메뉴 건너뛰기




Volumn 126, Issue , 2014, Pages 142-148

Dissolution of milk protein concentrate (MPC) powders by ultrasonication

Author keywords

Dissolution; Milk protein concentrate; Particle size; Ultrasonication

Indexed keywords

CONVENTIONAL METHODS; DISSOLUTION MODEL; HIGH INTENSITY ULTRASOUNDS; MILK PROTEIN; PROTEIN DENATURATION; REHYDRATION PROCESS; THERMAL DISSIPATION; ULTRA-SONICATION;

EID: 84890388973     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2013.11.002     Document Type: Article
Times cited : (62)

References (33)
  • 1
    • 25844444764 scopus 로고    scopus 로고
    • Effects of storage temperature on the solubility of milk protein concentrate (MPC85)
    • DOI 10.1016/j.foodhyd.2005.03.015, PII S0268005X05001165
    • S.G. Anema, D.N. Pinder, R.J. Hunter, and Y. Hemar Effects of storage temperature on the solubility of milk protein concentrate (MPC85) Food Hydrocolloids 20 2-3 2006 386 393 (Pubitemid 41390503)
    • (2006) Food Hydrocolloids , vol.20 , Issue.2-3 SPEC. ISS. , pp. 386-393
    • Anema, S.G.1    Pinder, D.N.2    Hunter, R.J.3    Hemar, Y.4
  • 3
    • 84860578583 scopus 로고    scopus 로고
    • Functionality of egg white proteins as affected by high intensity ultrasound
    • C. Arzeni, O.E. Pérez, and A.M.R. Pilosof Functionality of egg white proteins as affected by high intensity ultrasound Food Hydrocolloids 29 2 2012 308 316
    • (2012) Food Hydrocolloids , vol.29 , Issue.2 , pp. 308-316
    • Arzeni, C.1    Pérez, O.E.2    Pilosof, A.M.R.3
  • 6
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study
    • DOI 10.1016/S0963-9969(00)00112-5, PII S0963996900001125
    • J.I. Boye, and I. Alli Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study Food Research International 33 8 2000 673 682 (Pubitemid 30613402)
    • (2000) Food Research International , vol.33 , Issue.8 , pp. 673-682
    • Boye, J.I.1    Alli, I.2
  • 7
    • 79956344900 scopus 로고    scopus 로고
    • Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate
    • J. Chandrapala, B. Zisu, M. Palmer, S. Kentish, and M. Ashokkumar Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate Ultrasonics Sonochemistry 18 5 2011 951 957
    • (2011) Ultrasonics Sonochemistry , vol.18 , Issue.5 , pp. 951-957
    • Chandrapala, J.1    Zisu, B.2    Palmer, M.3    Kentish, S.4    Ashokkumar, M.5
  • 9
    • 77952543997 scopus 로고    scopus 로고
    • Simultaneous pasteurization and homogenization of human milk by combining heat and ultrasound: Effect on milk quality
    • C. Czank, K. Simmer, and P.E. Hartmann Simultaneous pasteurization and homogenization of human milk by combining heat and ultrasound: effect on milk quality Journal of Dairy Research 77 2 2010 183 189
    • (2010) Journal of Dairy Research , vol.77 , Issue.2 , pp. 183-189
    • Czank, C.1    Simmer, K.2    Hartmann, P.E.3
  • 10
    • 77957823932 scopus 로고    scopus 로고
    • On quantifying the dissolution behaviour of milk protein concentrate
    • Y. Fang, C. Selomulya, S. Ainsworth, M. Palmer, and X.D. Chen On quantifying the dissolution behaviour of milk protein concentrate Food Hydrocolloids 25 3 2011 503 510
    • (2011) Food Hydrocolloids , vol.25 , Issue.3 , pp. 503-510
    • Fang, Y.1    Selomulya, C.2    Ainsworth, S.3    Palmer, M.4    Chen, X.D.5
  • 11
    • 78649899399 scopus 로고    scopus 로고
    • Wetting, disintegration and dissolution of agglomerated water soluble powders
    • L. Forny, A. Marabi, and S. Palzer Wetting, disintegration and dissolution of agglomerated water soluble powders Powder Technology 206 1-2 2011 72 78
