메뉴 건너뛰기




Volumn 15, Issue 5, 2009, Pages 453-463

Structural and functional properties of heat-processed soybean flour: Effect of proteolytic modification

Author keywords

Autoclaving; Enzymatic modification; Functional properties; Soy flour

Indexed keywords

ACID SOLUBILITY; CONTROL VALUES; DEFATTED SOY FLOURS; EMULSIFYING PROPERTY; ENZYMATIC MODIFICATION; FOOD SYSTEM; FUNCTIONAL PROPERTIES; HEAT PROCESSING; PHYSICO-CHEMICALS; PHYSICOCHEMICAL PROPERTY; SOY FLOUR; SOYBEAN FLOUR; STRUCTURAL BEHAVIORS; STRUCTURAL CHANGE; STRUCTURAL STUDIES; SURFACE HYDROPHOBICITY;

EID: 76449100730     PISSN: 10820132     EISSN: 15321738     Source Type: Journal    
DOI: 10.1177/1082013209350347     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0018536145 scopus 로고
    • Determination of degree of hydrolysis of food protein hydrolysates by Trinitrobenzenesulfonic acid
    • Adler-Nissen J. (1979). Determination of degree of hydrolysis of food protein hydrolysates by Trinitrobenzenesulfonic acid. Journal of Agricultural Food Chemistry 27: 1256-1262.
    • (1979) Journal of Agricultural Food Chemistry , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 0002494352 scopus 로고
    • A review of food protein hydrolysis-specific areas
    • Adler-Nissen J. (ed.). New York: Elsevier Applied Science Publications
    • Adler-Nissen J. (1986). A review of food protein hydrolysis-specific areas. In: Adler-Nissen J. (ed.). Enzymic Hydrolysis of Food Proteins. New York: Elsevier Applied Science Publications, pp. 57-131.
    • (1986) Enzymic Hydrolysis of Food Proteins , pp. 57-131
    • Adler-Nissen, J.1
  • 3
    • 76449083516 scopus 로고    scopus 로고
    • Association of Official Analytical Chemists (AOAC) Connif P. (ed.). 17th edn, Virginia, USA: AOAC
    • Association of Official Analytical Chemists (AOAC) (2000). Animal feeds, In: Connif P. (ed.). Official Methods of Analysis, Chap. 4, Vol. I, 17 th edn, Virginia, USA: AOAC, pp. 1-37.
    • (2000) Official Methods of Analysis, Chap. 4 , pp. 1-37
  • 4
    • 84985280190 scopus 로고
    • Effect of lipophilization of soy protein on its emulsion stabilizing properties
    • Aoki H., Taneyama O., Orimo N. and Kitagawa I. (1981). Effect of lipophilization of soy protein on its emulsion stabilizing properties. Journal of Food Science 46: 1192-1195.
    • (1981) Journal of Food Science , vol.46 , pp. 1192-1195
    • Aoki, H.1    Taneyama, O.2    Orimo, N.3    Kitagawa, I.4
  • 5
    • 0043051955 scopus 로고
    • Functional properties of the flour and the major protein fraction from sesame seed, sunflower seed and safflower seed
    • Bhooma K. and Prakash V. (1990). Functional properties of the flour and the major protein fraction from sesame seed, sunflower seed and safflower seed. Acta Alimentaria 19: 163-176.
    • (1990) Acta Alimentaria , vol.19 , pp. 163-176
    • Bhooma, K.1    Prakash, V.2
  • 6
    • 0032829926 scopus 로고    scopus 로고
    • β-Lactoglobulin hydrolysis. 2. Peptide identification, SH/SS exchange, and functional properties of hydrolysate fractions formed by the action of plasmin
    • DOI 10.1021/jf981230o
    • Caessens P.W.J.R., Daamen W.F., Gruppen H., Visser S. and Voragen A.G.J. (1999). β-lactoglobulin hydrolysis. II Peptide identification, SH/SS exchange and functional properties hydrolysates fractions formed by the action of plasmin. Journal of Agricultural Food Chemistry 47: 2980-2990. (Pubitemid 29421980)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.8 , pp. 2980-2990
    • Caessens, P.W.J.R.1    Daamen, W.F.2    Gruppen, H.3    Visser, S.4    Voragen, A.G.J.5
  • 7
    • 0002432336 scopus 로고
    • Amino acids, peptides and proteins
    • Fennema O.R. (ed.). 2nd edn, New York: Marcel Dekker Inc.
    • Cheftel J.C., Cuq J.L. and Lorient D. (1985). Amino acids, peptides and proteins. In: Fennema O.R. (ed.). Food Chemistry. 2 nd edn, New York: Marcel Dekker Inc., pp. 246-414.
