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Volumn 52, Issue 15, 2004, Pages 4921-4927

Insights into the reaction mechanism of the coagulation of soy protein isolates induced by subtilisin Carlsberg

Author keywords

Aggregation; Coagulation; Food protein; Protease; Protease inhibitor; Soy protein

Indexed keywords

AMINO ACID; PROTEINASE; PROTEINASE INHIBITOR; SOYBEAN PROTEIN; SUBTILISIN; VEGETABLE PROTEIN;

EID: 3242779950     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf034845g     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 51249180057 scopus 로고
    • Functional properties of soy proteins
    • Kinsella, J. E. Functional properties of soy proteins. J. Am. Oil Chem. Soc. 1979, 56, 242-258.
    • (1979) J. Am. Oil Chem. Soc. , vol.56 , pp. 242-258
    • Kinsella, J.E.1
  • 2
    • 3242745355 scopus 로고    scopus 로고
    • Protein modification to optimize functionality: Protein hydrolysates
    • Whitaker, J. R., Voragen, A. G. J., Wong, D. W. S., Eds.; Dekker: New York
    • Kunst, T. Protein modification to optimize functionality: Protein hydrolysates. In Handbook of Food Enzymology; Whitaker, J. R., Voragen, A. G. J., Wong, D. W. S., Eds.; Dekker: New York, 2003; pp 221-236.
    • (2003) Handbook of Food Enzymology , pp. 221-236
    • Kunst, T.1
  • 3
    • 33845280838 scopus 로고
    • Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin
    • Chobert, J.-M.; Bertrand-Harb, C.; Nicolas, M.-G. Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J. Agric. Food Chem. 1988, 36, 883-892.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 883-892
    • Chobert, J.-M.1    Bertrand-Harb, C.2    Nicolas, M.-G.3
  • 4
    • 0016928361 scopus 로고
    • Solubilization of a fish protein concentrate with proteolytic enzymes
    • Hevia, P.; Whitaker, J. R.; Olcott, H. S. Solubilization of a fish protein concentrate with proteolytic enzymes. J. Agric. Food Chem. 1976, 24, 383-385.
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 383-385
    • Hevia, P.1    Whitaker, J.R.2    Olcott, H.S.3
  • 5
    • 0001750475 scopus 로고
    • Gelation of β-lactoglobulin treated with limited proteolysis by immobilized trypsin
    • Chen, S. X.; Swaisgood, H. E.; Foegeding, E. A. Gelation of β-lactoglobulin treated with limited proteolysis by immobilized trypsin. J. Agric. Food Chem. 1994, 42, 234-239.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 234-239
    • Chen, S.X.1    Swaisgood, H.E.2    Foegeding, E.A.3
  • 6
    • 0011650814 scopus 로고
    • Interfacial and emulsifying properties of whey peptide fractions obtained with a two-step ultrafiltration process
    • Turgeon, S. L.; Gauthier, S. F.; Paquin, P. Interfacial and emulsifying properties of whey peptide fractions obtained with a two-step ultrafiltration process. J. Agric. Food Chem. 1991, 39, 673-676.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 673-676
    • Turgeon, S.L.1    Gauthier, S.F.2    Paquin, P.3
  • 7
    • 0000050670 scopus 로고    scopus 로고
    • Plasmin hydrolysis of β-casein: Foaming and emulsifying properties of the fractionated hydrolysate
    • Caessens, P. W. J. R.; Gruppen, H.; Visser, S.; Van Aken, G. A.; Voragen, A. G. J. Plasmin hydrolysis of β-casein: foaming and emulsifying properties of the fractionated hydrolysate. J. Agric. Food Chem. 1997, 45, 2935-2941.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2935-2941
    • Caessens, P.W.J.R.1    Gruppen, H.2    Visser, S.3    Van Aken, G.A.4    Voragen, A.G.J.5
  • 8
    • 0032854339 scopus 로고    scopus 로고
    • β-lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and staphylococcus aureus V8 protease
    • Caessens P. W. J. R.; Visser, S.; Gruppen, H.; Voragen, A. G. J. β-lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and staphylococcus aureus V8 protease. J. Agric. Food Chem. 1999, 47, 2973-2979.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2973-2979
