsumura, Y., Mori, T., Identification of the epsilon-(gamma-glutamyl)lysine cross-linking sites in alpha-lactalbumin polymerized by mammalian and microbial transglutaminases. J. Agric. Food Chem. 2002, 50, 7412-7419.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 7412-7419
    • Lee, D.-S.1    Matsumoto, S.2    Matsumura, Y.3    Mori, T.4
  • 19
    • 0026510654 scopus 로고
    • Transglutamiase catalyses the modification of glutamine side chains in the C-terminal region of bovine beta-lactoglobulin
    • Coussons, P. J., Price, N. C., Kelly, S. M.; Smith, B. et al., Transglutamiase catalyses the modification of glutamine side chains in the C-terminal region of bovine beta-lactoglobulin. Biochem. J. 1992, 283, 803-806.
    • (1992) Biochem. J , vol.283 , pp. 803-806
    • Coussons, P.J.1    Price, N.C.2    Kelly, S.M.3    Smith, B.4
  • 20
    • 0842278662 scopus 로고    scopus 로고
    • Transglutaminase-mediated modification of glutamine and lysine residues in native bovine beta-lactoglobulin
    • Nieuwenhuizen, W. F., Dekker, H. L., Groeneveld, T., de Koster, C. G. et al. Transglutaminase-mediated modification of glutamine and lysine residues in native bovine beta-lactoglobulin. Biotechnol. Bioeng. 2004, 85, 248-258.
    • (2004) Biotechnol. Bioeng , vol.85 , pp. 248-258
    • Nieuwenhuizen, W.F.1    Dekker, H.L.2    Groeneveld, T.3    de Koster, C.G.4
  • 21
    • 0034807203 scopus 로고    scopus 로고
    • Enzymatic modification of beta-lactoglobulin with N-fatty-acyl-dipeptide by transglutaminase from Streptomyces mobaraense
    • Wada, E., Masuda, H., Imamura, K., Sakiyama, T. et al., Enzymatic modification of beta-lactoglobulin with N-fatty-acyl-dipeptide by transglutaminase from Streptomyces mobaraense. Biotechnol. Lett. 2001, 23, 1367-1372.
    • (2001) Biotechnol. Lett , vol.23 , pp. 1367-1372
    • Wada, E.1    Masuda, H.2    Imamura, K.3    Sakiyama, T.4
  • 22
    • 0026522680 scopus 로고
    • Factors that govern the specifity of transglutaminase-catalysed modification of proteins and peptides
    • Coussons, P. J., Price, N. C., Kelly, S. M., Smith, B. et al., Factors that govern the specifity of transglutaminase-catalysed modification of proteins and peptides. Biochem. J. 1992, 282, 929-930.
    • (1992) Biochem. J , vol.282 , pp. 929-930
    • Coussons, P.J.1    Price, N.C.2    Kelly, S.M.3    Smith, B.4
  • 23
    • 0034825616 scopus 로고    scopus 로고
    • PDB ID: 1B8E from http://www.pdb.org/; Oliveira, K. M., Valente-Masquita, V. L., Botelho, M. M., Sawyer, L. et al., Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Eur. J. Biochem. 2001, 268, 477-483.
    • PDB ID: 1B8E from http://www.pdb.org/; Oliveira, K. M., Valente-Masquita, V. L., Botelho, M. M., Sawyer, L. et al., Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Eur. J. Biochem. 2001, 268, 477-483.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.