메뉴 건너뛰기




Volumn 27, Issue 4, 2013, Pages 609-615

Effects of high hydrostatic pressure on the solubility and molecular structure of rice protein

Author keywords

Electrophoresis; High pressure; Molecular structure; Rice protein; Solubility

Indexed keywords


EID: 84890855233     PISSN: 10005773     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (21)
  • 1
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra-and intermolecular interactions within proteins
    • Boonchai B B, Chan B P, Douglas S C. Pressure effects on intra-and intermolecular interactions within proteins [J]. Biochim Biophys Acta, 2002, 1595 (1/2): 235-249.
    • (2002) Biochim Biophys Acta , vol.1595 , Issue.1-2 , pp. 235-249
    • Boonchai, B.B.1    Chan, B.P.2    Douglas, S.C.3
  • 2
    • 23844444764 scopus 로고    scopus 로고
    • The powerful high pressure tool for protein conformational studies
    • Marchal S, Torrent J, Masson P, et al. The powerful high pressure tool for protein conformational studies [J]. Braz J Med Biol Res, 2005, 38 (8): 1175-1183.
    • (2005) Braz J Med Biol Res , vol.38 , Issue.8 , pp. 1175-1183
    • Marchal, S.1    Torrent, J.2    Masson, P.3
  • 3
    • 44349182739 scopus 로고    scopus 로고
    • Review of modelling and simulation of high pressure treatment of materials of biological origin
    • Delgado A, Rauh C, Kowalczyk W, et al. Review of modelling and simulation of high pressure treatment of materials of biological origin [J]. Trends Food Sci Tech, 2008, 19 (6): 329-336.
    • (2008) Trends Food Sci Tech , vol.19 , Issue.6 , pp. 329-336
    • Delgado, A.1    Rauh, C.2    Kowalczyk, W.3
  • 4
    • 33645973697 scopus 로고    scopus 로고
    • What lies in the future of high-pressure bioscience?
    • Balny C. What lies in the future of high-pressure bioscience? [J]. Biochim Biophys Acta, 2006, 1764 (3): 632-639.
    • (2006) Biochim Biophys Acta , vol.1764 , Issue.3 , pp. 632-639
    • Balny, C.1
  • 5
    • 50949083505 scopus 로고    scopus 로고
    • The principles of ultra high pressure technology and its application in food processing/preservation: A review of microbiological and quality aspects
    • Yaldagard M, Mortazavi S A, Tabatabaie F. The principles of ultra high pressure technology and its application in food processing/preservation: A review of microbiological and quality aspects [J]. Afr J Biotechnol, 2008, 7: 2739-2767.
    • (2008) Afr J Biotechnol , vol.7 , pp. 2739-2767
    • Yaldagard, M.1    Mortazavi, S.A.2    Tabatabaie, F.3
  • 6
    • 42449089823 scopus 로고    scopus 로고
    • High hydrostatic pressure modification of whey protein concentrate for improved functional properties
    • Lim S Y, Swanson B G, Clark S. High hydrostatic pressure modification of whey protein concentrate for improved functional properties [J]. J Dairy Sci, 2008, 91 (4): 1299-1307.
    • (2008) J Dairy Sci , vol.91 , Issue.4 , pp. 1299-1307
    • Lim, S.Y.1    Swanson, B.G.2    Clark, S.3
  • 7
    • 0035021485 scopus 로고    scopus 로고
    • Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins
    • Molina E, Papadopoulou A, Ledward D A. Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins [J]. Food Hydrocolloid, 2001, 15 (3): 263-269.
    • (2001) Food Hydrocolloid , vol.15 , Issue.3 , pp. 263-269
    • Molina, E.1    Papadopoulou, A.2    Ledward, D.A.3
  • 8
    • 34047259662 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: Studies on gluten, gliadin and glutenin
    • Kieffer R, Schurer F, Köhler P, et al. Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: Studies on gluten, gliadin and glutenin [J]. J Cereal Sci, 2007, 45 (3): 285-292.
    • (2007) J Cereal Sci , vol.45 , Issue.3 , pp. 285-292
    • Kieffer, R.1    Schurer, F.2    Köhler, P.3
  • 9
    • 84890848248 scopus 로고    scopus 로고
    • Changes of solubility and rheological property of the isolated soybean protein after high pressure treatment and its mechanism
    • in Chinese
    • Li B S, Zeng Q X, Peng Z Y, et al. Changes of solubility and rheological property of the isolated soybean protein after high pressure treatment and its mechanism [J]. Chinese Journal of High Pressure Physics, 1999, 13 (1): 22-29.(in Chinese)
    • (1999) Chinese Journal of High Pressure Physics , vol.13 , Issue.1 , pp. 22-29
    • Li, B.S.1    Zeng, Q.X.2    Peng, Z.Y.3
  • 10
    • 33744502150 scopus 로고    scopus 로고
    • Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim mil
    • Patel H A, Singh H, Anema S G, et al. Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk [J]. J Agric Food Chem, 2006, 54 (9): 3409-3420.
    • (2006) J Agric Food Chem , vol.54 , Issue.9 , pp. 3409-3420
