메뉴 건너뛰기




Volumn 46, Issue 2, 2012, Pages 453-459

Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate

Author keywords

Acidic treatment; Functional properties; High pressure homogenization; Pepsin; Soybean protein isolate; Structures

Indexed keywords

AGGREGATES; EMULSIFICATION; FREEZING; HIGH PRESSURE EFFECTS; HYDROPHOBICITY; PARTICLE SIZE; PARTICLE SIZE ANALYSIS; PROTEOLYSIS; STRUCTURE (COMPOSITION);

EID: 84856035282     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2011.12.001     Document Type: Article
Times cited : (118)

References (30)
  • 1
    • 84856029325 scopus 로고    scopus 로고
    • Pretreatment methods on functional properties of wheat gluten and hydrolysis efficiency
    • An Z.C., Zhou H.M., Zhu K.X. Pretreatment methods on functional properties of wheat gluten and hydrolysis efficiency. Food and Fermentation Industries 2009, 35:25-30.
    • (2009) Food and Fermentation Industries , vol.35 , pp. 25-30
    • An, Z.C.1    Zhou, H.M.2    Zhu, K.X.3
  • 2
    • 8644278891 scopus 로고    scopus 로고
    • Interactions of polysaccharides with β-lactoglobulin adsorbed films at the air-water interface
    • Baeza R., Sanchez C.C., Rodríguez Patino J.M., Pilosof A.M.R. Interactions of polysaccharides with β-lactoglobulin adsorbed films at the air-water interface. Food Hydrocolloids 2005, 19:239-248.
    • (2005) Food Hydrocolloids , vol.19 , pp. 239-248
    • Baeza, R.1    Sanchez, C.C.2    Rodríguez Patino, J.M.3    Pilosof, A.M.R.4
  • 3
    • 18544381389 scopus 로고    scopus 로고
    • Effect of molecular surface packing on the enzymatic activity modulation of an anchored protein on phospholipid langmuir monolayers
    • Caseli L., Oliveira R.G., Masui D.C., Furriel RP.M., Leone F.A., Maggio B., et al. Effect of molecular surface packing on the enzymatic activity modulation of an anchored protein on phospholipid langmuir monolayers. Langmuir 2005, 21:4090-4095.
    • (2005) Langmuir , vol.21 , pp. 4090-4095
    • Caseli, L.1    Oliveira, R.G.2    Masui, D.C.3    Furriel, R.P.M.4    Leone, F.A.5    Maggio, B.6
  • 5
    • 34548205199 scopus 로고    scopus 로고
    • Characterization of fractionated soy proteins produced by a new simplified procedure
    • Deak N.A., Murphy P.A., Johnson L.A. Characterization of fractionated soy proteins produced by a new simplified procedure. Journal of American Oil Chemists' Society 2007, 84:137-149.
    • (2007) Journal of American Oil Chemists' Society , vol.84 , pp. 137-149
    • Deak, N.A.1    Murphy, P.A.2    Johnson, L.A.3
  • 6
    • 0031398182 scopus 로고    scopus 로고
    • Composition and functional properties of protein isolates obtained from commercial legumes grown in northern Spain
    • Fernandez Q.A., Macarulla M.T. Composition and functional properties of protein isolates obtained from commercial legumes grown in northern Spain. Plant Foods for Human Nutrition 1997, 51:331-342.
    • (1997) Plant Foods for Human Nutrition , vol.51 , pp. 331-342
    • Fernandez, Q.A.1    Macarulla, M.T.2
  • 7
    • 33847400444 scopus 로고    scopus 로고
    • Controlled enzymatic hydrolysis of glycinin: susceptibility of acidic and basic subunits to proteolytic enzymes
    • Govindaraju K., Srinivas H. Controlled enzymatic hydrolysis of glycinin: susceptibility of acidic and basic subunits to proteolytic enzymes. LWT- Food Science and Technology 2007, 40:1056-1065.
    • (2007) LWT- Food Science and Technology , vol.40 , pp. 1056-1065
    • Govindaraju, K.1    Srinivas, H.2
  • 8
    • 49249153429 scopus 로고
    • Proteins at liquid interfaces. I. Kinetics of adsorption and surface denaturation
