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Volumn 17, Issue 10, 2016, Pages

Interactions of β-Conglycinin (7S) with different phenolic acids-impact on structural characteristics and proteolytic degradation of proteins

Author keywords

7S; Caffeic acid; Chlorogenic acid; Gallic acid; Interaction; p coumalic acid; Conglycinin

Indexed keywords

BETA CONGLYCININ; CAFFEIC ACID; CHLOROGENIC ACID; COUMARIC ACID; GALLIC ACID; PEPSIN A; POLYPHENOL; SOYBEAN PROTEIN; TRYPSIN; UNCLASSIFIED DRUG; BETA-CONGLYCININ PROTEIN, GLYCINE MAX; CAFFEIC ACID DERIVATIVE; GLOBULIN; HYDROXYBENZOIC ACID DERIVATIVE; PHENOLIC ACID; PLANT ANTIGEN; SEED STORAGE PROTEIN;

EID: 84991316046     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms17101671     Document Type: Article
Times cited : (18)

References (43)
  • 1
    • 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
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 2
    • 0017093464 scopus 로고
    • Separation of the Glycopeptides from Soybean 7S Protein: Their Amino Acid Sequences
    • Yamauchi, F.; Thanh, V.H.; Kawase, M.; Kazuo, S. Separation of the Glycopeptides from Soybean 7S Protein: Their Amino Acid Sequences. Agric. Biol. Chem. 1976, 40, 691-696.
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 691-696
    • Yamauchi, F.1    Thanh, V.H.2    Kawase, M.3    Kazuo, S.4
  • 4
    • 51049083548 scopus 로고    scopus 로고
    • Soymilk treated by ultra-high-pressure homogenization: Acid coagulation properties and characteristics of a soy-yogurt product
    • [CrossRef]
    • Cruz, N.S.; Capellas, M.; Jaramillo, D.P.; Trujillo, A.J.; Guamis, B.; Ferragut, V. Soymilk treated by ultra-high-pressure homogenization: acid coagulation properties and characteristics of a soy-yogurt product. Food Hydrocoll. 2009, 23, 490-496. [CrossRef]
    • (2009) Food Hydrocoll. , vol.23 , pp. 490-496
    • Cruz, N.S.1    Capellas, M.2    Jaramillo, D.P.3    Trujillo, A.J.4    Guamis, B.5    Ferragut, V.6
  • 5
    • 84874574180 scopus 로고    scopus 로고
    • Transglutaminase-set soy globulin-stabilized emulsion gels: Influence of soy β-conglycinin/glycinin ratio on properties, microstructure and gelling mechanism
    • [CrossRef]
    • Tang, C.H.; Luo, L.J.; Liu, F.U.; Chen, Z. Transglutaminase-set soy globulin-stabilized emulsion gels: Influence of soy β-conglycinin/glycinin ratio on properties, microstructure and gelling mechanism. Food Res. Int. 2013, 51, 804-812. [CrossRef]
    • (2013) Food Res. Int. , vol.51 , pp. 804-812
    • Tang, C.H.1    Luo, L.J.2    Liu, F.U.3    Chen, Z.4
  • 6
    • 34547490682 scopus 로고    scopus 로고
    • Molecular nutraceutics as a mean to investigate the positive effects of legume seed proteins on human healthy
    • [CrossRef]
    • Scarafoni, A.; Magni, C.; Duranti, M. Molecular nutraceutics as a mean to investigate the positive effects of legume seed proteins on human healthy. Trends Food Sci. Technol. 2007, 18, 454-463. [CrossRef]
    • (2007) Trends Food Sci. Technol. , vol.18 , pp. 454-463
    • Scarafoni, A.1    Magni, C.2    Duranti, M.3
  • 7
    • 0026656950 scopus 로고
    • Low density lipoprotein receptor activity is modulated by soybean globulins in cell culture
    • Lovati, M.R.; Manzoni, C.; Corsini, A.; Granata, A.; Fumagalli, R.; Sirtori, C.R. Low density lipoprotein receptor activity is modulated by soybean globulins in cell culture. J. Nutr. 1992, 122, 1971-1978.
