메뉴 건너뛰기




Volumn 49, Issue 12, 2014, Pages 2529-2537

Gelation enhancement of soy protein isolate by sequential low- and ultrahigh-temperature two-stage preheating treatments

Author keywords

Gelling property; Solubility; Soy protein isolate; Two stage heating; Ultrahigh temperature

Indexed keywords

GELATION; PREHEATING; SOLUBILITY; SULFUR COMPOUNDS;

EID: 84939192070     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/ijfs.12694     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 0019346123 scopus 로고
    • Limited enzymic degradation of proteins: a new approach in the industrial application of hydrolases
    • Adler-Nissen, J. (1982). Limited enzymic degradation of proteins: a new approach in the industrial application of hydrolases. Journal of Chemical Technology and Biotechnology, 32, 138-156.
    • (1982) Journal of Chemical Technology and Biotechnology , vol.32 , pp. 138-156
    • Adler-Nissen, J.1
  • 2
    • 84939153350 scopus 로고
    • Extraction of soy protein
    • United States Patent Office
    • Anson, M.L. (1957). Extraction of soy protein. In: United States Patent Office, Patent No. 2785155.
    • (1957)
    • Anson, M.L.1
  • 4
    • 85032119438 scopus 로고
    • Determination of SH- and SS- groups in some food proteins using Ellman's reagent
    • Beveridge, T., Toma, S. & Nakai, S. (1974). Determination of SH- and SS- groups in some food proteins using Ellman's reagent. Journal of Food Science, 39, 49-51.
    • (1974) Journal of Food Science , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.2    Nakai, S.3
  • 5
    • 0000176234 scopus 로고
    • Gelation enhancement of soy protein isolate using the Maillard reaction and high temperatures
    • Cabodevila, O., Hill, S.E., Armstrong, H.J., Sousa, I. & Mitchell, J.R. (1994). Gelation enhancement of soy protein isolate using the Maillard reaction and high temperatures. Journal of Food Science, 59, 872-875.
    • (1994) Journal of Food Science , vol.59 , pp. 872-875
    • Cabodevila, O.1    Hill, S.E.2    Armstrong, H.J.3    Sousa, I.4    Mitchell, J.R.5
  • 6
    • 51049098678 scopus 로고    scopus 로고
    • Effects of heat treatment and glucono-delta-lactone-induced acidification on characteristics of soy protein isolate
    • Campbell, L.J., Gu, X., Dewar, S.J. & Euston, S.R. (2009). Effects of heat treatment and glucono-delta-lactone-induced acidification on characteristics of soy protein isolate. Food Hydrocolloids, 23, 344-351.
    • (2009) Food Hydrocolloids , vol.23 , pp. 344-351
    • Campbell, L.J.1    Gu, X.2    Dewar, S.J.3    Euston, S.R.4
  • 7
    • 84882589540 scopus 로고    scopus 로고
    • Physical properties of soy bean and broad bean 11S globulin gels formed by transglutaminase reaction
    • Chanyongvorakul, Y., Matsumura, Y., Nonaka, M., Motoki, M. & Mori, T. (2006). Physical properties of soy bean and broad bean 11S globulin gels formed by transglutaminase reaction. Journal of Food Science, 60, 483-488.
    • (2006) Journal of Food Science , vol.60 , pp. 483-488
    • Chanyongvorakul, Y.1    Matsumura, Y.2    Nonaka, M.3    Motoki, M.4    Mori, T.5
  • 8
    • 0036813469 scopus 로고    scopus 로고
    • Interaction of myofibrillar and preheated soy proteins
    • Feng, J. & Xiong, Y. (2002). Interaction of myofibrillar and preheated soy proteins. Journal of Food Science, 67, 2851-2856.
    • (2002) Journal of Food Science , vol.67 , pp. 2851-2856
    • Feng, J.1    Xiong, Y.2
  • 10
    • 0000786151 scopus 로고
    • Recent progress of soybean protein foods:chemistry, technology, and nutrition
    • Fukushima, D. (1991). Recent progress of soybean protein foods:chemistry, technology, and nutrition. Food Reviews International, 7, 323-351.
    • (1991) Food Reviews International , vol.7 , pp. 323-351
    • Fukushima, D.1
  • 11
    • 46049101599 scopus 로고    scopus 로고
    • Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase and Maillard cross-linking
    • Gan, C.Y., Cheng, L.H. & Easa, A.M. (2008). Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase and Maillard cross-linking. Food Research International, 41, 600-605.
    • (2008) Food Research International , vol.41 , pp. 600-605
    • Gan, C.Y.1    Cheng, L.H.2    Easa, A.M.3
  • 12
    • 84874416406 scopus 로고    scopus 로고
    • The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate
    • Hu, H., Li-Chan, E.C.Y., Wan, L., Tian, M. & Pan, S. (2013). The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32, 303-311.
    • (2013) Food Hydrocolloids , vol.32 , pp. 303-311
    • Hu, H.1    Li-Chan, E.C.Y.2    Wan, L.3    Tian, M.4    Pan, S.5
  • 14
    • 84870558602 scopus 로고    scopus 로고
    • Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase
