메뉴 건너뛰기




Volumn 92, Issue 1, 2014, Pages 30-37

Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate

Author keywords

Emulsifying properties; Peanut protein isolate; Structure; Surface hydrophobicity; Ultrasonic treatment

Indexed keywords

EMULSIFYING ACTIVITY INDICES; EMULSIFYING PROPERTY; ENVIRONMENTAL SCANNING ELECTRON MICROSCOPIES (ESEM); PEANUT PROTEIN ISOLATES (PPI); PEANUT PROTEINS; PROTEIN SURFACE HYDROPHOBICITIES; SURFACE HYDROPHOBICITY; ULTRASONIC TREATMENTS;

EID: 84892374387     PISSN: 09603085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fbp.2013.07.006     Document Type: Article
Times cited : (294)

References (35)
  • 1
    • 33845555305 scopus 로고
    • Composition and characteristics of basic proteins from peanut (Arachis hypogaea L.) seed
    • S.M. Basha, and S.K. Pancholy Composition and characteristics of basic proteins from peanut (Arachis hypogaea L.) seed J. Agric. Food Chem. 30 1982 1176 1179
    • (1982) J. Agric. Food Chem. , vol.30 , pp. 1176-1179
    • Basha, S.M.1    Pancholy, S.K.2
  • 3
    • 79952758423 scopus 로고    scopus 로고
    • Effects of ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates
    • L. Chen, J. Chen, J. Ren, and M. Zhao Effects of ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates J. Agric. Food Chem. 59 2011 2600 2609
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 2600-2609
    • Chen, L.1    Chen, J.2    Ren, J.3    Zhao, M.4
  • 4
    • 0001761960 scopus 로고
    • Comments on the evolving field of sonochemistry by a cavitation physicist
    • L.A. Crum Comments on the evolving field of sonochemistry by a cavitation physicist Ultrason. Sonochem. 2 1995 S147 S152
    • (1995) Ultrason. Sonochem. , vol.2
    • Crum, L.A.1
  • 6
    • 33749386447 scopus 로고    scopus 로고
    • Structural and functional changes in ultrasonicated bovine serum albumin solutions
    • İ. Gülseren, D. Güzey, B.D. Bruce, and J. Weiss Structural and functional changes in ultrasonicated bovine serum albumin solutions Ultrason. Sonochem. 14 2007 173 183
    • (2007) Ultrason. Sonochem. , vol.14 , pp. 173-183
    • Gülseren, I.1    Güzey, D.2    Bruce, B.D.3    Weiss, J.4
  • 8
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • N.J. Greenfield, and G.D. Fasman Computed circular dichroism spectra for the evaluation of protein conformation Biochem. 8 1969 4108 4116
    • (1969) Biochem. , vol.8 , pp. 4108-4116
    • Greenfield, N.J.1    Fasman, G.D.2
  • 10
    • 0015807889 scopus 로고
    • Conformations of oilseed storage proteins (globulins) determined by circular dichroism
    • T. Jacks, R. Barker, and O. Weigang Jr. Conformations of oilseed storage proteins (globulins) determined by circular dichroism Int. J. Pept. Protein Res. 5 1973 289 291
    • (1973) Int. J. Pept. Protein Res. , vol.5 , pp. 289-291
    • Jacks, T.1    Barker, R.2    Weigang, Jr.O.3
  • 11
    • 75749122983 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate
    • S. Jamdar, V. Rajalakshmi, M. Pednekar, F. Juan, V. Yardi, and A. Sharma Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate Food Chem. 121 2010 178 184
    • (2010) Food Chem. , vol.121 , pp. 178-184
    • Jamdar, S.1    Rajalakshmi, V.2    Pednekar, M.3    Juan, F.4    Yardi, V.5    Sharma, A.6
  • 12
    • 4043149377 scopus 로고    scopus 로고
    • Effect of high power ultrasound waves on properties of meat: A review
    • S. Jayasooriya, B. Bhandari, P. Torley, and B. D'Arcy Effect of high power ultrasound waves on properties of meat: a review Int. J. Food Prop. 7 2004 301 319
    • (2004) Int. J. Food Prop. , vol.7 , pp. 301-319
    • Jayasooriya, S.1    Bhandari, B.2    Torley, P.3    D'Arcy, B.4
  • 15
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • A. Kato, and S. Nakai Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins Biochim. Biophys. Acta-Protein Struct. 624 1980 13 20