    • (1985) Food Chemistry , pp. 246-414
    • Cheftel, J.C.1    Cuq, J.L.2    Lorient, D.3
  • 8
    • 21344475714 scopus 로고
    • Microcoagulation of proteins for development of creaminess
    • Cheftel J.C. and Dumay E. (1993). Microcoagulation of proteins for development of creaminess. Food Reviews International 9: 473-502.
    • (1993) Food Reviews International , vol.9 , pp. 473-502
    • Cheftel, J.C.1    Dumay, E.2
  • 9
    • 33845280838 scopus 로고
    • Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin
    • Chobert J.M., Bertrand-Harb C. and Nicolas M.G. (1988 a). Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. Journal of Agricultural Food Chemistry 36: 883-892.
    • (1988) Journal of Agricultural Food Chemistry , vol.36 , pp. 883-892
    • Chobert, J.M.1    Bertrand-Harb, C.2    Nicolas, M.G.3
  • 10
    • 0000207162 scopus 로고
    • Solubility and emulsifying properties of caseins modified enzymatically by Staphylococcus aureus V8 protease
    • Chobert J.M., Sitohy M.Z. and Whitaker J.H. (1988 b). Solubility and emulsifying properties of caseins modified enzymatically by Staphylococcus aureus V8 protease. Journal of Agricultural Food Chemistry 36: 220-224.
    • (1988) Journal of Agricultural Food Chemistry , vol.36 , pp. 220-224
    • Chobert, J.M.1    Sitohy, M.Z.2    Whitaker, J.H.3
  • 11
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides and proteins
    • Fennema W.O. (ed.). New York: Marcel Dekker Inc
    • Damodaran S. (1996). Amino acids, peptides and proteins. In: Fennema W.O. (ed.). Food Chemistry. New York: Marcel Dekker Inc, pp. 373-380.
    • (1996) Food Chemistry , pp. 373-380
    • Damodaran, S.1
  • 12
    • 0001823720 scopus 로고
    • Structure function relationship of food proteins
    • Zieger G.R. and Hettiarachchy N.S. (eds). New York: Marcel Dekker Inc.
    • Damodaran S. (1994). Structure function relationship of food proteins. In: Zieger G.R. and Hettiarachchy N.S. (eds). Protein Functionality in Food Systems. New York: Marcel Dekker Inc., pp. 190-225.
    • (1994) Protein Functionality in Food Systems , pp. 190-225
    • Damodaran, S.1
  • 13
    • 0028511883 scopus 로고
    • Proteins at liquid interfaces: Role of the molten globule state
    • Dickinson E. and Matsumura Y. (1994). Proteins at liquid interfaces: role of the molten globule state. Colloids Surfaces B. 3: 1-17.
    • (1994) Colloids Surfaces B , vol.3 , pp. 1-17
    • Dickinson, E.1    Matsumura, Y.2
  • 14
    • 0027349531 scopus 로고
    • Influence of milk peptides in determining the functionality of milk protein: A review
    • Haque Z.U. (1993). Influence of milk peptides in determining the functionality of milk protein: a review. Journal of Dairy Science 76: 311-320.
    • (1993) Journal of Dairy Science , vol.76 , pp. 311-320
    • Haque, Z.U.1
  • 15
    • 84985200365 scopus 로고
    • Relationship of hydrophobicity and net charge to the solubility of milk and salt proteins
    • Hayakawa S. and Nakai S. (1985). Relationship of hydrophobicity and net charge to the solubility of milk and salt proteins. Journal of Food Science 50: 486-491.
    • (1985) Journal of Food Science , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 16
    • 1542526976 scopus 로고    scopus 로고
    • Structural and functional changes of faba bean legumin during super-limited tryptic hydrolysis
    • Henning T., Mothes R., Dudek S., Krause J.P. and Schwenke K.D. (1997). Structural and functional changes of faba bean legumin during super-limited tryptic hydrolysis. Nahrung 41: 81-86.
    • (1997) Nahrung , vol.41 , pp. 81-86
    • Henning, T.1    Mothes, R.2    Dudek, S.3    Krause, J.P.4    Schwenke, K.D.5
  • 18
    • 0642272644 scopus 로고