    • Graham D.E., Phillips M.C. Proteins at liquid interfaces. I. Kinetics of adsorption and surface denaturation. Journal of Colloid and Interface Science 1979, 70:403-414.
    • (1979) Journal of Colloid and Interface Science , vol.70 , pp. 403-414
    • Graham, D.E.1    Phillips, M.C.2
  • 9
    • 0001823720 scopus 로고
    • Structure-function relationship of food protein
    • Marcel Dekker, New York, N.S. Hettiarachchy, G.R. Ziegler (Eds.)
    • Hettiarachchy N.S., Ziegler G.R. Structure-function relationship of food protein. Protein functionality in food systems 1994, 1-38. Marcel Dekker, New York. N.S. Hettiarachchy, G.R. Ziegler (Eds.).
    • (1994) Protein functionality in food systems , pp. 1-38
    • Hettiarachchy, N.S.1    Ziegler, G.R.2
  • 10
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A., Nakai S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Indian Journal of Biochemistry & Biophysics 1980, 624:13-20.
    • (1980) Indian Journal of Biochemistry & Biophysics , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 11
    • 0000115549 scopus 로고
    • Effect of oxidative sulfitolysis of disulfide bonds of glycinin on solubility, surface hydrophobicity, and invitro digestibility
    • Kella N.K.D., Barbeau W.E., Kinsella J.E. Effect of oxidative sulfitolysis of disulfide bonds of glycinin on solubility, surface hydrophobicity, and invitro digestibility. Journal of Agricultural and Food Chemistry 1986, 34:251-256.
    • (1986) Journal of Agricultural and Food Chemistry , vol.34 , pp. 251-256
    • Kella, N.K.D.1    Barbeau, W.E.2    Kinsella, J.E.3
  • 12
    • 84985287289 scopus 로고
    • Surface active properties of food proteins: effects of reduction of disulfide bonds on film properties and foam stability of glycinin
    • Kim S.H., Kinsella J.M. Surface active properties of food proteins: effects of reduction of disulfide bonds on film properties and foam stability of glycinin. Journal of Food Science 1987, 52:128-131.
    • (1987) Journal of Food Science , vol.52 , pp. 128-131
    • Kim, S.H.1    Kinsella, J.M.2
  • 14
    • 84985350681 scopus 로고
    • Comparison of acid induced conformation changes between 7S and 11S globulin in soybean seeds
    • Koshiyama I. Comparison of acid induced conformation changes between 7S and 11S globulin in soybean seeds. griculture 1972, 23:853-859.
    • (1972) griculture , vol.23 , pp. 853-859
    • Koshiyama, I.1
  • 16
    • 43649089763 scopus 로고    scopus 로고
    • Functional properties of protein isolates from soybeans stored under various conditions
    • Liu C., Wang X.S., Ma H., Zhang Z.Q., Gao W.R., Xiao L. Functional properties of protein isolates from soybeans stored under various conditions. Food Chemistry 2008, 111:29-37.
    • (2008) Food Chemistry , vol.111 , pp. 29-37
    • Liu, C.1    Wang, X.S.2    Ma, H.3    Zhang, Z.Q.4    Gao, W.R.5    Xiao, L.6
  • 18
    • 77950595205 scopus 로고    scopus 로고
    • Effects of limited proteolysis and high-pressure homogenisation on structural and functional characteristics of glycinin
    • Luo D.H., Zhao Q.Z., Zhao M.M., Yang B., Long X.T., Ren J.Y., et al. Effects of limited proteolysis and high-pressure homogenisation on structural and functional characteristics of glycinin. Food Chemistry 2010, 122:25-30.
    • (2010) Food Chemistry , vol.122 , pp. 25-30
    • Luo, D.H.1    Zhao, Q.Z.2    Zhao, M.M.3    Yang, B.4    Long, X.T.5    Ren, J.Y.6
  • 19
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing the functionality of food proteins by enzymatic modification
    • Panyam D., Kilara A. Enhancing the functionality of food proteins by enzymatic modification. Trends in Food Science and Technology 1996, 7:120-125.
    • (1996) Trends in Food Science and Technology , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2
