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Volumn 7, Issue 9, 2019, Pages 8117-8125

Conformational Changes of Soy Proteins under High-Intensity Ultrasound and High-Speed Shearing Treatments

Author keywords

Aqueous solution; Denaturation; Mechanical shearing; Neutral pH; Soy protein isolate; Ultrasound

Indexed keywords

DENATURATION; PARTICLE SIZE; PARTICLE SIZE ANALYSIS; SHEARING; SOLUTIONS; ULTRASONICS;

EID: 85065437700     PISSN: None     EISSN: 21680485     Source Type: Journal    
DOI: 10.1021/acssuschemeng.8b05713     Document Type: Article
Times cited : (30)

References (40)
  • 1
    • 34547663072 scopus 로고    scopus 로고
    • Feature: Environmental Trade-offs of Biobased Production
    • Miller, S. A.; Landis, A. E.; Theis, T. L. Feature: Environmental Trade-offs of Biobased Production. Environ. Sci. Technol. 2007, 41 (15), 5176-5182, 10.1021/es072581z
    • (2007) Environ. Sci. Technol. , vol.41 , Issue.15 , pp. 5176-5182
    • Miller, S.A.1    Landis, A.E.2    Theis, T.L.3
  • 3
    • 84879349447 scopus 로고    scopus 로고
    • Sustainable Polymers: Opportunities for the Next Decade
    • Miller, S. A. Sustainable Polymers: Opportunities for the Next Decade. ACS Macro Lett. 2013, 2 (6), 550-554, 10.1021/mz400207g
    • (2013) ACS Macro Lett. , vol.2 , Issue.6 , pp. 550-554
    • Miller, S.A.1
  • 4
    • 84889675797 scopus 로고    scopus 로고
    • Environmental Life Cycle Analysis of Distributed Three-Dimensional Printing and Conventional Manufacturing of Polymer Products
    • Kreiger, M.; Pearce, J. M. Environmental Life Cycle Analysis of Distributed Three-Dimensional Printing and Conventional Manufacturing of Polymer Products. ACS Sustainable Chem. Eng. 2013, 1 (12), 1511-1519, 10.1021/sc400093k
    • (2013) ACS Sustainable Chem. Eng. , vol.1 , Issue.12 , pp. 1511-1519
    • Kreiger, M.1    Pearce, J.M.2
  • 6
    • 0033907513 scopus 로고    scopus 로고
    • 'Green' polymers
    • Scott, G. 'Green' polymers. Polym. Degrad. Stab. 2000, 68 (1), 1-7, 10.1016/S0141-3910(99)00182-2
    • (2000) Polym. Degrad. Stab. , vol.68 , Issue.1 , pp. 1-7
    • Scott, G.1
  • 7
    • 84897516128 scopus 로고    scopus 로고
    • Protein Nanoparticles as Drug Delivery Carriers for Cancer Therapy
    • Lohcharoenkal, W.; Wang, L. Y.; Chen, Y. C.; Rojanasakul, Y. Protein Nanoparticles as Drug Delivery Carriers for Cancer Therapy. BioMed Res. Int. 2014, 2014, 1, 10.1155/2014/180549
    • (2014) BioMed Res. Int. , vol.2014 , pp. 1
    • Lohcharoenkal, W.1    Wang, L.Y.2    Chen, Y.C.3    Rojanasakul, Y.4
  • 8
    • 85032644538 scopus 로고    scopus 로고
    • Optical Spectroscopic and Morphological Characterizations of Curcuminized Silk Biomaterials: A Perspective from Drug Stabilization
    • Panja, S.; Behera, S.; Kundu, S. C.; Halder, M. Optical Spectroscopic and Morphological Characterizations of Curcuminized Silk Biomaterials: A Perspective from Drug Stabilization. Acs Omega 2017, 2 (10), 6755-6767, 10.1021/acsomega.7b00809
    • (2017) Acs Omega , vol.2 , Issue.10 , pp. 6755-6767
    • Panja, S.1    Behera, S.2    Kundu, S.C.3    Halder, M.4