    • Patel, H.A.1    Singh, H.2    Anema, S.G.3
  • 11
    • 55549102634 scopus 로고    scopus 로고
    • Effect of high pressure treatment on aggregation and structural properties of soy protein isolate
    • Tang C He, Ma C Y. Effect of high pressure treatment on aggregation and structural properties of soy protein isolate [J]. LWT-Food Sci Tech, 2009, 42 (2): 606-611.
    • (2009) LWT-Food Sci Tech , vol.42 , Issue.2 , pp. 606-611
    • Tang, C.H.1    Ma, C.Y.2
  • 12
    • 31344467064 scopus 로고    scopus 로고
    • Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure
    • Lee S H, Carpenter J F, Chang B S, et al. Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure [J]. Protein Sci, 2006, 15 (2): 304-313.
    • (2006) Protein Sci , vol.15 , Issue.2 , pp. 304-313
    • Lee, S.H.1    Carpenter, J.F.2    Chang, B.S.3
  • 13
    • 17444399352 scopus 로고    scopus 로고
    • Effects of high pressure and microwave on pronase and α-chymotrypsin hydrolysis of β-lactoglobulin
    • Izquierdo F J, Alli I, Gomez R, et al. Effects of high pressure and microwave on pronase and α-chymotrypsin hydrolysis of β-lactoglobulin [J]. Food Chem, 2005, 92 (2): 713-719.
    • (2005) Food Chem , vol.92 , Issue.2 , pp. 713-719
    • Izquierdo, F.J.1    Alli, I.2    Gomez, R.3
  • 14
    • 36348936097 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin
    • Zeece M, Huppertz T, Kelly A. Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin [J]. Innovat Food Sci Emerg Tech, 2008, 9 (1): 62-69.
    • (2008) Innovat Food Sci Emerg Tech , vol.9 , Issue.1 , pp. 62-69
    • Zeece, M.1    Huppertz, T.2    Kelly, A.3
  • 15
    • 4444270688 scopus 로고    scopus 로고
    • Kinetic study on the changes in the susceptibility of egg white proteins to enzymatic hydrolysis induced by heat and high hydrostatic pressure pretreatment
    • van der Plancken I, Delattre M, Indrawati I, et al. Kinetic study on the changes in the susceptibility of egg white proteins to enzymatic hydrolysis induced by heat and high hydrostatic pressure pretreatment [J]. J Agric Food Chem, 2004, 52 (18): 5621-5626.
    • (2004) J Agric Food Chem , vol.52 , Issue.18 , pp. 5621-5626
    • van der Plancken, I.1    Delattre, M.2    Indrawati, I.3
  • 16
    • 34249093940 scopus 로고    scopus 로고
    • The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin
    • Quiros A, Chichon R, Recio I, et al. The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin [J]. Food Chem, 2007, 104 (4): 1734-1739.
    • (2007) Food Chem , vol.104 , Issue.4 , pp. 1734-1739
    • Quiros, A.1    Chichon, R.2    Recio, I.3
  • 17
    • 0942278928 scopus 로고    scopus 로고
    • High pressure and the enzymatic hydrolysis of soybean whey proteins
    • Penas E, Prestamo G, Rosario G. High pressure and the enzymatic hydrolysis of soybean whey proteins [J]. Food Chem, 2004, 85 (4): 641-648.
    • (2004) Food Chem , vol.85 , Issue.4 , pp. 641-648
    • Penas, E.1    Prestamo, G.2    Rosario, G.3
  • 18
    • 84890809825 scopus 로고    scopus 로고
    • Characteristics and structure of thermo-denatured rice proteins-II. Characterization of rice protein fractions
    • in Chinese
    • Wang Z C, Dong J L, Zheng J Q, et al. Characteristics and structure of thermo-denatured rice proteins-II. Characterization of rice protein fractions [J]. Journal of the Chinese Cereals and Oils Association, 2008, 23 (4): 1-4.(in Chinese)
    • (2008) Journal of the Chinese Cereals and Oils Association , vol.23 , Issue.4 , pp. 1-4
    • Wang, Z.C.1    Dong, J.L.2    Zheng, J.Q.3
  • 19
    • 84890823333 scopus 로고    scopus 로고
    • Mechanism of enzymetic hydrolysis of rice protein (II): Change of protein components during hydrolysis
    • in Chinese
    • Wang Z C, Liu W D, Shen R L, et al. Mechanism of enzymetic hydrolysis of rice protein (II): Change of protein components during hydrolysis [J]. Journal of the Chinese Cereals and Oils Association, 2007, 22 (4): 5-8.(in Chinese)
    • (2007) Journal of the Chinese Cereals and Oils Association , vol.22 , Issue.4 , pp. 5-8
    • Wang, Z.C.1    Liu, W.D.2    Shen, R.L.3
  • 20
    • 85032119438 scopus 로고
    • Determination of SH-and SS-groups in some food proteins using Ellman's reagent
    • Beveridge T, Toma S J, Nakai S. Determination of SH-and SS-groups in some food proteins using Ellman's reagent [J]. J Food Sci, 1974, 39 (1): 49-51.
    • (1974) J Food Sci , vol.39 , Issue.1 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.3
  • 21
    • 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 [J]. Nature, 1970, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.