    • (1992) J. Nutr. , vol.122 , pp. 1971-1978
    • Lovati, M.R.1    Manzoni, C.2    Corsini, A.3    Granata, A.4    Fumagalli, R.5    Sirtori, C.R.6
  • 8
    • 2642556417 scopus 로고    scopus 로고
    • The α' subunit from soybean 7S globulin lowers plasma lipids and upregulates liver β-VLDL receptors in rats fed a hypercholesterolemic diet
    • Marcello, D.; Maria Rosa, L.; Valeria, D.; Alberto, B.; Alessio, S.; Silvia, C. The α' subunit from soybean 7S globulin lowers plasma lipids and upregulates liver β-VLDL receptors in rats fed a hypercholesterolemic diet. J. Nutr. 2004, 134, 1334-1339.
    • (2004) J. Nutr. , vol.134 , pp. 1334-1339
    • Marcello, D.1    Maria Rosa, L.2    Valeria, D.3    Alberto, B.4    Alessio, S.5    Silvia, C.6
  • 9
    • 0035021485 scopus 로고    scopus 로고
    • Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins
    • [CrossRef]
    • Molina, E.; Papadopoulou, A.; Ledward, D.A. Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins. Food Hydrocoll. 2001, 15, 263-269. [CrossRef]
    • (2001) Food Hydrocoll. , vol.15 , pp. 263-269
    • Molina, E.1    Papadopoulou, A.2    Ledward, D.A.3
  • 10
    • 84908553793 scopus 로고    scopus 로고
    • Texture characteristics of soymilk gels formed by lactic fermentation: A comparison of soymilk prepared by blanching soybeans under different temperatures
    • [CrossRef]
    • Peng, X.; Guo, S. Texture characteristics of soymilk gels formed by lactic fermentation: A comparison of soymilk prepared by blanching soybeans under different temperatures. Food Hydrocoll. 2015, 43, 58-65. [CrossRef]
    • (2015) Food Hydrocoll. , vol.43 , pp. 58-65
    • Peng, X.1    Guo, S.2
  • 11
    • 84918558198 scopus 로고    scopus 로고
    • The binding mechanism of lecithin to soybean 11S and 7S globulins using fluorescence spectroscopy
    • [CrossRef]
    • Li, J.; Li, Y.; Guo, S. The binding mechanism of lecithin to soybean 11S and 7S globulins using fluorescence spectroscopy. Food Sci. Biotechnol. 2014, 23, 1785-1791. [CrossRef]
    • (2014) Food Sci. Biotechnol. , vol.23 , pp. 1785-1791
    • Li, J.1    Li, Y.2    Guo, S.3
  • 12
    • 77949570474 scopus 로고    scopus 로고
    • Impact of high intensity pulsed electric field on antioxidant properties and quality parameters of a fruit juice-soymilk beverage in chilled storage
    • [CrossRef]
    • Morales-de la Peña, M.; Salvia-Trujillo, L.; Rojas-Graü, M.A.; Martín-Belloso, O. Impact of high intensity pulsed electric field on antioxidant properties and quality parameters of a fruit juice-soymilk beverage in chilled storage. LWT-Food Sci. Technol. 2010, 43, 872-881. [CrossRef]
    • (2010) LWT-Food Sci. Technol. , vol.43 , pp. 872-881
    • Morales-de la Peña, M.1    Salvia-Trujillo, L.2    Rojas-Graü, M.A.3    Martín-Belloso, O.4
  • 13
    • 79960195407 scopus 로고    scopus 로고
    • Changes on phenolic and carotenoid composition of high intensity pulsed electric field and thermally treated fruit juice-soymilk beverages during refrigerated storage
    • [CrossRef] [PubMed]
    • Morales-de la Peña, M.; Salvia-Trujillo, L.; Rojas-Graü, M.A.; Martín-Belloso, O. Changes on phenolic and carotenoid composition of high intensity pulsed electric field and thermally treated fruit juice-soymilk beverages during refrigerated storage. Food Chem. 2011, 129, 982-990. [CrossRef] [PubMed]
