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Volumn 29, Issue , 2016, Pages 380-387

Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel

Author keywords

Cold gel; Gelation property; High intensity ultrasound; Soy protein isolate; Transglutaminase

Indexed keywords

AMINO ACIDS; CATALYSIS; COVALENT BONDS; GELATION; HYDROPHOBICITY; PHYSICOCHEMICAL PROPERTIES; SCANNING ELECTRON MICROSCOPY; SULFUR COMPOUNDS; ULTRASONICS;

EID: 84946924689     PISSN: 13504177     EISSN: 18732828     Source Type: Journal    
DOI: 10.1016/j.ultsonch.2015.10.014     Document Type: Article
Times cited : (137)

References (46)
  • 1
  • 2
    • 44449100194 scopus 로고    scopus 로고
    • Health effects of soy protein and isoflavones in humans
    • C.W. Xiao Health effects of soy protein and isoflavones in humans J. Nutr. 138 2008 1244S 1249S
    • (2008) J. Nutr. , vol.138 , pp. 1244S-1249S
    • Xiao, C.W.1
  • 3
    • 80053947750 scopus 로고    scopus 로고
    • Biodegradable soy protein isolate-based materials: A review
    • F. Song D.L. Tang X.L. Wang Y.Z. Wang Biodegradable soy protein isolate-based materials: a review Biomacromolecules 12 2011 3369 3380
    • (2011) Biomacromolecules , vol.12 , pp. 3369-3380
    • Song, F.1    Tang, D.L.2    Wang, X.L.3    Wang, Y.Z.4
  • 4
    • 84894088317 scopus 로고    scopus 로고
    • Soy proteins: A review on composition, aggregation and emulsification
    • K. Nishinari Y. Fang S. Guo G. Phillips Soy proteins: a review on composition, aggregation and emulsification Food Hydrocolloid 39 2014 301 318
    • (2014) Food Hydrocolloid , vol.39 , pp. 301-318
    • Nishinari, K.1    Fang, Y.2    Guo, S.3    Phillips, G.4
  • 5
    • 67349098526 scopus 로고    scopus 로고
    • Soy protein cold-set hydrogels as controlled delivery devices for nutraceutical compounds
    • A. Maltais G.E. Remondetto M. Subirade Soy protein cold-set hydrogels as controlled delivery devices for nutraceutical compounds Food Hydrocolloid 23 2009 1647 1653
    • (2009) Food Hydrocolloid , vol.23 , pp. 1647-1653
    • Maltais, A.1    Remondetto, G.E.2    Subirade, M.3
  • 6
    • 28844500312 scopus 로고    scopus 로고
    • Effect of soy protein subunit composition on tofu quality
    • V. Poysa L. Woodrow K. Yu Effect of soy protein subunit composition on tofu quality Food Res. Int. 39 2006 309 317
    • (2006) Food Res. Int. , vol.39 , pp. 309-317
    • Poysa, V.1    Woodrow, L.2    Yu, K.3
  • 7
    • 0000403060 scopus 로고
    • Rheological characteristics and gelation mechanism of tofu (soybean curd)
    • K. Kohyama Y. Sano E. Doi Rheological characteristics and gelation mechanism of tofu (soybean curd) J. Agric. Food Chem. 43 1995 1808 1812
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 1808-1812
    • Kohyama, K.1    Sano, Y.2    Doi, E.3
  • 8
    • 51049098678 scopus 로고    scopus 로고
    • Effects of heat treatment and glucono-δ-lactone-induced acidification on characteristics of soy protein isolate
    • L.J. Campbell X. Gu S.J. Dewar S.R. Euston Effects of heat treatment and glucono-δ-lactone-induced acidification on characteristics of soy protein isolate Food Hydrocolloid 23 2009 344 351
    • (2009) Food Hydrocolloid , vol.23 , pp. 344-351
    • Campbell, L.J.1    Gu, X.2    Dewar, S.J.3    Euston, S.R.4
  • 9
    • 0004789031 scopus 로고    scopus 로고
    • The effects of continuous flow microwave treatment and conventional heating on the nutritional value of milk as shown by influence on vitamin B1 retention