    • Caessens, P.W.J.R.1    Visser, S.2    Gruppen, H.3    Voragen, A.G.J.4
  • 9
    • 0030873439 scopus 로고    scopus 로고
    • Antihypertensive peptides derived from food proteins
    • Yamamoto, N. Antihypertensive peptides derived from food proteins. Biopolymers 1997, 43, 129-134.
    • (1997) Biopolymers , vol.43 , pp. 129-134
    • Yamamoto, N.1
  • 10
    • 0030875609 scopus 로고    scopus 로고
    • Release of opioid peptides, gluten exorphins by the action of pancreatic elastase
    • Fukudome, S.; Jinsmaa, Y.; Matsukawa, T.; Sasaki R.; Yoshikawa, M. Release of opioid peptides, gluten exorphins by the action of pancreatic elastase. FEBS Lett. 1997, 412, 475-479.
    • (1997) FEBS Lett. , vol.412 , pp. 475-479
    • Fukudome, S.1    Jinsmaa, Y.2    Matsukawa, T.3    Sasaki, R.4    Yoshikawa, M.5
  • 13
    • 0000271924 scopus 로고
    • Nature of stem bromelain treatments on the aggregation and gelation of soybean proteins
    • Fuke, Y.; Sekiguchi, M.; Matsuoka, H. Nature of stem bromelain treatments on the aggregation and gelation of soybean proteins. J. Food Sci. 1985, 50, 1283-1288.
    • (1985) J. Food Sci. , vol.50 , pp. 1283-1288
    • Fuke, Y.1    Sekiguchi, M.2    Matsuoka, H.3
  • 14
    • 85004642612 scopus 로고
    • Purification and characterization of soymilk-clotting enzymes from Bacillus sp. K-295G-7
    • Park, Y. W.; Kobayashi, H.; Kusakabe, I.; Murakami, K. Purification and characterization of soymilk-clotting enzymes from Bacillus sp. K-295G-7. Agric. Biol. Chem. 1987, 51, 2343-2349.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2343-2349
    • Park, Y.W.1    Kobayashi, H.2    Kusakabe, I.3    Murakami, K.4
  • 16
    • 0037180992 scopus 로고    scopus 로고
    • Coagulation of soy protein isolates induced by subutilisin Carlsberg
    • Inouye, K.; Nagai, K.; Takita T. Coagulation of soy protein isolates induced by subutilisin Carlsberg. J. Agric. Food Chem. 2002, 50, 1237-1242.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1237-1242
    • Inouye, K.1    Nagai, K.2    Takita, T.3
  • 17
    • 0001546940 scopus 로고
    • Improvement of the off-flavor of soy protein isolate by removing oil-body associated proteins and polar lipids
    • Samoto, M.; Miyazaki, C.; Kanamori, J.; Akasaka, T.; Kawamura, Y. Improvement of the off-flavor of soy protein isolate by removing oil-body associated proteins and polar lipids. Biosci. Biotechnol. Biochem. 1988, 52, 935-940.
    • (1988) Biosci. Biotechnol. Biochem. , vol.52 , pp. 935-940
    • Samoto, M.1    Miyazaki, C.2    Kanamori, J.3    Akasaka, T.4    Kawamura, Y.5
  • 19
    • 0039234462 scopus 로고
    • Subtilisins: Primary structure, chemical and physical properties
    • Boyer, D., Ed.; Academic Press: New York
    • Markland, F. S.; Smith, E. L. Subtilisins: Primary Structure, Chemical and Physical Properties. In The Enzymes, 3rd ed.; Boyer, D., Ed.; Academic Press: New York, 1971; Vol. 3, pp 561-608.
    • (1971) The Enzymes, 3rd Ed. , vol.3 , pp. 561-608
    • Markland, F.S.1    Smith, E.L.2
  • 20
    • 3242761611 scopus 로고    scopus 로고
    • Thermolysin
    • Whitaker, J. R., Voragen, A. G. J., Wong, D. W. S., Eds.; Dekker: New York
    • Inouye, K. Thermolysin. In Handbook of Food Enzymology; Whitaker, J. R., Voragen, A. G. J., Wong, D. W. S., Eds.; Dekker: New York, 2003; pp 1019-1028.
    • (2003) Handbook of Food Enzymology , pp. 1019-1028
    • Inouye, K.1
  • 21
    • 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 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0033819120 scopus 로고    scopus 로고
    • States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence
