메뉴 건너뛰기




Volumn 52, Issue 11, 2004, Pages 3612-3616

Glycosylation modification improved the characteristics of recombinant chicken cystatin and its application on mackerel surimi

Author keywords

Characterization; Chicken cystatin; Glycosylation modification; Pichia pastoris X 33; Surimi

Indexed keywords

CYSTATIN; CYSTEINE PROTEINASE; GLYCOCYSTATIN; MANNOSE; POLYSACCHARIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 2542450374     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0351016     Document Type: Article
Times cited : (12)

References (29)
  • 1
    • 0347366930 scopus 로고    scopus 로고
    • Effect of proteinases on the meat texture and seafood quality
    • Jiang, S. T. Effect of proteinases on the meat texture and seafood quality (a review). Food Sci. Agric. Chem. 2000, 2, 55-74.
    • (2000) Food Sci. Agric. Chem. , vol.2 , pp. 55-74
    • Jiang, S.T.1
  • 2
    • 0012204094 scopus 로고    scopus 로고
    • Enzymes and their effects on seafood texture
    • Haard, N. F., Simpson, B. K., Eds.; Marcel Dekker: New York; Chapter 15
    • Jiang, S. T. Enzymes and their Effects on Seafood Texture. In Seafood Enzymes; Haard, N. F., Simpson, B. K., Eds.; Marcel Dekker: New York, 2000; Chapter 15, pp 411-450.
    • (2000) Seafood Enzymes , pp. 411-450
    • Jiang, S.T.1
  • 3
    • 0030968742 scopus 로고    scopus 로고
    • Mackerel cathepsins B and L effects on thermal degradation of surimi
    • Jiang, S. T.; Lee, B. L.; Tsao, C. Y.; Lee, J. J. Mackerel cathepsins B and L effects on thermal degradation of surimi. J. Food Sci. 1997, 62, 310-315.
    • (1997) J. Food Sci. , vol.62 , pp. 310-315
    • Jiang, S.T.1    Lee, B.L.2    Tsao, C.Y.3    Lee, J.J.4
  • 4
    • 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
  • 5
    • 84919617127 scopus 로고
    • Cathepsin degradation of Pacific whiting surimi proteins
    • An, H.; Weerasinghe, V.; Seymour, T. A.; Morrissey, M. T. Cathepsin degradation of Pacific whiting surimi proteins. J. Food Sci. 1994, 59, 1013-1017 and 1033.
    • (1994) J. Food Sci. , vol.59 , pp. 1013-1017
    • An, H.1    Weerasinghe, V.2    Seymour, T.A.3    Morrissey, M.T.4
  • 6
    • 21444438718 scopus 로고    scopus 로고
    • Marked proteolysis occurring during thermal gel formation of the minced meat from matured chum salmon and restraining effect of protease inhibitor on geldegradation
    • Yamashita, M.; Henmi, H.; Ueda, T.; Obara, M.; Taro, T.; Nishioka, F.; Konagaya, S. Marked proteolysis occurring during thermal gel formation of the minced meat from matured chum salmon and restraining effect of protease inhibitor on geldegradation. Nippon Suisan Gakkaishi 1996, 62, 934-938.
    • (1996) Nippon Suisan Gakkaishi , vol.62 , pp. 934-938
    • Yamashita, M.1    Henmi, H.2    Ueda, T.3    Obara, M.4    Taro, T.5    Nishioka, F.6    Konagaya, S.7
  • 7
    • 0034471044 scopus 로고    scopus 로고
    • Inhibition of thermal degradation of mackerel surimi by pig plasma protein and L-kininogen
    • Lee, J. J.; Tzeng, S. S.; Wu, J.; Jiang, S. T. Inhibition of thermal degradation of mackerel surimi by pig plasma protein and L-kininogen. J. Food Sci. 2000, 65, 1124-1129.
    • (2000) J. Food Sci. , vol.65 , pp. 1124-1129
    • Lee, J.J.1    Tzeng, S.S.2    Wu, J.3    Jiang, S.T.4
  • 9
    • 0023268643 scopus 로고
    • The cystatins: A new class of peptidase inhibitors
    • Barrett, A. J. The cystatins: a new class of peptidase inhibitors. Trends Biochem. Sci. 1987, 12, 193-196.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 193-196
    • Barrett, A.J.1
  • 10
    • 0034073998 scopus 로고    scopus 로고
    • Purification and characterization of low molecular weight kininogen from pig plasma
    • Lee, J. J.; Tzeng, S. S.; Jiang, S. T. Purification and characterization of low molecular weight kininogen from pig plasma. J. Food Sci. 2000, 65, 81-86.
    • (2000) J. Food Sci. , vol.65 , pp. 81-86
    • Lee, J.J.1    Tzeng, S.S.2    Jiang, S.T.3
  • 11
    • 0035118185 scopus 로고    scopus 로고
    • 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-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
    • 0037063435 scopus 로고    scopus 로고
    • 108T) on the freezing stability of recombinant chicken cystatin overexpressed in Pichia pastoris X-33
    • 108T) on the freezing stability of recombinant chicken cystatin overexpressed in Pichia pastoris X-33. J. Agric. Food Chem. 2002, 50, 5313-5317.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 5313-5317
    • Jiang, S.T.1    Chen, G.H.2    Tang, S.J.3    Chen, C.S.4
  • 13
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg, J. M.; Vedvick, T. S.; Raschke, W. C. Recent advances in the expression of foreign genes in Pichia pastoris. Bio/Technol. 1993, 11, 905-910.
    • (1993) Bio/Technol. , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 14
    • 0002184856 scopus 로고
    • Strategies for optimizing protein expression and secretion in the methylotrophic yeast Pichia pastoris
    • American Society for Microbiology: Washington, DC
    • Sreekrishna, K. Strategies for optimizing protein expression and secretion in the methylotrophic yeast Pichia pastoris. Industrial Microorganisms: Basic and Applied Molecular Genetics; American Society for Microbiology: Washington, DC, 1993; pp 119-126.