    • (2011) Powder Technology , vol.206 , Issue.12 , pp. 72-78
    • Forny, L.1    Marabi, A.2    Palzer, S.3
  • 12
    • 34247862268 scopus 로고    scopus 로고
    • Dairy powder rehydration: Influence of protein state, incorporation mode, and agglomeration
    • C. Gaiani, P. Schuck, J. Scher, S. Desobry, and S. Banon Dairy powder rehydration: influence of protein state, incorporation mode, and agglomeration Journal of Dairy Science 90 2 2007 570 581 (Pubitemid 350049705)
    • (2007) Journal of Dairy Science , vol.90 , Issue.2 , pp. 570-581
    • Gaiani, C.1    Schuck, P.2    Scher, J.3    Desobry, S.4    Banon, S.5
  • 13
    • 60249100157 scopus 로고    scopus 로고
    • Use of a turbidity sensor to determine dairy powder rehydration properties
    • C. Gaiani, J. Scher, P. Schuck, S. Desobry, and S. Banon Use of a turbidity sensor to determine dairy powder rehydration properties Powder Technology 190 1-2 2009 2 5
    • (2009) Powder Technology , vol.190 , Issue.12 , pp. 2-5
    • Gaiani, C.1    Scher, J.2    Schuck, P.3    Desobry, S.4    Banon, S.5
  • 15
    • 33749386447 scopus 로고    scopus 로고
    • Structural and functional changes in ultrasonicated bovine serum albumin solutions
    • DOI 10.1016/j.ultsonch.2005.07.006, PII S1350417706000678
    • İ. Gülseren, D. Güzey, B.D. Bruce, and J. Weiss Structural and functional changes in ultrasonicated bovine serum albumin solutions Ultrasonics Sonochemistry 14 2 2007 173 183 (Pubitemid 44500713)
    • (2007) Ultrasonics Sonochemistry , vol.14 , Issue.2 , pp. 173-183
    • Gulseren, I.1    Guzey, D.2    Bruce, B.D.3    Weiss, J.4
  • 16
    • 30744444212 scopus 로고    scopus 로고
    • Protein interactions in milk protein concentrate powders
    • DOI 10.1016/j.idairyj.2005.06.005, PII S0958694605001342
    • P. Havea Protein interactions in milk protein concentrate powders International Dairy Journal 16 5 2006 415 422 (Pubitemid 43098715)
    • (2006) International Dairy Journal , vol.16 , Issue.5 , pp. 415-422
    • Havea, P.1
  • 17
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • DOI 10.1016/S0958-6946(98)00040-5, PII S0958694698000405
    • D.S. Horne Casein Interactions: casting light on the black boxes, the structure in dairy products International Dairy Journal 8 3 1998 171 177 (Pubitemid 28436832)
    • (1998) International Dairy Journal , vol.8 , Issue.3 , pp. 171-177
    • Horne, D.S.1
  • 18
    • 77952683779 scopus 로고    scopus 로고
    • The influence of stirring speed, temperature and solid concentration on the rehydration time of micellar casein powder
    • R. Jeantet, P. Schuck, T. Six, C. Andre, and G. Delaplace The influence of stirring speed, temperature and solid concentration on the rehydration time of micellar casein powder Dairy Science and Technology 90 2-3 2010 225 236
    • (2010) Dairy Science and Technology , vol.90 , Issue.23 , pp. 225-236
    • Jeantet, R.1    Schuck, P.2    Six, T.3    Andre, C.4    Delaplace, G.5
  • 19
    • 84872597169 scopus 로고    scopus 로고
    • Ultrasonic energy input influence οn the production of sub-micron o/w emulsions containing whey protein and common stabilizers
    • O. Kaltsa, C. Michon, S. Yanniotis, and I. Mandala Ultrasonic energy input influence οn the production of sub-micron o/w emulsions containing whey protein and common stabilizers Ultrasonics Sonochemistry 20 3 2013 881 891
    • (2013) Ultrasonics Sonochemistry , vol.20 , Issue.3 , pp. 881-891
    • Kaltsa, O.1    Michon, C.2    Yanniotis, S.3    Mandala, I.4