    • (2011) Food Chem. , vol.129 , pp. 982-990
    • Morales-de la Peña, M.1    Salvia-Trujillo, L.2    Rojas-Graü, M.A.3    Martín-Belloso, O.4
  • 14
    • 84870513321 scopus 로고    scopus 로고
    • High intensity pulsed electric fields or thermal treatments effects on the amino acid profile of a fruit juice-soymilk beverage during refrigeration storage
    • [CrossRef]
    • Morales-de la Peña, M.; Salvia-Trujillo, L.; Garde-Cerdan, T.; Rojas-Graü, M.A.; Martín-Belloso, O. High intensity pulsed electric fields or thermal treatments effects on the amino acid profile of a fruit juice-soymilk beverage during refrigeration storage. Innov. Food Sci. Emerg. Technol. 2012, 16, 47-53. [CrossRef]
    • (2012) Innov. Food Sci. Emerg. Technol. , vol.16 , pp. 47-53
    • Morales-de la Peña, M.1    Salvia-Trujillo, L.2    Garde-Cerdan, T.3    Rojas-Graü, M.A.4    Martín-Belloso, O.5
  • 16
    • 84905905554 scopus 로고    scopus 로고
    • Artemisia dracunculus L. polyphenols complexed to soy protein show enhanced bioavailability and hypoglycemic activity in C57BL/6 mice
    • [CrossRef] [PubMed]
    • Ribnicky, D.M.; Roopchand, D.E.; Poulev, A.; Kuhn, P.; Oren, A.; Cefalu,W.T.; Raskin, I. Artemisia dracunculus L. polyphenols complexed to soy protein show enhanced bioavailability and hypoglycemic activity in C57BL/6 mice. Nutrition 2014, 30, 4-10. [CrossRef] [PubMed]
    • (2014) Nutrition , vol.30 , pp. 4-10
    • Ribnicky, D.M.1    Roopchand, D.E.2    Poulev, A.3    Kuhn, P.4    Oren, A.5    Cefalu, W.T.6    Raskin, I.7
  • 17
    • 84867896149 scopus 로고    scopus 로고
    • Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
    • [CrossRef] [PubMed]
    • Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Velickovic, C.T. Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. Food Chem. 2013, 136, 1263-1271. [CrossRef] [PubMed]
    • (2013) Food Chem. , vol.136 , pp. 1263-1271
    • Stojadinovic, M.1    Radosavljevic, J.2    Ognjenovic, J.3    Vesic, J.4    Prodic, I.5    Stanic-Vucinic, D.6    Velickovic, C.T.7
  • 18
    • 36148935581 scopus 로고    scopus 로고
    • Phenolics from walnut (Juglans regia L.) kernels: Antioxidant activity and interactions with proteins
    • [CrossRef]
    • Labuckas, D.O.; Maestri, D.M.; Perelló, M.; Martínez, M.L.; Lamarque, A.L. Phenolics from walnut (Juglans regia L.) kernels: Antioxidant activity and interactions with proteins. Food Chem. 2008, 107, 607-612. [CrossRef]
    • (2008) Food Chem. , vol.107 , pp. 607-612
    • Labuckas, D.O.1    Maestri, D.M.2    Perelló, M.3    Martínez, M.L.4    Lamarque, A.L.5
  • 19
    • 0037129793 scopus 로고    scopus 로고
    • Interactions of different phenolic acids and flavonoids with soy proteins
    • [CrossRef]
    • Rawel, H.M.; Czajka, D.; Rohn, S.; Kroll, J. Interactions of different phenolic acids and flavonoids with soy proteins. Int. J. Biol. Macromol. 2002, 30, 137-150. [CrossRef]
    • (2002) Int. J. Biol. Macromol. , vol.30 , pp. 137-150
    • Rawel, H.M.1    Czajka, D.2    Rohn, S.3    Kroll, J.4
  • 20
    • 0035238955 scopus 로고    scopus 로고
    • Reactions of phenolic substances with lysozyme-physicochemical characterisation and proteolytic digestion of the derivatives
    • [CrossRef]