    • I. Sierra C. Vidal-Valverde A. Olano The effects of continuous flow microwave treatment and conventional heating on the nutritional value of milk as shown by influence on vitamin B1 retention Eur. Food Res. Technol. 209 1999 352 354
    • (1999) Eur. Food Res. Technol. , vol.209 , pp. 352-354
    • Sierra, I.1    Vidal-Valverde, C.2    Olano, A.3
  • 10
    • 75349112726 scopus 로고    scopus 로고
    • Encapsulation for preservation of functionality and targeted delivery of bioactive food components
    • P. de Vos M.M. Faas M. Spasojevic J. Sikkema Encapsulation for preservation of functionality and targeted delivery of bioactive food components Int. Dairy J. 20 2010 292 302
    • (2010) Int. Dairy J. , vol.20 , pp. 292-302
    • De Vos, P.1    Faas, M.M.2    Spasojevic, M.3    Sikkema, J.4
  • 11
    • 0030222324 scopus 로고    scopus 로고
    • Influence of gelatin matrices cross-linked with transglutaminase on the properties of an enclosed bioactive material using β-galactosidase as model system
    • H.L. Fuchsbauer U. Gerber J. Engelmann T. Seeger C. Sinks T. Hecht Influence of gelatin matrices cross-linked with transglutaminase on the properties of an enclosed bioactive material using β-galactosidase as model system Biomaterials 17 1996 1481 1488
    • (1996) Biomaterials , vol.17 , pp. 1481-1488
    • Fuchsbauer, H.L.1    Gerber, U.2    Engelmann, J.3    Seeger, T.4    Sinks, C.5    Hecht, T.6
  • 12
    • 64849114357 scopus 로고    scopus 로고
    • Properties of biopolymers produced by transglutaminase treatment of whey protein isolate and gelatin
    • E. Hernàndez-Balada M.M. Taylor J.G. Phillips W.N. Marmer E.M. Brown Properties of biopolymers produced by transglutaminase treatment of whey protein isolate and gelatin Bioresource Technol. 100 2009 3638 3643
    • (2009) Bioresource Technol. , vol.100 , pp. 3638-3643
    • Hernàndez-Balada, E.1    Taylor, M.M.2    Phillips, J.G.3    Marmer, W.N.4    Brown, E.M.5
  • 13
    • 84912073492 scopus 로고    scopus 로고
    • Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin
    • H. Hu I.W. Cheung S. Pan E.C. Li-Chan Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin Food Hydrocolloid 45 2015 102 110
    • (2015) Food Hydrocolloid , vol.45 , pp. 102-110
    • Hu, H.1    Cheung, I.W.2    Pan, S.3    Li-Chan, E.C.4
  • 14
    • 26844437327 scopus 로고    scopus 로고
    • Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase
    • C.H. Tang H. Wu Z. Chen X.Q. Yang Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase Food Res. Int. 39 2006 87 97
    • (2006) Food Res. Int. , vol.39 , pp. 87-97
    • Tang, C.H.1    Wu, H.2    Chen, Z.3    Yang, X.Q.4
  • 15
    • 33846360753 scopus 로고    scopus 로고
    • Formation and rheological properties of 'cold-set'tofu induced by microbial transglutaminase
    • C.H. Tang L. Li J.L. Wang X.Q. Yang Formation and rheological properties of 'cold-set'tofu induced by microbial transglutaminase LWT-Food Sci. Technol. 40 2007 579 586
    • (2007) LWT-Food Sci. Technol. , vol.40 , pp. 579-586
    • Tang, C.H.1    Li, L.2    Wang, J.L.3    Yang, X.Q.4
  • 16
    • 84936852918 scopus 로고    scopus 로고
    • Applications of ultrasound in food and bioprocessing
    • M. Ashokkumar Applications of ultrasound in food and bioprocessing Ultrason. Sonochem. 25 2015 17 23
    • (2015) Ultrason. Sonochem. , vol.25 , pp. 17-23
    • Ashokkumar, M.1
  • 19
    • 84922419259 scopus 로고    scopus 로고
    • Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal
    • J. Jin H. Ma K. Wang A.E.G.A. Yagoub J. Owusu W. Qu R. He C. Zhou X. Ye Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal Ultrason. Sonochem. 24 2015 55 64
    • (2015) Ultrason. Sonochem. , vol.24 , pp. 55-64
    • Jin, J.1    Ma, H.2    Wang, K.3    Yagoub, A.E.G.A.4    Owusu, J.5    Qu, W.6    He, R.7    Zhou, C.8    Ye, X.9
  • 20
    • 28444436246 scopus 로고    scopus 로고
    • Innovative applications of power ultrasound during food freezing processes -A review
    • L. Zheng D.W. Sun Innovative applications of power ultrasound during food freezing processes-a review Trends Food Sci. Technol. 17 2006 16 23
    • (2006) Trends Food Sci. Technol. , vol.17 , pp. 16-23
    • Zheng, L.1    Sun, D.W.2
  • 21
    • 80054951068 scopus 로고    scopus 로고
    • Comparative study of high intensity ultrasound effects on food proteins functionality
    • C. Arzeni K. Martinez P. Zema A. Arias O. Perez A. Pilosof Comparative study of high intensity ultrasound effects on food proteins functionality J. Food Eng. 108 2012 463 472
    • (2012) J. Food Eng. , vol.108 , pp. 463-472
    • Arzeni, C.1    Martinez, K.2    Zema, P.3    Arias, A.4    Perez, O.5    Pilosof, A.6
  • 23
    • 84897690229 scopus 로고    scopus 로고
    • Applications of power ultrasound in food processing
    • S. Kentish H. Feng Applications of power ultrasound in food processing Annu. Rev. Food Sci. Technol. 5 2014 263 284
    • (2014) Annu. Rev. Food Sci. Technol. , vol.5 , pp. 263-284
    • Kentish, S.1    Feng, H.2
  • 24
    • 84939942662 scopus 로고    scopus 로고
    • Modification of foaming properties of soy protein isolate by high ultrasound intensity: Particle size effect
    • R. Morales K.D. Martínez V.M.P. Ruiz-Henestrosa A.M. Pilosof Modification of foaming properties of soy protein isolate by high ultrasound intensity: particle size effect Ultrason. Sonochem. 26 2015 48 55
    • (2015) Ultrason. Sonochem. , vol.26 , pp. 48-55
    • Morales, R.1    Martínez, K.D.2    Ruiz-Henestrosa, V.M.P.3    Pilosof, A.M.4
  • 26
    • 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
    • H. Hu E.C. Li-Chan L. Wan M. Tian S. Pan The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate Food Hydrocolloid 32 2013 303 311
    • (2013) Food Hydrocolloid , vol.32 , pp. 303-311
    • Hu, H.1    Li-Chan, E.C.2    Wan, L.3    Tian, M.4    Pan, S.5
  • 27
    • 84867744049 scopus 로고    scopus 로고
    • Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments
    • H. Hu X. Fan Z. Zhou X. Xu G. Fan L. Wang X. Huang S. Pan L. Zhu Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments Ultrason. Sonochem. 20 2013 187 195
    • (2013) Ultrason. Sonochem. , vol.20 , pp. 187-195
    • Hu, H.1    Fan, X.2    Zhou, Z.3    Xu, X.4    Fan, G.5    Wang, L.6    Huang, X.7    Pan, S.8    Zhu, L.9
  • 28
    • 66349130160 scopus 로고    scopus 로고
    • Effect of ultrasound on gelation property of commercial soy protein isolate
    • In Chinese
    • C.H. Tang Y. Jiang X.Q. Yang Z. Chen Effect of ultrasound on gelation property of commercial soy protein isolate J. Chin. Cereals Oils Assoc. 20 2006 72 77 In Chinese
    • (2006) J. Chin. Cereals Oils Assoc. , vol.20 , pp. 72-77
    • Tang, C.H.1    Jiang, Y.2    Yang, X.Q.3    Chen, Z.4
  • 29
    • 0342963509 scopus 로고
    • Determination of sulfhydryl groups and disulfide bonds in heat-induced gels of soy protein isolate