  • 20
    • 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 Journal of Food Engineering 87 1 2008 64 73
    • (2008) Journal of Food Engineering , vol.87 , Issue.1 , pp. 64-73
    • Krešić, G.1    Lelas, V.2    Jambrak, A.R.3    Herceg, Z.4    Brnčić, S.R.5
  • 21
    • 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 277 1970 680 685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 68549104038 scopus 로고    scopus 로고
    • Comparison of pH-dependent sonodisruption of re-assembled casein micelles by 35 and 130 kHz ultrasounds
    • A. Madadlou, M.E. Mousavi, Z. Emam-Djomeh, M. Ehsani, and D. Sheehan Comparison of pH-dependent sonodisruption of re-assembled casein micelles by 35 and 130 kHz ultrasounds Journal of Food Engineering 95 3 2009 505 509
    • (2009) Journal of Food Engineering , vol.95 , Issue.3 , pp. 505-509
    • Madadlou, A.1    Mousavi, M.E.2    Emam-Djomeh, Z.3    Ehsani, M.4    Sheehan, D.5
  • 24
    • 77949308270 scopus 로고    scopus 로고
    • Investigation of the microstructure of milk protein concentrate powders during rehydration: Alterations during storage
    • A. Mimouni, H.C. Deeth, A.K. Whittaker, M.J. Gidley, and B.R. Bhandari Investigation of the microstructure of milk protein concentrate powders during rehydration: alterations during storage Journal of Dairy Science 93 2 2010 463 472
    • (2010) Journal of Dairy Science , vol.93 , Issue.2 , pp. 463-472
    • Mimouni, A.1    Deeth, H.C.2    Whittaker, A.K.3    Gidley, M.J.4    Bhandari, B.R.5
  • 25
    • 0000149343 scopus 로고
    • Delactosed, high milk protein powder. 1. Manufacture and composition
    • V.V. Mistry, and H.N. Hassan Delactosed, high milk protein powder. 1. Manufacture and composition Journal of Dairy Science 74 4 1991 1163 1169
    • (1991) Journal of Dairy Science , vol.74 , Issue.4 , pp. 1163-1169
    • Mistry, V.V.1    Hassan, H.N.2
  • 26
    • 0032650808 scopus 로고    scopus 로고
    • Influence of different factors on the output power transferred into medium by ultrasound
    • J. Raso, P. Mañas, R. Pagán, and F.J. Sala Influence of different factors on the output power transferred into medium by ultrasound Ultrasonics Sonochemistry 5 4 1999 157 162
    • (1999) Ultrasonics Sonochemistry , vol.5 , Issue.4 , pp. 157-162
    • Raso, J.1    Mañas, P.2    Pagán, R.3    Sala, F.J.4
  • 27
    • 17444425380 scopus 로고    scopus 로고
    • Ultrasonication for tomato pectinmethylesterase inactivation: Effect of cavitation intensity and temperature on inactivation
    • DOI 10.1016/j.jfoodeng.2004.09.028, PII S0260877404004686
    • P. Raviyan, Z. Zhang, and H. Feng Ultrasonication for tomato pectinmethylesterase inactivation: effect of cavitation intensity and temperature on inactivation Journal of Food Engineering 70 2 2005 189 196 (Pubitemid 40538739)
    • (2005) Journal of Food Engineering , vol.70 , Issue.2 , pp. 189-196
    • Raviyan, P.1    Zhang, Z.2    Feng, H.3
  • 32
    • 0036225354 scopus 로고    scopus 로고
    • Characterization of protein components of natural and heat-treated milk fat globule membranes
    • DOI 10.1016/S0958-6946(02)00034-1, PII S0958694602000341
    • A. Ye, H. Singh, M.W. Taylor, and S.G. Anema Characterization of protein components of natural and heat-treated milk fat globule membranes International Dairy Journal 12 4 2002 393 402 (Pubitemid 34416025)
    • (2002) International Dairy Journal , vol.12 , Issue.4 , pp. 393-402
    • Ye, A.1    Singh, H.2    Taylor, M.W.3    Anema, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.