메뉴 건너뛰기




Volumn 57, Issue 2, 2009, Pages 717-723

Effects of thermal treatment on the coagulation of soy proteins induced by subtilisin Carlsberg

Author keywords

Coagulation; Soy protein; Subtilisin Carlsberg; Thermal treatment; Turbidity

Indexed keywords

GLYCINE MAX;

EID: 59849087348     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf802693f     Document Type: Article
Times cited : (21)

References (30)
  • 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
    • 0020374278 scopus 로고
    • Studies on the mechanism of antihypercholesterolemic action of soy protein and soy proteintype amino acid mixtures in relation to the casein counterparts in rats
    • Nagata. Y.; Ishiwaki, N.; Sugano, M. Studies on the mechanism of antihypercholesterolemic action of soy protein and soy proteintype amino acid mixtures in relation to the casein counterparts in rats. J. Nutr. 1982, 112, 1614-1625.
    • (1982) J. Nutr , vol.112 , pp. 1614-1625
    • Nagata, Y.1    Ishiwaki, N.2    Sugano, M.3
  • 3
    • 0029056306 scopus 로고
    • Metaanalysis of the effects of soy protein intake on serum lipids
    • Anderson, J. W.; Johnstone, B. M.; Cook-Newell, M. E. Metaanalysis of the effects of soy protein intake on serum lipids. N. Engl. J. Med. 1995, 333, 276-282.
    • (1995) N. Engl. J. Med , vol.333 , pp. 276-282
    • Anderson, J.W.1    Johnstone, B.M.2    Cook-Newell, M.E.3
  • 4
    • 4544298886 scopus 로고    scopus 로고
    • Soybean β-conglycinin diet suppresses serum triglyceride levels in normal and genetically obese mice by induction of β-oxidation, downregulation of fatty acid synthase, and inhibition of triglyceride absorption
    • Moriyama, T.; Kishimoto, K.; Nagai, K.; Urade, R.; Ogawa, T.; Utsumi, S.; Maruyama, N.; Maebuchi, M. Soybean β-conglycinin diet suppresses serum triglyceride levels in normal and genetically obese mice by induction of β-oxidation, downregulation of fatty acid synthase, and inhibition of triglyceride absorption. Biosci., Biotechnol., Biochem. 2004, 68, 352-359.
    • (2004) Biosci., Biotechnol., Biochem , vol.68 , pp. 352-359
    • Moriyama, T.1    Kishimoto, K.2    Nagai, K.3    Urade, R.4    Ogawa, T.5    Utsumi, S.6    Maruyama, N.7    Maebuchi, M.8
  • 7
    • 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
  • 8
    • 0008582625 scopus 로고
    • Production and properties of a soymilk-clotting enzyme system from a microorganism
    • Park, Y. W.; Kusakabe. I.; Kobayashi. H.; Murakami, K. Production and properties of a soymilk-clotting enzyme system from a microorganism. Agric. Biol. Chem. 1985, 49, 3215-3219.
    • (1985) Agric. Biol. Chem , vol.49 , pp. 3215-3219
    • Park, Y.W.1    Kusakabe, I.2    Kobayashi, H.3    Murakami, K.4
  • 9
  • 11
    • 1642298359 scopus 로고    scopus 로고
    • Otte, J.; Ipsen, R.; Ladefoged, A. M.; S0rensen, J. Protease-fnduced aggregation of bovine α-lactalbumin: Identification of the primary associating fragment. J. Daily Res. 2004, 71, 88-96.
    • Otte, J.; Ipsen, R.; Ladefoged, A. M.; S0rensen, J. Protease-fnduced aggregation of bovine α-lactalbumin: Identification of the primary associating fragment. J. Daily Res. 2004, 71, 88-96.
  • 12
    • 16344365621 scopus 로고    scopus 로고
    • Gel formation of peptides produced by extensive enzymatic hydrolysis of β-lactoglobulin
    • Doucet, D.; Foegeding, E. A. Gel formation of peptides produced by extensive enzymatic hydrolysis of β-lactoglobulin. Biomacromolecules 2005, 6, 1140-1148.
    • (2005) Biomacromolecules , vol.6 , pp. 1140-1148
    • Doucet, D.1    Foegeding, E.A.2
  • 13
    • 0037180992 scopus 로고    scopus 로고
    • Coagulation of soy protein isolates induced by subtilisin Carlsberg
    • Inouye, K.; Nagai, K.; Takita, T. Coagulation of soy protein isolates induced by subtilisin 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
  • 14
    • 3242779950 scopus 로고    scopus 로고
    • Insights into the reaction mechanisms of the coagulation of soy protein isolates induced by subtilisin Carlsberg
    • Nagai. K.; Inouye, K. Insights into the reaction mechanisms of the coagulation of soy protein isolates induced by subtilisin Carlsberg. J. Agric. Food Chem. 2004, 52, 4921-4927.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 4921-4927
    • Nagai, K.1    Inouye, K.2
  • 15
    • 0037070368 scopus 로고    scopus 로고
    • Deodorization of soybean proteins by enzymatic and physicochemical treatments
    • Inouye, K.; Shiihara. M.; Uno. T.; Takita, T. Deodorization of soybean proteins by enzymatic and physicochemical treatments. J. Agric. Food Chem. 2002, 50, 1652-1658.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 1652-1658