    • Further studies on the aggregation and insolubilization of soy bean 11S globulin with humidity storage
    • Hoshi Y. and Yamauchi F. (1983). Further studies on the aggregation and insolubilization of soy bean 11S globulin with humidity storage. Agricultural Biological Chemistry 47: 1473-1479.
    • (1983) Agricultural Biological Chemistry , vol.47 , pp. 1473-1479
    • Hoshi, Y.1    Yamauchi, F.2
  • 19
    • 14844310248 scopus 로고    scopus 로고
    • Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis
    • Jung S., Murphy P.A. and Johnson L.A. (2005). Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis. Journal of Food Science 70: C180 - C187.
    • (2005) Journal of Food Science , vol.70
    • Jung, S.1    Murphy, P.A.2    Johnson, L.A.3
  • 20
    • 0000617029 scopus 로고
    • Functional properties of proteolytic enzyme modified soy protein isolate
    • Kim S.Y., Park P.S.W. and Rhee K.C. (1990). Functional properties of proteolytic enzyme modified soy protein isolate. Journal of Agricultural Food Chemistry 38: 651-656.
    • (1990) Journal of Agricultural Food Chemistry , vol.38 , pp. 651-656
    • Kim, S.Y.1    Park, P.S.W.2    Rhee, K.C.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • LaemmLi U.K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0028526893 scopus 로고
    • Physicochemical and functional properties of protein hydrolysates in nutrition products
    • Mahmoud M.I. (1994). Physicochemical and functional properties of protein hydrolysates in nutrition products. Food Technology 48: 89-95.
    • (1994) Food Technology , vol.48 , pp. 89-95
    • Mahmoud, M.I.1
  • 26
    • 0036392199 scopus 로고    scopus 로고
    • Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties
    • Molina Ortiz S.E. and Wagner J.R. (2002). Hydrolysates of native and modified soy protein isolates: structural characteristics, solubility and foaming properties. Food Research International 35: 511-518.
    • (2002) Food Research International , vol.35 , pp. 511-518
    • Molina Ortiz, S.E.1    Wagner, J.R.2
  • 27
    • 0018322290 scopus 로고
    • Conformation and functionality of milk proteins
    • Pour-El A. (ed.). Washington DC, USA: ACS Symposium Series 91
    • Morr C.V. (1979). Conformation and functionality of milk proteins. In: Pour-El A. (ed.). Functionality and Protein Structure. Washington DC, USA: ACS Symposium Series 91, pp. 65-80.
    • (1979) Functionality and Protein Structure , pp. 65-80
    • Morr, C.V.1
  • 28
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing the functionality of food proteins by enzymatic modification
    • Panyam D. and Kilara A. (1996). Enhancing the functionality of food proteins by enzymatic modification. Trends in Food Science and Technology 7: 120-125.
    • (1996) Trends in Food Science and Technology , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2
  • 29
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidometric technique
    • Pearce K.N. and Kinsella J.E. (1978). Emulsifying properties of proteins: evaluation of a turbidometric technique. Journal of Agricultural Food Chemistry 26: 716-723.
    • (1978) Journal of Agricultural Food Chemistry , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 32
    • 0000997716 scopus 로고
    • Modification of functional properties of soy proteins by proteolytic enzyme treatment
    • Puski G. (1975). Modification of functional properties of soy proteins by proteolytic enzyme treatment. Cereal Chemistry 52: 655-664.
    • (1975) Cereal Chemistry , vol.52 , pp. 655-664
    • Puski, G.1
  • 33
    • 0031423685 scopus 로고    scopus 로고
    • Solubility and emulsifying properties of soy protein isolates modified by pancreatin
    • Qi M., Hettiarachchy N.S. and Kalapathy U. (1997). Solubility and emulsifying properties of soy protein isolates modified by pancreatin. Journal of Food Science 62: 1110-1115.