    • K. Shimada J.C. Cheftel Determination of sulfhydryl groups and disulfide bonds in heat-induced gels of soy protein isolate J. Agric. Food Chem. 36 1988 147 153
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 147-153
    • Shimada, K.1    Cheftel, J.C.2
  • 30
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate
    • K. Shimada J.C. Cheftel Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate J. Agric. Food Chem. 37 1989 161 168
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 31
    • 84887730864 scopus 로고    scopus 로고
    • Determination of α-tocopherol in vegetable oils using a molecularly imprinted polymers-surface-enhanced Raman spectroscopic biosensor
    • S. Feng F. Gao Z. Chen E. Grant D.D. Kitts S. Wang X. Lu Determination of α-tocopherol in vegetable oils using a molecularly imprinted polymers-surface-enhanced Raman spectroscopic biosensor J. Agric. Food Chem. 61 2013 10467 10475
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 10467-10475
    • Feng, S.1    Gao, F.2    Chen, Z.3    Grant, E.4    Kitts, D.D.5    Wang, S.6    Lu, X.7
  • 32
    • 79955018532 scopus 로고    scopus 로고
    • 2, glucono-δ-lactone (GDL), and transglutaminase: Influence of thermal treatments before and/or after emulsification
    • 2, glucono-δ-lactone (GDL), and transglutaminase: influence of thermal treatments before and/or after emulsification J. Agric. Food Chem. 59 2011 4071 4077
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 4071-4077
    • Tang, C.H.1    Chen, L.2    Foegeding, E.A.3
  • 33
    • 34248329577 scopus 로고    scopus 로고
    • Effect of thermal pretreatment of raw soymilk on the gel strength and microstructure of tofu induced by microbial transglutaminase
    • C.H. Tang Effect of thermal pretreatment of raw soymilk on the gel strength and microstructure of tofu induced by microbial transglutaminase LWT-Food Sci. Technol. 40 2007 1403 1409
    • (2007) LWT-Food Sci. Technol. , vol.40 , pp. 1403-1409
    • Tang, C.H.1
  • 34
    • 0038605875 scopus 로고    scopus 로고
    • Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures
    • J. Ramlrez-Suárez Y.L. Xiong Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures Meat Sci. 65 2003 899 907
    • (2003) Meat Sci. , vol.65 , pp. 899-907
    • Ramlrez-Suárez, J.1    Xiong, Y.L.2
  • 35
    • 84946397721 scopus 로고    scopus 로고
    • Effect of ultrasound pre-treatment on formation of transglutaminase-catalyzed soy protein hydrogel as a riboflavin vehicle for functional foods
    • H. Hu X. Zhu T. Hu I. Cheung S. Pan E. Li-Chan Effect of ultrasound pre-treatment on formation of transglutaminase-catalyzed soy protein hydrogel as a riboflavin vehicle for functional foods J. Funct. Foods 19 2015 182 193
    • (2015) J. Funct. Foods , vol.19 , pp. 182-193
    • Hu, H.1    Zhu, X.2    Hu, T.3    Cheung, I.4    Pan, S.5    Li-Chan, E.6
  • 36
    • 59649119443 scopus 로고    scopus 로고
    • The effect of thermosonication of milk on selected physicochemical and microstructural properties of yoghurt gels during fermentation
    • J. Riener F. Noci D.A. Cronin D.J. Morgan J.G. Lyng The effect of thermosonication of milk on selected physicochemical and microstructural properties of yoghurt gels during fermentation Food Chem. 114 2009 905 911
    • (2009) Food Chem. , vol.114 , pp. 905-911
    • Riener, J.1    Noci, F.2    Cronin, D.A.3    Morgan, D.J.4    Lyng, J.G.5
  • 37
    • 69249218963 scopus 로고    scopus 로고
    • Physicochemical changes in whey protein concentrate texturized by reactive supercritical fluid extrusion