  • 9
    • 84988857120 scopus 로고    scopus 로고
    • Hydrogel films and microcapsules based on soy protein isolate combined with alginate
    • Tansaz, S.; Durmann, A. K.; Detsch, R.; Boccaccini, A. R. Hydrogel films and microcapsules based on soy protein isolate combined with alginate. J. Appl. Polym. Sci. 2017, 134 (4), 44358, 10.1002/app.44358
    • (2017) J. Appl. Polym. Sci. , vol.134 , Issue.4 , pp. 44358
    • Tansaz, S.1    Durmann, A.K.2    Detsch, R.3    Boccaccini, A.R.4
  • 10
    • 84988419342 scopus 로고    scopus 로고
    • Simulation of novel soy protein-based systems for tissue regeneration applications
    • Knani, D.; Barkay-Olami, H.; Alperstein, D.; Zilberman, M. Simulation of novel soy protein-based systems for tissue regeneration applications. Polym. Adv. Technol. 2017, 28 (4), 496-505, 10.1002/pat.3918
    • (2017) Polym. Adv. Technol. , vol.28 , Issue.4 , pp. 496-505
    • Knani, D.1    Barkay-Olami, H.2    Alperstein, D.3    Zilberman, M.4
  • 11
    • 84923108448 scopus 로고    scopus 로고
    • A sustainable slashing industry using biodegradable sizes from modified soy protein to replace petro-based poly(vinyl alcohol)
    • Zhao, Y.; Zhao, Y.; Xu, H.; Yang, Y. A sustainable slashing industry using biodegradable sizes from modified soy protein to replace petro-based poly(vinyl alcohol). Environ. Sci. Technol. 2015, 49 (4), 2391-7, 10.1021/es504988w
    • (2015) Environ. Sci. Technol. , vol.49 , Issue.4 , pp. 2391-2397
    • Zhao, Y.1    Zhao, Y.2    Xu, H.3    Yang, Y.4
  • 12
    • 84955215966 scopus 로고    scopus 로고
    • Biomedical applications of soy protein: A brief overview
    • Tansaz, S.; Boccaccini, A. R. Biomedical applications of soy protein: A brief overview. J. Biomed. Mater. Res., Part A 2016, 104 (2), 553-69, 10.1002/jbm.a.35569
    • (2016) J. Biomed. Mater. Res., Part A , vol.104 , Issue.2 , pp. 553-569
    • Tansaz, S.1    Boccaccini, A.R.2
  • 13
    • 80053947750 scopus 로고    scopus 로고
    • Biodegradable soy protein isolate-based materials: A review
    • Song, F.; Tang, D. L.; Wang, X. L.; Wang, Y. Z. Biodegradable soy protein isolate-based materials: a review. Biomacromolecules 2011, 12 (10), 3369-80, 10.1021/bm200904x
    • (2011) Biomacromolecules , vol.12 , Issue.10 , pp. 3369-3380
    • Song, F.1    Tang, D.L.2    Wang, X.L.3    Wang, Y.Z.4
  • 16
    • 84957727731 scopus 로고    scopus 로고
    • Treatments of protein for biopolymer production in view of processability and physical properties: A review
    • Du, Y. C.; Li, S. Z.; Zhang, Y. C.; Rempel, C.; Liu, Q. Treatments of protein for biopolymer production in view of processability and physical properties: A review. J. Appl. Polym. Sci. 2016, 133 (17), 43351, 10.1002/app.43351
    • (2016) J. Appl. Polym. Sci. , vol.133 , Issue.17 , pp. 43351
    • Du, Y.C.1    Li, S.Z.2    Zhang, Y.C.3    Rempel, C.4    Liu, Q.5
  • 17
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. A straightforward fractionation and their characterization
    • Vu Huu, T.; Shibasaki, K. Major proteins of soybean seeds. A straightforward fractionation and their characterization. J. Agric. Food Chem. 1976, 24 (6), 1117-1121, 10.1021/jf60208a030