    • (1980) Biochim. Biophys. Acta-Protein Struct. , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 16
    • 39549116952 scopus 로고    scopus 로고
    • Influence of novel food processing technologies on the rheological and thermophysical properties of whey proteins
    • G. Krešić, V. Lelas, A.R. Jambrak, Z. Herceg, and S.R. Brnčić Influence of novel food processing technologies on the rheological and thermophysical properties of whey proteins J. Food Eng. 87 2008 64 73
    • (2008) J. Food Eng. , vol.87 , pp. 64-73
    • Krešić, G.1    Lelas, V.2    Jambrak, A.R.3    Herceg, Z.4    Brnčić, S.R.5
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 79955624347 scopus 로고    scopus 로고
    • Relationship between functional properties and aggregation changes of whey protein induced by high pressure microfluidization
    • C.M. Liu, J.Z. Zhong, W. Liu, Z.C. Tu, J. Wan, X.F. Cai, and X.Y. Song Relationship between functional properties and aggregation changes of whey protein induced by high pressure microfluidization J. Food Sci. 76 2011 E341 E347
    • (2011) J. Food Sci. , vol.76
    • Liu, C.M.1    Zhong, J.Z.2    Liu, W.3    Tu, Z.C.4    Wan, J.5    Cai, X.F.6    Song, X.Y.7
  • 19
    • 77954620043 scopus 로고    scopus 로고
    • The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin
    • W. Liu, Z.-Q. Zhang, C.-M. Liu, M.-Y. Xie, Z.-C. Tu, J.-H. Liu, and R.-H. Liang The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin Food Chem. 123 2010 616 621
    • (2010) Food Chem. , vol.123 , pp. 616-621
    • Liu, W.1    Zhang, Z.-Q.2    Liu, C.-M.3    Xie, M.-Y.4    Tu, Z.-C.5    Liu, J.-H.6    Liang, R.-H.7
  • 20
    • 80755125220 scopus 로고    scopus 로고
    • Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction
    • Y. Liu, G. Zhao, M. Zhao, J. Ren, and B. Yang Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction Food Chem. 131 2011 901 906
    • (2011) Food Chem. , vol.131 , pp. 901-906
    • Liu, Y.1    Zhao, G.2    Zhao, M.3    Ren, J.4    Yang, B.5
  • 21
    • 34249019182 scopus 로고    scopus 로고
    • Ultrasound-assisted crystallization (sonocrystallization)
    • M. Luque de Castro, and F. Priego-Capote Ultrasound-assisted crystallization (sonocrystallization) Ultrason. Sonochem. 14 2007 717 724
    • (2007) Ultrason. Sonochem. , vol.14 , pp. 717-724
    • Luque De Castro, M.1    Priego-Capote, F.2
  • 22
    • 0030197068 scopus 로고    scopus 로고
    • Ultrasonic intensification of chemical processing and related operations: A review
    • T. Mason, and E. Cordemans Ultrasonic intensification of chemical processing and related operations: a review Chem. Eng. Res. Des. 74 1996 511 516
    • (1996) Chem. Eng. Res. Des. , vol.74 , pp. 511-516
    • Mason, T.1    Cordemans, E.2
  • 23
    • 84859004102 scopus 로고    scopus 로고
    • Effect of osmosis and ultrasound pretreatment on the moisture adsorption isotherms of quince
    • M. Noshad, M. Mohebbi, F. Shahidi, and S.A. Mortazavi Effect of osmosis and ultrasound pretreatment on the moisture adsorption isotherms of quince Food Bioprod. Process. 90 2012 266 274
    • (2012) Food Bioprod. Process. , vol.90 , pp. 266-274
    • Noshad, M.1    Mohebbi, M.2    Shahidi, F.3    Mortazavi, S.A.4
  • 24
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • I. Pallarès, J. Vendrell, F.X. Avilés, and S. Ventura Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin J. Mol. Biol. 342 2004 321 331
    • (2004) J. Mol. Biol. , vol.342 , pp. 321-331
    • Pallarès, I.1    Vendrell, J.2    Avilés, F.X.3    Ventura, S.4
  • 25
    • 0942278928 scopus 로고    scopus 로고
    • High pressure and the enzymatic hydrolysis of soybean whey proteins
    • E. Penas, G. Préstamo, and R. Gomez High pressure and the enzymatic hydrolysis of soybean whey proteins Food Chem. 85 2004 641 648
    • (2004) Food Chem. , vol.85 , pp. 641-648
    • Penas, E.1    Préstamo, G.2    Gomez, R.3
  • 26
    • 84859152164 scopus 로고    scopus 로고