    • Jiang, J. & Xiong, Y.L. (2013). Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase. Meat Science, 93, 469-476.
    • (2013) Meat Science , vol.93 , pp. 469-476
    • Jiang, J.1    Xiong, Y.L.2
  • 15
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato, A. & Nakai, S. (1980). Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta (BBA)-Protein Structure, 624, 13-20.
    • (1980) Biochimica et Biophysica Acta (BBA)-Protein Structure , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 17
    • 79551479183 scopus 로고    scopus 로고
    • Effect of microwave heating on the viscoelastic property and microstructure of soy protein isolate gel
    • Liu, H.H. & Kuo, M.I. (2011). Effect of microwave heating on the viscoelastic property and microstructure of soy protein isolate gel. Journal of Texture Studies, 42, 1-9.
    • (2011) Journal of Texture Studies , vol.42 , pp. 1-9
    • Liu, H.H.1    Kuo, M.I.2
  • 18
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu, G. & Xiong, Y.L. (2000). Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. Journal of Agricultural and Food Chemistry, 48, 624-630.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 19
    • 0000229099 scopus 로고    scopus 로고
    • Dynamic viscoelastic study on the gelation properties of β-conglycinin-rich and glycinin-rich soybean protein isolates
    • Nagano, T., Fukuda, Y. & Akasaka, T. (1996). Dynamic viscoelastic study on the gelation properties of β-conglycinin-rich and glycinin-rich soybean protein isolates. Journal of Agricultural and Food Chemistry, 44, 3484-3488.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 3484-3488
    • Nagano, T.1    Fukuda, Y.2    Akasaka, T.3
  • 23
    • 0001565172 scopus 로고    scopus 로고
    • Structural properties of heat-induced soy protein gels as affected by ionic strength and pH
    • Puppo, M.C. & Añón, M.C. (1998). Structural properties of heat-induced soy protein gels as affected by ionic strength and pH. Journal of Agricultural and Food Chemistry, 46, 3583-3589.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 3583-3589
    • Puppo, M.C.1    Añón, M.C.2
  • 24
    • 84907421742 scopus 로고
    • Gelation of soybean protein isolates in acidic conditions. Effect of pH and protein concentration
    • Puppo, M.C., Lupano, C.E. & Añón, M.C. (1995). Gelation of soybean protein isolates in acidic conditions. Effect of pH and protein concentration. Journal of Agricultural and Food Chemistry, 43, 2356-2361.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2356-2361
    • Puppo, M.C.1    Lupano, C.E.2    Añón, M.C.3
  • 26
    • 0035186748 scopus 로고    scopus 로고
    • Gel formation by [beta]-conglycinin and glycinin and their mixtures
    • Renkema, J., Knabben, J. & Van Vliet, T. (2001). Gel formation by [beta]-conglycinin and glycinin and their mixtures. Food Hydrocolloids, 15, 407-414.
    • (2001) Food Hydrocolloids , vol.15 , pp. 407-414
    • Renkema, J.1    Knabben, J.2    Van Vliet, T.3
  • 27
    • 7444224672 scopus 로고    scopus 로고
    • Effect of extraction pH and temperature on isoflavone and saponin partitioning and profile during soy protein isolate production
    • Rickert, D., Meyer, M., Hu, J. & Murphy, P. (2004). Effect of extraction pH and temperature on isoflavone and saponin partitioning and profile during soy protein isolate production. Journal of Food Science, 69, C623-C631.
    • (2004) Journal of Food Science , vol.69 , pp. C623-C631
    • Rickert, D.1    Meyer, M.2    Hu, J.3    Murphy, P.4
  • 28
    • 0040058658 scopus 로고
    • Relation between denaturation and some functional properties of soybean protein
    • Shiga, K. & Nakamura, Y. (1987). Relation between denaturation and some functional properties of soybean protein. Journal of Food Science, 52, 681-684.
    • (1987) Journal of Food Science , vol.52 , pp. 681-684
    • Shiga, K.1    Nakamura, Y.2
  • 29
    • 84907421527 scopus 로고
    • Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions
    • Sorgentini, D.A., Wagner, J.R. & Añón, M.C. (1995). Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions. Journal of Agricultural and Food Chemistry, 43, 2471-2479.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2471-2479
    • Sorgentini, D.A.1    Wagner, J.R.2    Añón, M.C.3
  • 30
    • 84907421523 scopus 로고    scopus 로고
    • Gelation of soybean proteins induced by sequential high-pressure and thermal treatments
    • Speroni, F., Beaumal, V., De Lamballerie, M., Anton, M., Añón, M. & Puppo, M. (2009). Gelation of soybean proteins induced by sequential high-pressure and thermal treatments. Food Hydrocolloids, 23, 1433-1442.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1433-1442