    • (1976) J. Agric. Food Chem. , vol.24 , Issue.6 , pp. 1117-1121
    • Vu Huu, T.1    Shibasaki, K.2
  • 18
    • 79951744042 scopus 로고    scopus 로고
    • Physicochemical properties of beta and alpha'alpha subunits isolated from soybean beta-conglycinin
    • Mo, X.; Wang, D.; Sun, X. S. Physicochemical properties of beta and alpha'alpha subunits isolated from soybean beta-conglycinin. J. Agric. Food Chem. 2011, 59 (4), 1217-1222, 10.1021/jf102903b
    • (2011) J. Agric. Food Chem. , vol.59 , Issue.4 , pp. 1217-1222
    • Mo, X.1    Wang, D.2    Sun, X.S.3
  • 19
    • 84985400015 scopus 로고
    • Molecular Weight and Amino Acid Composition of Glycinin Subunits
    • Catsimpoolas, N.; Kenney, J. A.; Meyer, E. W.; Szuhaj, B. F. Molecular Weight and Amino Acid Composition of Glycinin Subunits. J. Sci. Food Agric. 1971, 22 (9), 448, 10.1002/jsfa.2740220905
    • (1971) J. Sci. Food Agric. , vol.22 , Issue.9 , pp. 448
    • Catsimpoolas, N.1    Kenney, J.A.2    Meyer, E.W.3    Szuhaj, B.F.4
  • 20
    • 0033790812 scopus 로고    scopus 로고
    • Solubility, tensile, and color properties of modified soy protein isolate films
    • Rhim, J. W.; Gennadios, A.; Handa, A.; Weller, C. L.; Hanna, M. A. Solubility, tensile, and color properties of modified soy protein isolate films. J. Agric. Food Chem. 2000, 48 (10), 4937-41, 10.1021/jf0005418
    • (2000) J. Agric. Food Chem. , vol.48 , Issue.10 , pp. 4937-4941
    • Rhim, J.W.1    Gennadios, A.2    Handa, A.3    Weller, C.L.4    Hanna, M.A.5
  • 21
    • 34047248365 scopus 로고    scopus 로고
    • Preparation and physical properties of soy protein isolate and gelatin composite films
    • Cao, N.; Fu, Y. H.; He, J. H. Preparation and physical properties of soy protein isolate and gelatin composite films. Food Hydrocolloids 2007, 21 (7), 1153-1162, 10.1016/j.foodhyd.2006.09.001
    • (2007) Food Hydrocolloids , vol.21 , Issue.7 , pp. 1153-1162
    • Cao, N.1    Fu, Y.H.2    He, J.H.3
  • 22
    • 51349117138 scopus 로고    scopus 로고
    • Effects of drying conditions on some physical properties of soy protein films
    • Denavi, G.; Tapia-Blacido, D. R.; Anon, M. C.; Sobral, P. J. A.; Mauri, A. N.; Menegalli, F. C. Effects of drying conditions on some physical properties of soy protein films. J. Food Eng. 2009, 90 (3), 341-349, 10.1016/j.jfoodeng.2008.07.001
    • (2009) J. Food Eng. , vol.90 , Issue.3 , pp. 341-349
    • Denavi, G.1    Tapia-Blacido, D.R.2    Anon, M.C.3    Sobral, P.J.A.4    Mauri, A.N.5    Menegalli, F.C.6
  • 24
    • 84876591406 scopus 로고    scopus 로고
    • Mechanical and water barrier properties of soy protein isolate film incorporated with gelatin
    • Bai, H. Y.; Xu, J.; Liao, P.; Liu, X. Y. Mechanical and water barrier properties of soy protein isolate film incorporated with gelatin. J. Plast. Film Sheeting 2013, 29 (2), 174-188, 10.1177/8756087912468744
    • (2013) J. Plast. Film Sheeting , vol.29 , Issue.2 , pp. 174-188
    • Bai, H.Y.1    Xu, J.2    Liao, P.3    Liu, X.Y.4
  • 25