    • K. Manoi S.S. Rizvi Physicochemical changes in whey protein concentrate texturized by reactive supercritical fluid extrusion J. Food Eng. 95 2009 627 635
    • (2009) J. Food Eng. , vol.95 , pp. 627-635
    • Manoi, K.1    Rizvi, S.S.2
  • 38
    • 38849203059 scopus 로고    scopus 로고
    • Mechanisms involved in the formation and structure of soya protein cold-set gels: A molecular and supramolecular investigation
    • A. Maltais G.E. Remondetto M. Subirade Mechanisms involved in the formation and structure of soya protein cold-set gels: a molecular and supramolecular investigation Food Hydrocolloid 22 2008 550 559
    • (2008) Food Hydrocolloid , vol.22 , pp. 550-559
    • Maltais, A.1    Remondetto, G.E.2    Subirade, M.3
  • 39
    • 0030829061 scopus 로고    scopus 로고
    • In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy
    • M. Bouraoui S. Nakai E. Li-Chan In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy Food Res. Int. 30 1997 65 72
    • (1997) Food Res. Int. , vol.30 , pp. 65-72
    • Bouraoui, M.1    Nakai, S.2    Li-Chan, E.3
  • 40
    • 79957607056 scopus 로고    scopus 로고
    • Raman spectroscopic study of the effects of microbial transglutaminase on heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristics
    • H. Chen M. Han Raman spectroscopic study of the effects of microbial transglutaminase on heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristics Food Res. Int. 44 2011 1514 1520
    • (2011) Food Res. Int. , vol.44 , pp. 1514-1520
    • Chen, H.1    Han, M.2
  • 41
    • 1542299045 scopus 로고    scopus 로고
    • Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels
    • S. Ikeda E.C. Li-Chan Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels Food Hydrocolloid 18 2004 489 498
    • (2004) Food Hydrocolloid , vol.18 , pp. 489-498
    • Ikeda, S.1    Li-Chan, E.C.2
  • 43
    • 80054686062 scopus 로고    scopus 로고
    • Evaluation of structural changes in raw and heated meat batters prepared with different lipids using Raman spectroscopy
    • J.H. Shao Y.F. Zou X.L. Xu J.Q. Wu G.H. Zhou Evaluation of structural changes in raw and heated meat batters prepared with different lipids using Raman spectroscopy Food Res. Int. 44 2011 2955 2961
    • (2011) Food Res. Int. , vol.44 , pp. 2955-2961
    • Shao, J.H.1    Zou, Y.F.2    Xu, X.L.3    Wu, J.Q.4    Zhou, G.H.5
  • 44
    • 41849101479 scopus 로고    scopus 로고
    • Vibrational spectroscopy applied to the study of milk proteins
    • E.C. Li-Chan Vibrational spectroscopy applied to the study of milk proteins Le Lait 87 2007 443 458
    • (2007) Le Lait , vol.87 , pp. 443-458
    • Li-Chan, E.C.1
  • 45
    • 79952536911 scopus 로고    scopus 로고
    • Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties
    • R. Liu S.M. Zhao B.J. Xie S.B. Xiong Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties Food Hydrocolloid 25 2011 898 906
    • (2011) Food Hydrocolloid , vol.25 , pp. 898-906
    • Liu, R.1    Zhao, S.M.2    Xie, B.J.3    Xiong, S.B.4
  • 46
    • 36448962326 scopus 로고    scopus 로고
    • Raman spectroscopy a promising technique for quality assessment of meat and fish: A review
    • A.M. Herrero Raman spectroscopy a promising technique for quality assessment of meat and fish: a review Food Chem. 107 2008 1642 1651
    • (2008) Food Chem. , vol.107 , pp. 1642-1651
    • Herrero, A.M.1


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