    • Inouye, K.; Tanaka, H.; Oneda, H. States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence. J. Biochem. 2000, 128, 363-369.
    • (2000) J. Biochem. , vol.128 , pp. 363-369
    • Inouye, K.1    Tanaka, H.2    Oneda, H.3
  • 23
    • 0000172656 scopus 로고
    • The seed globulins
    • Hudson, B. J. F., Ed.; Elsevier: London
    • Wright, D. J. The seed globulins. In Developments in Food Proteins-5; Hudson, B. J. F., Ed.; Elsevier: London, 1987; pp 81-157.
    • (1987) Developments in Food Proteins-5 , pp. 81-157
    • Wright, D.J.1
  • 24
    • 0000172656 scopus 로고
    • The seed globulins - Part II
    • Hudson, B. J. F., Ed.; Elsevier: London
    • Wright, D. J. The seed globulins-Part II. In Developments in Food Proteins-6; Hudson, B. J. F., Ed.; Elsevier: London, 1988; pp 119-178.
    • (1988) Developments in Food Proteins-6 , pp. 119-178
    • Wright, D.J.1
  • 25
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana, A.; Fassina, G.; Vita, C.; Dalzoppo, D.; Zamai, M.; Zambonin, M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry 1986, 25, 1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 26
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • Hubbard, S. J.; Eisenmenger, F.; Thomton, J. M. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 1994, 3, 757-768.
    • (1994) Protein Sci. , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmenger, F.2    Thomton, J.M.3
  • 28
    • 0017642740 scopus 로고
    • The stoichiometry of inhibition and binding of a protein proteinase inhibitor from Streptomyces (Streptomyces subtilisin inhibitor) against subtilisin BPN′
    • Inouye, K.; Tonomura, B.; Hiromi, K.; Sato, S.; Murao, S. The stoichiometry of inhibition and binding of a protein proteinase inhibitor from Streptomyces (Streptomyces subtilisin inhibitor) against subtilisin BPN′. J. Biochem. 1977, 82, 961-967.
    • (1977) J. Biochem. , vol.82 , pp. 961-967
    • Inouye, K.1    Tonomura, B.2    Hiromi, K.3    Sato, S.4    Murao, S.5
  • 29
    • 0018377017 scopus 로고
    • Interaction of α-chymotrypsin and a protein proteinase inhibitor, Streptomyces subtilisin inhibitor. The formation of ternary complex of Streptomyces subtilisin inhibitor, α-chymotrypsin, and proflavin
    • Inouye, K.; Tonomura, B.; Hiromi, K. Interaction of α-chymotrypsin and a protein proteinase inhibitor, Streptomyces subtilisin inhibitor. The formation of ternary complex of Streptomyces subtilisin inhibitor, α-chymotrypsin, and proflavin. J. Biochem. 1979, 85, 601-607.
    • (1979) J. Biochem. , vol.85 , pp. 601-607
    • Inouye, K.1    Tonomura, B.2    Hiromi, K.3
  • 30
    • 0018393576 scopus 로고
    • Interaction of a tyrosyl residue and carboxyl groups in the specific interaction between Streptomyces subtilisin inhibitor and subtilisin BPN′. A chemical modification study
    • Inouye, K.; Tonomura, B.; Hiromi, K. Interaction of a tyrosyl residue and carboxyl groups in the specific interaction between Streptomyces subtilisin inhibitor and subtilisin BPN′. A chemical modification study. J. Biochem. 1979, 85, 1115-1126.
    • (1979) J. Biochem. , vol.85 , pp. 1115-1126
    • Inouye, K.1    Tonomura, B.2    Hiromi, K.3
  • 31
    • 0027620748 scopus 로고
    • Identification of the soybean allergic protein, Gly m Bd 30K, with the soybean seed 34 kDa oil-body-associated protein
    • Ogawa, T.; Tsuji, H.; Bando, N.; Kitamura, K.; Zhu, Y.-L.; Hirano, H.; Nishikawa, K. Identification of the soybean allergic protein, Gly m Bd 30K, with the soybean seed 34 kDa oil-body-associated protein. Biosci. Biotechnol. Biochem. 1993, 57, 1030-1033.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1030-1033
    • Ogawa, T.1    Tsuji, H.2    Bando, N.3    Kitamura, K.4    Zhu, Y.-L.5    Hirano, H.6    Nishikawa, K.7


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