    • 79953058808 scopus 로고    scopus 로고
    • Functional properties of films based on soy protein isolate and gelatin processed by compression molding
    • Guerrero, P.; Stefani, P. M.; Ruseckaite, R. A.; de la Caba, K. Functional properties of films based on soy protein isolate and gelatin processed by compression molding. J. Food Eng. 2011, 105 (1), 65-72, 10.1016/j.jfoodeng.2011.02.003
    • (2011) J. Food Eng. , vol.105 , Issue.1 , pp. 65-72
    • Guerrero, P.1    Stefani, P.M.2    Ruseckaite, R.A.3    De La Caba, K.4
  • 27
    • 84921021461 scopus 로고    scopus 로고
    • Characterization of Conformational Structures of Plant Proteins in Solutions
    • Aghanouri, A.; Shoemaker, C. F.; Sun, G. Characterization of Conformational Structures of Plant Proteins in Solutions. Ind. Eng. Chem. Res. 2015, 54 (1), 188-197, 10.1021/ie5032502
    • (2015) Ind. Eng. Chem. Res. , vol.54 , Issue.1 , pp. 188-197
    • Aghanouri, A.1    Shoemaker, C.F.2    Sun, G.3
  • 28
    • 84964321121 scopus 로고    scopus 로고
    • Prediction of Solubility Behavior of Globular Plant Proteins with Hansen Solubility Parameters: A Conformational Study
    • Aghanouri, A.; Sun, G. Prediction of Solubility Behavior of Globular Plant Proteins with Hansen Solubility Parameters: A Conformational Study. ACS Sustainable Chem. Eng. 2016, 4 (4), 2337-2344, 10.1021/acssuschemeng.6b00022
    • (2016) ACS Sustainable Chem. Eng. , vol.4 , Issue.4 , pp. 2337-2344
    • Aghanouri, A.1    Sun, G.2
  • 29
    • 84916624283 scopus 로고    scopus 로고
    • Hansen solubility parameters as a useful tool in searching for solvents for soy proteins
    • Aghanouri, A.; Sun, G. Hansen solubility parameters as a useful tool in searching for solvents for soy proteins. RSC Adv. 2015, 5 (3), 1890-1892, 10.1039/C4RA09115A
    • (2015) RSC Adv. , vol.5 , Issue.3 , pp. 1890-1892
    • Aghanouri, A.1    Sun, G.2
  • 30
    • 84894088317 scopus 로고    scopus 로고
    • Soy proteins: A review on composition, aggregation and emulsification
    • Nishinari, K.; Fang, Y.; Guo, S.; Phillips, G. O. Soy proteins: A review on composition, aggregation and emulsification. Food Hydrocolloids 2014, 39, 301-318, 10.1016/j.foodhyd.2014.01.013
    • (2014) Food Hydrocolloids , vol.39 , pp. 301-318
    • Nishinari, K.1    Fang, Y.2    Guo, S.3    Phillips, G.O.4
  • 32
    • 85046140463 scopus 로고    scopus 로고
    • Effect of high intensity ultrasound on structure and foaming properties of pea protein isolate
    • Xiong, T.; Xiong, W.; Ge, M.; Xia, J.; Li, B.; Chen, Y. Effect of high intensity ultrasound on structure and foaming properties of pea protein isolate. Food Res. Int. 2018, 109, 260-267, 10.1016/j.foodres.2018.04.044
    • (2018) Food Res. Int. , vol.109 , pp. 260-267
    • Xiong, T.1    Xiong, W.2    Ge, M.3    Xia, J.4    Li, B.5    Chen, Y.6
  • 33
    • 85017342599 scopus 로고    scopus 로고
    • Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments
    • Jiang, S.; Ding, J.; Andrade, J.; Rababah, T. M.; Almajwal, A.; Abulmeaty, M. M.; Feng, H. Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrason. Sonochem. 2017, 38, 835-842, 10.1016/j.ultsonch.2017.03.046