    • (1993) Industrial Microorganisms: Basic and Applied Molecular Genetics , pp. 119-126
    • Sreekrishna, K.1
  • 15
    • 0031579445 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris glyceraidehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter
    • Waterham, H. R.; Digan, M. E.; Koutz, P. J.; Lair, S. V.; Cregg, J. M. Isolation of the Pichia pastoris glyceraidehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene 1997, 186, 37-44.
    • (1997) Gene , vol.186 , pp. 37-44
    • Waterham, H.R.1    Digan, M.E.2    Koutz, P.J.3    Lair, S.V.4    Cregg, J.M.5
  • 16
    • 0033937731 scopus 로고    scopus 로고
    • Overexpression of the soluble form of chicken cystatin in Escherichia coli and its purification
    • Chen, G. H.; Tang, S. J.; Chen, C. S.; Jiang, S. T. Overexpression of the soluble form of chicken cystatin in Escherichia coli and its purification. J. Agric. Food Chem. 2000, 48, 2602-2607.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 2602-2607
    • Chen, G.H.1    Tang, S.J.2    Chen, C.S.3    Jiang, S.T.4
  • 17
    • 0037134640 scopus 로고    scopus 로고
    • Enhanced expression of chicken cystatin as a thioredoxin fusion form in Escherichia coli AD494(DE3)pLysS and its effect on the prevention of surimi gel softening
    • Jiang, S. T.; Tzeng, S. S.; Wu, W. T.; Chen, G. H. Enhanced expression of chicken cystatin as a thioredoxin fusion form in Escherichia coli AD494(DE3)pLysS and its effect on the prevention of surimi gel softening. J. Agric. Food Chem. 2002, 50, 3731-3737.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 3731-3737
    • Jiang, S.T.1    Tzeng, S.S.2    Wu, W.T.3    Chen, G.H.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 1970, 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gel including isoelectric focusing gels with clear background at nanogram sensitivity using coomassie brilliant blue G-250 and R-250
    • Neuhoff, V.; Arold, N.; Taube, D.; Ehrhardt, W. Improved staining of proteins in polyacrylamide gel 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, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 20
    • 0014548372 scopus 로고
    • Glycoprotein staining following electrophoresis on acrylamide gels
    • Zachariou, R. M.; Zell, T. E.; Morrison, J. M.; Woodlock, J. J. Glycoprotein staining following electrophoresis on acrylamide gels. Anal. Biochem. 1969, 30, 148-152.
    • (1969) Anal. Biochem. , vol.30 , pp. 148-152
    • Zachariou, R.M.1    Zell, T.E.2    Morrison, J.M.3    Woodlock, J.J.4
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M.; Gilles, K. A.; Hamilton, J. K.; Rebers, P. A.; Smith, F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1956, 28, 350-354.
    • (1956) Anal. Chem. , vol.28 , pp. 350-354
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 24
    • 0019765848 scopus 로고
    • Cathepsin B cathepsin H, and cathepsin L
    • Barrett, A. J.; Kirschke, H. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 1981, 80, 535-561.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 25
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W.; Engh, R. A.; Musil, D.; Thiele, U.; Huber, R.; Karshikov, A.; Brzin, J.; Kos, J.; Turk, V. The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 1988, 7, 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.A.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 26
    • 0003357057 scopus 로고    scopus 로고
    • Effects of polymannosylation of recombinant cystatin C in yeast on its stability and activity
    • Nakamura, S.; Ogawa, M.; Nakai, S. Effects of polymannosylation of recombinant cystatin C in yeast on its stability and activity. J. Agric. Food Chem. 1998, 46, 2882-2887.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2882-2887
    • Nakamura, S.1    Ogawa, M.2    Nakai, S.3
  • 27
    • 0027278928 scopus 로고
    • Hyperglycosylation of hen egg white lysozyme in yeast
    • Nakamura, S.; Takasaki, H.; Kobayashi, K.; Kato, A. Hyperglycosylation of hen egg white lysozyme in yeast. J. Biol. Chem. 1993, 268, 12706-12712.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12706-12712
    • Nakamura, S.1    Takasaki, H.2    Kobayashi, K.3    Kato, A.4
  • 28
    • 0034739288 scopus 로고    scopus 로고
    • Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification
    • Kato, A.; Nakamura, S.; Ban, M.; Azakami, H.; Yutani, K. Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification. Biochim. Biophys. Acta 2000, 1481, 88-96.
    • (2000) Biochim. Biophys. Acta , vol.1481 , pp. 88-96
    • Kato, A.1    Nakamura, S.2    Ban, M.3    Azakami, H.4    Yutani, K.5
  • 29
    • 0032496403 scopus 로고    scopus 로고
    • Application of polymannosylated cystatin to surimi from roe-herring to prevent gel weakening
    • Nakamura, S.; Ogawa, M.; Saito, M.; Nakai, S. Application of polymannosylated cystatin to surimi from roe-herring to prevent gel weakening. FEBS Lett. 1998, 427, 252-254.
    • (1998) FEBS Lett. , vol.427 , pp. 252-254
    • Nakamura, S.1    Ogawa, M.2    Saito, M.3    Nakai, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.