    • Inouye, K.1    Shiihara, M.2    Uno, T.3    Takita, T.4
  • 16
    • 3142603220 scopus 로고    scopus 로고
    • Selective proteolysis of the glycinin and β-conglycinin fractions in a soy protein isolates by pepsin and papain with controlled pH and temperature
    • Tsumura, K.; Saito, T.; Kugimiya, W.; Inouye, K. Selective proteolysis of the glycinin and β-conglycinin fractions in a soy protein isolates by pepsin and papain with controlled pH and temperature. J. Food Sci. 2004, 69, C363-C367.
    • (2004) J. Food Sci , vol.69
    • Tsumura, K.1    Saito, T.2    Kugimiya, W.3    Inouye, K.4
  • 17
    • 58849100989 scopus 로고
    • Relationship between Theological properties and conformational states of 7S globulin from soybeans at acidic pH
    • Nishinari, K, Doi, E, Ed, Plenum Press: New York
    • Nagano, T.; Mori, H.; Nishinari, K. Relationship between Theological properties and conformational states of 7S globulin from soybeans at acidic pH. In Food Hydrocolloids: Structures, Properties, and Functions; Nishinari, K.. Doi, E., Ed.; Plenum Press: New York, 1994; pp 355-360.
    • (1994) Food Hydrocolloids: Structures, Properties, and Functions , pp. 355-360
    • Nagano, T.1    Mori, H.2    Nishinari, K.3
  • 18
    • 0039234462 scopus 로고    scopus 로고
    • 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; 3. pp 561-608.
    • 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.
  • 20
    • 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
  • 21
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen, Y.-H.; Yang, J. T.; Chau, K. H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 1974, 13, 3351-3359.
    • (1974) Biochemistry , vol.13 , pp. 3351-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 22
    • 35548957779 scopus 로고    scopus 로고
    • A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (US) and β-conglycinin (7S)
    • Clara Sze, K. W.; Kshirsagar, H. H.; Venkatachalam. M.; Sathe, S. K. A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (US) and β-conglycinin (7S). J. Agric. Food Chem. 2007, 55, 8745-8753.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 8745-8753
    • Clara Sze, K.W.1    Kshirsagar, H.H.2    Venkatachalam, M.3    Sathe, S.K.4
  • 24
    • 1642292488 scopus 로고    scopus 로고
    • Changes in characters of soybean glycinin groups I, IIa, and IIb caused by heating
    • Tezuka, M.; Yagasaki, K.; Ono, T. Changes in characters of soybean glycinin groups I, IIa, and IIb caused by heating. J. Agric. Food Chem. 2004, 52, 1693-1699.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 1693-1699
    • Tezuka, M.1    Yagasaki, K.2    Ono, T.3
  • 25
    • 0038644459 scopus 로고    scopus 로고
    • Thermally induced structural changes in glycinin, the 1 IS globulin of soya bean (Glycine max) -An in situ spectroscopic study
    • Mills. E. N.; Marigheto, N. A.; Wellner. N.; Faihurst. S. A.; Jenkins, J. A.; Mann, R.; Belton, P. S. Thermally induced structural changes in glycinin, the 1 IS globulin of soya bean (Glycine max) -An in situ spectroscopic study. Biochim. Biophys. Acta 2003, 1648, 105-114.
    • (2003) Biochim. Biophys. Acta , vol.1648 , pp. 105-114
    • Mills, E.N.1    Marigheto, N.A.2    Wellner, N.3    Faihurst, S.A.4    Jenkins, J.A.5    Mann, R.6    Belton, P.S.7
  • 26
    • 36148977234 scopus 로고    scopus 로고
    • Hydrolysis of whey protein isolates with Bacillus licheniformis protease: Fractionation and identification of aggregating peptides
    • Creusot, N.; Gruppen, H. Hydrolysis of whey protein isolates with Bacillus licheniformis protease: Fractionation and identification of aggregating peptides. J. Agric. Food Chem. 2007, 55, 9241-9250.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 9241-9250
    • Creusot, N.1    Gruppen, H.2
  • 27
    • 34648819856 scopus 로고    scopus 로고
    • Enzyme-induced aggregation and gelation of proteins
    • Creusot, N.; Gruppen, H. Enzyme-induced aggregation and gelation of proteins. Biotechnol. Adv. 2007, 25, 597-601.
    • (2007) Biotechnol. Adv , vol.25 , pp. 597-601
    • Creusot, N.1    Gruppen, H.2
  • 28
    • 34648834583 scopus 로고    scopus 로고
    • Comparison of the aggregation behavior of soy and bovine whey protein hydrolysates
    • Kuipers, B. J.: Alting, A. C.; Gruppen, H. Comparison of the aggregation behavior of soy and bovine whey protein hydrolysates. Biotechnol. Adv. 2007, 25, 606-610.
    • (2007) Biotechnol. Adv , vol.25 , pp. 606-610
    • Kuipers, B.J.1    Alting, A.C.2    Gruppen, H.3
  • 29
    • 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
  • 30
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.