    • Rawel, H.M.; Kroll, J.; Rohn, S. Reactions of phenolic substances with lysozyme-physicochemical characterisation and proteolytic digestion of the derivatives. Food Chem. 2001, 72, 59-71. [CrossRef]
    • (2001) Food Chem. , vol.72 , pp. 59-71
    • Rawel, H.M.1    Kroll, J.2    Rohn, S.3
  • 21
    • 19944398463 scopus 로고    scopus 로고
    • Chlorogenic acid moderately decreases the quality of whey proteins in rats
    • [CrossRef] [PubMed]
    • Petzke, K.J.; Stefanie, S.; Sascha, R.; Rawel, H.M.; Jürgen, K. Chlorogenic acid moderately decreases the quality of whey proteins in rats. J. Agric. Food Chem. 2005, 53, 3714-3720. [CrossRef] [PubMed]
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 3714-3720
    • Petzke, K.J.1    Stefanie, S.2    Sascha, R.3    Rawel, H.M.4    Jürgen, K.5
  • 22
    • 33748416859 scopus 로고    scopus 로고
    • Reactions of chlorogenic acid and quercetin with a soy protein isolate-Influence on the in vivo food protein quality in rats
    • [CrossRef] [PubMed]
    • Rohn, S.; Petzke, K.J.; Rawel, H.M.; Kroll, J. Reactions of chlorogenic acid and quercetin with a soy protein isolate-Influence on the in vivo food protein quality in rats. Mol. Nutr. Food Res. 2006, 50, 696-704. [CrossRef] [PubMed]
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 696-704
    • Rohn, S.1    Petzke, K.J.2    Rawel, H.M.3    Kroll, J.4
  • 23
    • 77953163607 scopus 로고    scopus 로고
    • Polyphenolic apple extracts: Effects of raw material and production method on antioxidant effectiveness and reduction of DNA damage in Caco-2 cells
    • [CrossRef] [PubMed]
    • Bellion, P.; Dioles, J.; Will, F. Polyphenolic apple extracts: Effects of raw material and production method on antioxidant effectiveness and reduction of DNA damage in Caco-2 cells. J. Agric. Food Chem. 2010, 58, 6636-6642. [CrossRef] [PubMed]
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 6636-6642
    • Bellion, P.1    Dioles, J.2    Will, F.3
  • 24
    • 0029975684 scopus 로고    scopus 로고
    • In vitro anticancer activity of fruit extracts from Vaccinium species
    • [CrossRef] [PubMed]
    • Bomser, J.; Madhavi, D.L.; Singletary, K.; Smith, M.A.L. In vitro anticancer activity of fruit extracts from Vaccinium species. Planta Med. 1996, 62, 212-216. [CrossRef] [PubMed]
    • (1996) Planta Med. , vol.62 , pp. 212-216
    • Bomser, J.1    Madhavi, D.L.2    Singletary, K.3    Smith, M.A.L.4
  • 25
    • 68149124472 scopus 로고    scopus 로고
    • Dietary phenolics: Chemistry, bioavailability and effects on health
    • [CrossRef] [PubMed]
    • Crozier, A.; Jaganath, I.B.; Clifford, M.N. Dietary phenolics: Chemistry, bioavailability and effects on health. Nat. Prod. Rep. 2009, 26, 1001-1043. [CrossRef] [PubMed]
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1001-1043
    • Crozier, A.1    Jaganath, I.B.2    Clifford, M.N.3
  • 26
    • 0034849369 scopus 로고    scopus 로고
    • Enzyme-assisted extraction of antioxidative phenols from black currant juice residue (Ribesnigrum)
    • [CrossRef] [PubMed]
    • Landbo, A.K.; Meyer, A.S. Enzyme-assisted extraction of antioxidative phenols from black currant juice residue (Ribesnigrum). J. Agric. Food Chem. 2001, 49, 3169-3177. [CrossRef] [PubMed]
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 3169-3177
    • Landbo, A.K.1    Meyer, A.S.2
  • 27
    • 41549123951 scopus 로고    scopus 로고