  • 20
    • 0942278928 scopus 로고    scopus 로고
    • High pressure and the enzymatic hydrolysis of soybean whey proteins
    • Peñasa E., Préstamo G., Gomezb R. High pressure and the enzymatic hydrolysis of soybean whey proteins. Food Chemistry 2004, 85(4):641-648.
    • (2004) Food Chemistry , vol.85 , Issue.4 , pp. 641-648
    • Peñasa, E.1    Préstamo, G.2    Gomezb, R.3
  • 22
    • 18344416037 scopus 로고    scopus 로고
    • Functional properties of improved glycinin and b-conglycinin fractions
    • Rickert D.A., Johnson L.A., Murphy P.A. Functional properties of improved glycinin and b-conglycinin fractions. Journal of Food Science 2004, 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
  • 24
    • 0032001694 scopus 로고
    • Effect of dynamic high pressure on the secondary structure of b-lactoglobulin and on its conformational properties as determined by Fourier transform infrared spectroscopy
    • Subirade M., Loupil F., Allain A.F., Paquin P. Effect of dynamic high pressure on the secondary structure of b-lactoglobulin and on its conformational properties as determined by Fourier transform infrared spectroscopy. International Dairy Journal 1981, 8:135-140.
    • (1981) International Dairy Journal , vol.8 , pp. 135-140
    • Subirade, M.1    Loupil, F.2    Allain, A.F.3    Paquin, P.4
  • 25
    • 55549102634 scopus 로고    scopus 로고
    • Effect of high pressure treatment on aggregation and structural properties of soy protein isolate
    • Tang C.H., Ma C.Y. Effect of high pressure treatment on aggregation and structural properties of soy protein isolate. LWT - Food Science and Technology 2009, 42:606-611.
    • (2009) LWT - Food Science and Technology , vol.42 , pp. 606-611
    • Tang, C.H.1    Ma, C.Y.2
  • 26
    • 60249084349 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates
    • Tang C.H., Wang X.S., Yang X.C. Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates. Food Chemistry 2009, 114:1484-1490.
    • (2009) Food Chemistry , vol.114 , pp. 1484-1490
    • Tang, C.H.1    Wang, X.S.2    Yang, X.C.3
  • 27
    • 61349110033 scopus 로고    scopus 로고
    • Formation of soluble aggregates from insoluble commercial soy protein isolated by means of ultrasonic treatment and their gelling properties
    • Tang C.H., Wang X.Y., Yang X.C., Li L. Formation of soluble aggregates from insoluble commercial soy protein isolated by means of ultrasonic treatment and their gelling properties. Journal of Food Engineering 2009, 92:432-437.
    • (2009) Journal of Food Engineering , vol.92 , pp. 432-437
    • Tang, C.H.1    Wang, X.Y.2    Yang, X.C.3    Li, L.4
  • 29
    • 0041643782 scopus 로고
    • Studies on the cold insoluble fraction of the water extractable soybean proteins II. Factors influencing conformation changes in the 11S component
    • Wolf W.J., Briggs D.R. Studies on the cold insoluble fraction of the water extractable soybean proteins II. Factors influencing conformation changes in the 11S component. Archive of Biochemistry and Biophysics 1958, 76:377-393.
    • (1958) Archive of Biochemistry and Biophysics , vol.76 , pp. 377-393
    • Wolf, W.J.1    Briggs, D.R.2
  • 30
    • 0002534162 scopus 로고
    • Improvement of the emulsifi{ligature}cation properties of soy protein by limited pepsin hydrolysis
    • Zakaria F., McFeeters R.F. Improvement of the emulsifi{ligature}cation properties of soy protein by limited pepsin hydrolysis. Lebensmittel- Wissenschaft und- Technologie 1978, 11:42-44.
    • (1978) Lebensmittel- Wissenschaft und- Technologie , vol.11 , pp. 42-44
    • Zakaria, F.1    McFeeters, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.