    • (2017) Ultrason. Sonochem. , vol.38 , pp. 835-842
    • Jiang, S.1    Ding, J.2    Andrade, J.3    Rababah, T.M.4    Almajwal, A.5    Abulmeaty, M.M.6    Feng, H.7
  • 34
    • 84866265898 scopus 로고    scopus 로고
    • Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions
    • Hu, H.; Wu, J. H.; Li-Chan, E. C. Y.; Zhu, L.; Zhang, F.; Xu, X. Y.; Fan, G.; Wang, L. F.; Huang, X. J.; Pan, S. Y. Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids 2013, 30 (2), 647-655, 10.1016/j.foodhyd.2012.08.001
    • (2013) Food Hydrocolloids , vol.30 , Issue.2 , pp. 647-655
    • Hu, H.1    Wu, J.H.2    Li-Chan, E.C.Y.3    Zhu, L.4    Zhang, F.5    Xu, X.Y.6    Fan, G.7    Wang, L.F.8    Huang, X.J.9    Pan, S.Y.10
  • 35
    • 84883480405 scopus 로고    scopus 로고
    • Effect of ultrasound treatment on particle size and molecular weight of whey proteins
    • Jambrak, A. R.; Mason, T. J.; Lelas, V.; Paniwnyk, L.; Herceg, Z. Effect of ultrasound treatment on particle size and molecular weight of whey proteins. J. Food Eng. 2014, 121, 15-23, 10.1016/j.jfoodeng.2013.08.012
    • (2014) J. Food Eng. , vol.121 , pp. 15-23
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Paniwnyk, L.4    Herceg, Z.5
  • 36
    • 84865415843 scopus 로고    scopus 로고
    • Effect of high-pressure homogenization on particle size and film properties of soy protein isolate
    • Song, X. Z.; Zhou, C. J.; Fu, F.; Chen, Z. L.; Wu, Q. L. Effect of high-pressure homogenization on particle size and film properties of soy protein isolate. Ind. Crops Prod. 2013, 43, 538-544, 10.1016/j.indcrop.2012.08.005
    • (2013) Ind. Crops Prod. , vol.43 , pp. 538-544
    • Song, X.Z.1    Zhou, C.J.2    Fu, F.3    Chen, Z.L.4    Wu, Q.L.5
  • 37
    • 84912073492 scopus 로고    scopus 로고
    • Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin
    • Hu, H.; Cheung, I. W. Y.; Pan, S.; Li-Chan, E. C. Y. Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin. Food Hydrocolloids 2015, 45, 102-110, 10.1016/j.foodhyd.2014.11.004
    • (2015) Food Hydrocolloids , vol.45 , pp. 102-110
    • Hu, H.1    Cheung, I.W.Y.2    Pan, S.3    Li-Chan, E.C.Y.4
  • 38
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N.; Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 287 (2), 252-60, 10.1006/abio.2000.4880
    • (2000) Anal. Biochem. , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 39
    • 84923807325 scopus 로고    scopus 로고
    • Relationship between Surface Hydrophobicity and Structure of Soy Protein Isolate Subjected to Different Ionic Strength
    • Jiang, L. Z.; Wang, Z. J.; Li, Y.; Meng, X. H.; Sui, X. N.; Qi, B. K.; Zhou, L. Y. Relationship Between Surface Hydrophobicity and Structure of Soy Protein Isolate Subjected to Different Ionic Strength. Int. J. Food Prop. 2015, 18 (5), 1059-1074, 10.1080/10942912.2013.865057
    • (2015) Int. J. Food Prop. , vol.18 , Issue.5 , pp. 1059-1074
    • Jiang, L.Z.1    Wang, Z.J.2    Li, Y.3    Meng, X.H.4    Sui, X.N.5    Qi, B.K.6    Zhou, L.Y.7


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