    • Chemistry, natural sources, dietary intake and pharmacokinetic properties of ferulic acid: A review
    • [CrossRef] [PubMed]
    • Zhao, Z.; Moghadasian, M.H. Chemistry, natural sources, dietary intake and pharmacokinetic properties of ferulic acid: A review. Food Chem. 2008, 109, 691-702. [CrossRef] [PubMed]
    • (2008) Food Chem. , vol.109 , pp. 691-702
    • Zhao, Z.1    Moghadasian, M.H.2
  • 28
    • 84886281954 scopus 로고    scopus 로고
    • Effect of hydrolysis of soy β-conglycinin on the oxidative stability of o/wemulsions
    • [CrossRef]
    • Phoon, P.Y.; Narsimhan, G. Effect of hydrolysis of soy β-conglycinin on the oxidative stability of o/wemulsions. Food Hydrocoll. 2014, 35, 429-443. [CrossRef]
    • (2014) Food Hydrocoll. , vol.35 , pp. 429-443
    • Phoon, P.Y.1    Narsimhan, G.2
  • 29
    • 84862811298 scopus 로고    scopus 로고
    • Effect of tannic acid on properties of soybean (Glycine maxseed ferritin: A model for interaction between naturally-occurring components in foodstuffs
    • [CrossRef] [PubMed]
    • Li, M.; Jia, X.; Yang, J. Effect of tannic acid on properties of soybean (Glycine maxseed ferritin: A model for interaction between naturally-occurring components in foodstuffs. Food Chem. 2012, 133, 410-415. [CrossRef] [PubMed]
    • (2012) Food Chem. , vol.133 , pp. 410-415
    • Li, M.1    Jia, X.2    Yang, J.3
  • 30
    • 77957819609 scopus 로고    scopus 로고
    • Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein
    • [CrossRef] [PubMed]
    • Deng, J.; Liao, X.; Yang, H.; Zhang, X.; Hua, Z.; Masuda, T.; Goto, F.; Yoshihara, T.; Zhao, G. Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein. J. Biol. Chem. 2010, 285, 32075-32086. [CrossRef] [PubMed]
    • (2010) J. Biol. Chem. , vol.285 , pp. 32075-32086
    • Deng, J.1    Liao, X.2    Yang, H.3    Zhang, X.4    Hua, Z.5    Masuda, T.6    Goto, F.7    Yoshihara, T.8    Zhao, G.9
  • 31
    • 67650522876 scopus 로고    scopus 로고
    • Protein association and dissociation regulated by ferric ion: A novel pathway for oxidative deposition of iron in pea seed ferritin
    • [CrossRef] [PubMed]
    • Li, C.R.; Fu, X.P.; Xin, Q.; Hu, X.S.; Chasteen, N.D.; Zhao, G.H. Protein association and dissociation regulated by ferric ion: A novel pathway for oxidative deposition of iron in pea seed ferritin. J. Biol. Chem. 2009, 284, 16743-16751. [CrossRef] [PubMed]
    • (2009) J. Biol. Chem. , vol.284 , pp. 16743-16751
    • Li, C.R.1    Fu, X.P.2    Xin, Q.3    Hu, X.S.4    Chasteen, N.D.5    Zhao, G.H.6
  • 33
    • 1642590674 scopus 로고
    • Structural similarity between legumin and vicilin storage proteins from legumes
    • [PubMed]
    • Argos, P.; Narayana, S.V.L.; Nielsen, N.C. Structural similarity between legumin and vicilin storage proteins from legumes. EMBO J. 1985, 4, 1111-1117. [PubMed]
    • (1985) EMBO J. , vol.4 , pp. 1111-1117
    • Argos, P.1    Narayana, S.V.L.2    Nielsen, N.C.3
  • 34
    • 0030610813 scopus 로고    scopus 로고
    • 1Ia and 1Ib transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins
    • [PubMed]
    • Callis, P.R. 1Ia and 1Ib transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 1997, 278, 113-150. [PubMed]
    • (1997) Methods Enzymol. , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 36
    • 79952534339 scopus 로고    scopus 로고
    • Milk β-lactoglobulin complexes with tea polyphenols