    • Microfluidization as a potential technique to modify surface properties of soy protein isolate
    • L. Shen, and C.-H. Tang Microfluidization as a potential technique to modify surface properties of soy protein isolate Food Research International 48 2012 108 118
    • (2012) Food Research International , vol.48 , pp. 108-118
    • Shen, L.1    Tang, C.-H.2
  • 27
    • 84907421527 scopus 로고
    • Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions
    • D.A. Sorgentini, J.R. Wagner, and M.C. Anon Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions J. Agric. Food Chem. 43 1995 2471 2479
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2471-2479
    • Sorgentini, D.A.1    Wagner, J.R.2    Anon, M.C.3
  • 28
    • 77954083367 scopus 로고    scopus 로고
    • Effect of ultrasound on the technological properties and bioactivity of food: A review
    • A.C. Soria, and M. Villamiel Effect of ultrasound on the technological properties and bioactivity of food: a review Trends Food Sci. Tech. 21 2010 323 331
    • (2010) Trends Food Sci. Tech. , vol.21 , pp. 323-331
    • Soria, A.C.1    Villamiel, M.2
  • 29
    • 0000974490 scopus 로고
    • Functionality of flours, protein fractions and isolates from field peas and faba bean
    • F. Sosulski, and A. McCurdy Functionality of flours, protein fractions and isolates from field peas and faba bean J. Food Sci. 52 1987 1010 1014
    • (1987) J. Food Sci. , vol.52 , pp. 1010-1014
    • Sosulski, F.1    McCurdy, A.2
  • 30
    • 38949131508 scopus 로고    scopus 로고
    • Applications and opportunities for ultrasound assisted extraction in the food industry-A review
    • K. Vilkhu, R. Mawson, L. Simons, and D. Bates Applications and opportunities for ultrasound assisted extraction in the food industry-A review Innov. Food Sci. Emerg. Technol. 9 2008 161 169
    • (2008) Innov. Food Sci. Emerg. Technol. , vol.9 , pp. 161-169
    • Vilkhu, K.1    Mawson, R.2    Simons, L.3    Bates, D.4
  • 31
    • 0034408369 scopus 로고    scopus 로고
    • Degassing of milk by high-intensity ultrasound
    • M. Villamiel, R. Verdurmen, and P. Jong Degassing of milk by high-intensity ultrasound Milchwissenschaft 55 2000 123 125
    • (2000) Milchwissenschaft , vol.55 , pp. 123-125
    • Villamiel, M.1    Verdurmen, R.2    Jong, P.3
  • 32
    • 0002609034 scopus 로고
    • Relationships of hydrophobicity to emulsifying properties of heat denatured proteins
    • L.P. Voutsinas, E. Cheung, and S. Nakai Relationships of hydrophobicity to emulsifying properties of heat denatured proteins J. Food Sci. 48 1983 26 32
    • (1983) J. Food Sci. , vol.48 , pp. 26-32
    • Voutsinas, L.P.1    Cheung, E.2    Nakai, S.3
  • 33
    • 60749134640 scopus 로고    scopus 로고
    • Comparative studies on the functional properties of various protein concentrate preparations of peanut protein
    • H. Wu, Q. Wang, T. Ma, and J. Ren Comparative studies on the functional properties of various protein concentrate preparations of peanut protein Food Res. Int. 42 2009 343 348
    • (2009) Food Res. Int. , vol.42 , pp. 343-348
    • Wu, H.1    Wang, Q.2    Ma, T.3    Ren, J.4
  • 34
    • 33847174684 scopus 로고    scopus 로고
    • Peanut protein concentrate: Production and functional properties as affected by processing
    • J. Yu, M. Ahmedna, and I. Goktepe Peanut protein concentrate: production and functional properties as affected by processing Food Chem. 103 2007 121 129
    • (2007) Food Chem. , vol.103 , pp. 121-129
    • Yu, J.1    Ahmedna, M.2    Goktepe, I.3
  • 35
    • 79953203868 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate
    • G. Zhao, Y. Liu, M. Zhao, J. Ren, and B. Yang Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate Food Chem. 127 2011 1438 1443
    • (2011) Food Chem. , vol.127 , pp. 1438-1443
    • Zhao, G.1    Liu, Y.2    Zhao, M.3    Ren, J.4    Yang, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.