    • Speroni, F.1    Beaumal, V.2    De Lamballerie, M.3    Anton, M.4    Añón, M.5    Puppo, M.6
  • 31
    • 74249086246 scopus 로고    scopus 로고
    • Effects of calcium and pressure treatment on thermal gelation of soybean protein
    • Speroni, F., Jung, S. & De Lamballerie, M. (2010). Effects of calcium and pressure treatment on thermal gelation of soybean protein. Journal of Food Science, 75, E30-E38.
    • (2010) Journal of Food Science , vol.75 , pp. E30-E38
    • Speroni, F.1    Jung, S.2    De Lamballerie, M.3
  • 32
    • 26844437327 scopus 로고    scopus 로고
    • Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase
    • Tang, C.H., Wu, H., Chen, Z. & Yang, X.Q. (2006). Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Research International, 39, 87-97.
    • (2006) Food Research International , vol.39 , pp. 87-97
    • Tang, C.H.1    Wu, H.2    Chen, Z.3    Yang, X.Q.4
  • 33
    • 61349110033 scopus 로고    scopus 로고
    • Formation of soluble aggregates from insoluble commercial soy protein isolate by means of ultrasonic treatment and their gelling properties
    • Tang, C.H., Wang, X.Y., Yang, X.Q. & Li, L. (2009). Formation of soluble aggregates from insoluble commercial soy protein isolate by means of ultrasonic treatment and their gelling properties. Journal of Food Engineering, 92, 432-437.
    • (2009) Journal of Food Engineering , vol.92 , pp. 432-437
    • Tang, C.H.1    Wang, X.Y.2    Yang, X.Q.3    Li, L.4
  • 34
    • 85008191781 scopus 로고
    • Effect of physical and chemical factors on rheological behavior of commercial soy protein isolates: protein concentration, water imbibing capacity, salt addition, and thermal treatment
    • Wagner, J.R., Sorgentini, D.A. & Añón, M.C. (1992). Effect of physical and chemical factors on rheological behavior of commercial soy protein isolates: protein concentration, water imbibing capacity, salt addition, and thermal treatment. Journal of Agricultural and Food Chemistry, 40, 1930-1937.
    • (1992) Journal of Agricultural and Food Chemistry , vol.40 , pp. 1930-1937
    • Wagner, J.R.1    Sorgentini, D.A.2    Añón, M.C.3
  • 35
    • 0033852356 scopus 로고    scopus 로고
    • Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates
    • Wagner, J.R., Sorgentini, D.A. & Añón, M.C. (2000). Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates. Journal of Agricultural and Food Chemistry, 48, 3159-3165.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 3159-3165
    • Wagner, J.R.1    Sorgentini, D.A.2    Añón, M.C.3
  • 36
    • 0035247893 scopus 로고    scopus 로고
    • Functional properties of hydrothermally cooked soy protein products
    • Wang, C. & Johnson, L.A. (2001). Functional properties of hydrothermally cooked soy protein products. Journal of the American Oil Chemists' Society, 78, 189-195.
    • (2001) Journal of the American Oil Chemists' Society , vol.78 , pp. 189-195
    • Wang, C.1    Johnson, L.A.2
  • 37
    • 30344460965 scopus 로고    scopus 로고
    • Effect of alkali on the refunctionalization of soy protein by hydrothermal cooking
    • Wang, H., Wang, T. & Johnson, L. (2005). Effect of alkali on the refunctionalization of soy protein by hydrothermal cooking. Journal of the American Oil Chemists' Society, 82, 451-456.
    • (2005) Journal of the American Oil Chemists' Society , vol.82 , pp. 451-456
    • Wang, H.1    Wang, T.2    Johnson, L.3
  • 38
    • 79959923003 scopus 로고    scopus 로고
    • Rheology and microstructure of myofibrillar protein-plant lipid composite gels: effect of emulsion droplet size and membrane type
    • Wu, M., Xiong, Y.L. & Chen, J. (2011). Rheology and microstructure of myofibrillar protein-plant lipid composite gels: effect of emulsion droplet size and membrane type. Journal of Food Engineering, 106, 318-324.
    • (2011) Journal of Food Engineering , vol.106 , pp. 318-324
    • Wu, M.1    Xiong, Y.L.2    Chen, J.3
  • 39
    • 34247187913 scopus 로고
    • Molecular understanding of heat-induced phenomena of soybean protein
    • Yamauchi, F., Yamagishi, T. & Iwabuchi, S. (1991). Molecular understanding of heat-induced phenomena of soybean protein. Food Reviews International, 7, 283-322.
    • (1991) Food Reviews International , vol.7 , pp. 283-322
    • Yamauchi, F.1    Yamagishi, T.2    Iwabuchi, S.3
  • 40
    • 39149111921 scopus 로고    scopus 로고
    • Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties
    • Zheng, H.G., Yang, X.Q., Tang, C.H., Li, L. & Ahmad, I. (2008). Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties. Food Research International, 41, 154-164.
    • (2008) Food Research International , vol.41 , pp. 154-164
    • Zheng, H.G.1    Yang, X.Q.2    Tang, C.H.3    Li, L.4    Ahmad, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.