    • [CrossRef] [PubMed]
    • Kanakis, C.D.; Hasni, I.; Bourassa, P.; Tarantilis, P.A.; Polissiou, M.G. Milk β-lactoglobulin complexes with tea polyphenols. Food Chem. 2011, 127, 1046-1055. [CrossRef] [PubMed]
    • (2011) Food Chem. , vol.127 , pp. 1046-1055
    • Kanakis, C.D.1    Hasni, I.2    Bourassa, P.3    Tarantilis, P.A.4    Polissiou, M.G.5
  • 37
    • 0042259181 scopus 로고    scopus 로고
    • Interactions of glycinin with plant phenols-influence on chemical properties and proteolytic degradation of the proteins
    • [CrossRef]
    • Kroll, J.; Rawel, H.M.; Rohn, S.; Czajka, D. Interactions of glycinin with plant phenols-influence on chemical properties and proteolytic degradation of the proteins. Mol. Nutr. Food Res. 2001, 45, 388-389. [CrossRef]
    • (2001) Mol. Nutr. Food Res. , vol.45 , pp. 388-389
    • Kroll, J.1    Rawel, H.M.2    Rohn, S.3    Czajka, D.4
  • 38
    • 2442530678 scopus 로고    scopus 로고
    • Influence of the tannin structur e on the disruption effect of carbohydrates on protein-tannin aggregates
    • [CrossRef]
    • Mateus, C.; Carvalho, E.; Luis, C.; de Freitas, V. Influence of the tannin structur e on the disruption effect of carbohydrates on protein-tannin aggregates. Anal. Chim. Acta 2004, 513, 135-140. [CrossRef]
    • (2004) Anal. Chim. Acta , vol.513 , pp. 135-140
    • Mateus, C.1    Carvalho, E.2    Luis, C.3    De Freitas, V.4
  • 39
    • 76749084741 scopus 로고    scopus 로고
    • Characterization of binding interactions between green tea flavanoids and milk proteins
    • [CrossRef]
    • Yuksel, Z.; Avcı, E.; Erdem, Y.K. Characterization of binding interactions between green tea flavanoids and milk proteins. Food Chem. 2010, 121, 450-456. [CrossRef]
    • (2010) Food Chem. , vol.121 , pp. 450-456
    • Yuksel, Z.1    Avcı, E.2    Erdem, Y.K.3
  • 40
    • 84866493882 scopus 로고    scopus 로고
    • Spectroscopic and isothermal titration calorimetry studies of binding interaction of ferulic acid with bovine serum albumin
    • [CrossRef]
    • Ojha, H.; Mishra, K.; Hassan, M.I.; Chaudhury, N.K. Spectroscopic and isothermal titration calorimetry studies of binding interaction of ferulic acid with bovine serum albumin. Thermochim. Acta 2012, 548, 56-64. [CrossRef]
    • (2012) Thermochim. Acta , vol.548 , pp. 56-64
    • Ojha, H.1    Mishra, K.2    Hassan, M.I.3    Chaudhury, N.K.4
  • 42
    • 33751392653 scopus 로고
    • Dynamic viscoelastic study on the gelation of 7 S globulin from soybeans
    • [CrossRef]
    • Nagano, T.; Hirotsuka, M.; Mori, H.; Kohyama, K.; Nishinari, K. Dynamic viscoelastic study on the gelation of 7 S globulin from soybeans. J. Agric. Food Chem. 1992, 40, 941-944. [CrossRef]
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 941-944
    • Nagano, T.1    Hirotsuka, M.2    Mori, H.3    Kohyama, K.4    Nishinari, K.5
  • 43
    • 0003331354 scopus 로고
    • The United States Pharmacopeial Convention, Inc.: Rockville, MD, USA
    • Anonymous Simulated gastric fluid and simulated intestinal fluid, TS. The United States Pharmacopeia 23, the National Formulary 18; The United States Pharmacopeial Convention, Inc.: Rockville, MD, USA, 1995; p. 2053.
    • (1995) The United States Pharmacopeia 23, the National Formulary 18 , pp. 2053


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