    • (1997) Journal of Food Science , vol.62 , pp. 1110-1115
    • Qi, M.1    Hettiarachchy, N.S.2    Kalapathy, U.3
  • 34
    • 53149094669 scopus 로고    scopus 로고
    • Chemical cleavage of bovine β-lactoglobulin by BNPS-skatole for preparative purposes: Comparative study of hydrolytic procedures and peptide characterization
    • Rahali V. and Gueguen J. (1999). Chemical cleavage of bovine β-lactoglobulin by BNPS-skatole for preparative purposes: comparative study of hydrolytic procedures and peptide characterization. Journal of Protein Chemistry 18: 1-12.
    • (1999) Journal of Protein Chemistry , vol.18 , pp. 1-12
    • Rahali, V.1    Gueguen, J.2
  • 35
    • 18344416037 scopus 로고    scopus 로고
    • Functional properties of improved glycinin and β-conglycinin fractions
    • Rickert D.A., Johnson L.A. and Murphy P.A. (2004). Functional properties of improved glycinin and β-conglycinin fractions. Journal of Food Science 69: 303-311.
    • (2004) Journal of Food Science , vol.69 , pp. 303-311
    • Rickert, D.A.1    Johnson, L.A.2    Murphy, P.A.3
  • 36
    • 0030078033 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin
    • Stapelfeldt H., Petersen P.H., Kristiansen K.R., Qvist K.B. and Skilbsted L.H. (1996). Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin. Journal of Dairy Research 63: 111-118.
    • (1996) Journal of Dairy Research , vol.63 , pp. 111-118
    • Stapelfeldt, H.1    Petersen, P.H.2    Kristiansen, K.R.3    Qvist, K.B.4    Skilbsted, L.H.5
  • 37
    • 84987339598 scopus 로고
    • Emulsifying property of whey peptide fractions as a function of pH and ionic strength
    • Turgeon S.L., Gauthier S.F. and Paquin P. (1992). Emulsifying property of whey peptide fractions as a function of pH and ionic strength. Journal of Food Science 57: 601-604.
    • (1992) Journal of Food Science , vol.57 , pp. 601-604
    • Turgeon, S.L.1    Gauthier, S.F.2    Paquin, P.3
  • 38
    • 0002609034 scopus 로고
    • Relationship of hydrophobicity to emulsifying properties of heat denatured proteins
    • Voutsinas L.P., Cheung E. and Nakai S. (1983). Relationship of hydrophobicity to emulsifying properties of heat denatured proteins. Journal of Food Science 48: 26-32.
    • (1983) Journal of Food Science , vol.48 , pp. 26-32
    • Voutsinas, L.P.1    Cheung, E.2    Nakai, S.3
  • 39
    • 0033852356 scopus 로고    scopus 로고
    • Relation between solubility and surface aromatic hydrophobicity as an indicator of modification during preparation processes of commercial and laboratory prepared soy protein isolates
    • Wagner J.R., Sorgentini D.A. and Anon M.C. (2000). Relation between solubility and surface aromatic hydrophobicity as an indicator of modification during preparation processes of commercial and laboratory prepared soy protein isolates. Journal of Agricultural Food Chemistry 48: 3159-3165.
    • (2000) Journal of Agricultural Food Chemistry , vol.48 , pp. 3159-3165
    • Wagner, J.R.1    Sorgentini, D.A.2    Anon, M.C.3
  • 40
    • 0000147349 scopus 로고
    • Heat denaturation of soybean 11S protein
    • Wolf W.J. and Tamura T. (1969). Heat denaturation of soybean 11S protein. Cereal Chemistry 46: 331-344.
    • (1969) Cereal Chemistry , vol.46 , pp. 331-344
    • Wolf, W.J.1    Tamura, T.2
  • 41
    • 0032116216 scopus 로고    scopus 로고
    • Hydrophobicity, solubility and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration
    • Wu W.U., Hettiarachchy N.S. and Qi M. (1998). Hydrophobicity, solubility and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. Journal of American Oil Chemists Society 75: 845-850.
    • (1998) Journal of American Oil Chemists Society , vol.75 , pp. 845-850
    • Wu, W.U.1    Hettiarachchy, N.S.2    Qi, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.