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Volumn 96, Issue 9, 2013, Pages 5494-5500

PH treatment as an effective tool to select the functional and structural properties of yak milk caseins

Author keywords

Functional property; PH; Structural property; Yak milk casein

Indexed keywords

BOS GRUNNIENS;

EID: 84882898418     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2013-6609     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 0000579294 scopus 로고
    • The influence of processing parameters on food protein functionality. 1. Differential scanning calorimetry as an indicator of protein denaturation
    • Arntfield S.D., Murray E.D. The influence of processing parameters on food protein functionality. 1. Differential scanning calorimetry as an indicator of protein denaturation. Canadian Inst. Food Sci. Technol. J 1981, 14:289-294.
    • (1981) Canadian Inst. Food Sci. Technol. J , vol.14 , pp. 289-294
    • Arntfield, S.D.1    Murray, E.D.2
  • 2
    • 1642346225 scopus 로고    scopus 로고
    • Studies on physicochemical and functional properties of commercial sweet whey powders
    • Banavara D.S., Anupama D., Rankin S.A. Studies on physicochemical and functional properties of commercial sweet whey powders. J. Dairy Sci 2003, 86:3866-3875.
    • (2003) J. Dairy Sci , vol.86 , pp. 3866-3875
    • Banavara, D.S.1    Anupama, D.2    Rankin, S.A.3
  • 3
    • 0000356729 scopus 로고
    • A Colloidal approach of milk acidification by glucono-delta-lactone
    • Banon S., Hardy J. A Colloidal approach of milk acidification by glucono-delta-lactone. J. Dairy Sci 1992, 75:935-941.
    • (1992) J. Dairy Sci , vol.75 , pp. 935-941
    • Banon, S.1    Hardy, J.2
  • 4
    • 34250000513 scopus 로고    scopus 로고
    • PH-induced structural transitions of caseins
    • Chakraborty A., Basak S. pH-induced structural transitions of caseins. J. Photochem. Photobiol. B 2007, 87:191-199.
    • (2007) J. Photochem. Photobiol. B , vol.87 , pp. 191-199
    • Chakraborty, A.1    Basak, S.2
  • 5
    • 0000900989 scopus 로고
    • Studies on micellar calcium-phosphate: Composition and apparent solubility product in milk over a wide pH range
    • Chaplin L.C. Studies on micellar calcium-phosphate: Composition and apparent solubility product in milk over a wide pH range. J. Dairy Res 1984, 51:251-257.
    • (1984) J. Dairy Res , vol.51 , pp. 251-257
    • Chaplin, L.C.1
  • 6
    • 84971758074 scopus 로고
    • PH-induced dissociation of bovine casein micelles. 1. Analysis of liberated caseins
    • Dalgleish D.G., Law A.J.R. pH-induced dissociation of bovine casein micelles. 1. Analysis of liberated caseins. J. Dairy Res 1988, 55:529-538.
    • (1988) J. Dairy Res , vol.55 , pp. 529-538
    • Dalgleish, D.G.1    Law, A.J.R.2
  • 7
    • 1642356627 scopus 로고    scopus 로고
    • Structural aspects of functional properties of milk proteins
    • Dziuba J., Darewicz M. Structural aspects of functional properties of milk proteins. Natural Sci 2000, 4:257-272.
    • (2000) Natural Sci , vol.4 , pp. 257-272
    • Dziuba, J.1    Darewicz, M.2
  • 8
    • 0037214940 scopus 로고    scopus 로고
    • Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis
    • Flanagan J., FitzGerald R.J. Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis. Int. Dairy J 2003, 13:135-143.
    • (2003) Int. Dairy J , vol.13 , pp. 135-143
    • Flanagan, J.1    FitzGerald, R.J.2
  • 10
    • 0030139289 scopus 로고    scopus 로고
    • Heat-induced modification of the functional properties of sodium caseinate
    • Guo M.R., Fox P.F., Flynn A., Kindstedt P.S. Heat-induced modification of the functional properties of sodium caseinate. Int. Dairy J 1996, 6:473-485.
    • (1996) Int. Dairy J , vol.6 , pp. 473-485
    • Guo, M.R.1    Fox, P.F.2    Flynn, A.3    Kindstedt, P.S.4
  • 11
    • 43049111426 scopus 로고    scopus 로고
    • Reformation of casein particles from alkaline-disrupted casein micelles
    • Huppertz T., Vaia B., Smiddy M.A. Reformation of casein particles from alkaline-disrupted casein micelles. J. Dairy Res 2008, 75:44-47.
    • (2008) J. Dairy Res , vol.75 , pp. 44-47
    • Huppertz, T.1    Vaia, B.2    Smiddy, M.A.3
  • 12
    • 0030728622 scopus 로고    scopus 로고
    • Heat-induced hydrolysis of sodium caseinate
    • Hustinx J.C.A., Singh T.K., Fox P.F. Heat-induced hydrolysis of sodium caseinate. Int. Dairy J 1997, 7:207-212.
    • (1997) Int. Dairy J , vol.7 , pp. 207-212
    • Hustinx, J.C.A.1    Singh, T.K.2    Fox, P.F.3
  • 13
    • 0033868551 scopus 로고    scopus 로고
    • Soluble protein fractions from pH and heat treated sodium caseinate: Physicochemical and functional properties
    • Jahaniaval F., Kakuda Y., Abraham V., Marcone M.F. Soluble protein fractions from pH and heat treated sodium caseinate: Physicochemical and functional properties. Food Res. Int 2000, 33:637-647.
    • (2000) Food Res. Int , vol.33 , pp. 637-647
    • Jahaniaval, F.1    Kakuda, Y.2    Abraham, V.3    Marcone, M.F.4
  • 14
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A., Nakai S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 1980, 624:13-20.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 15
    • 0001183694 scopus 로고
    • Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH
    • Lee S.-Y., Morr C.V., Ha E.Y.W. Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH. J. Food Sci 1992, 57:1210-1229.
    • (1992) J. Food Sci , vol.57 , pp. 1210-1229
    • Lee, S.-Y.1    Morr, C.V.2    Ha, E.Y.W.3
  • 16
    • 21344483421 scopus 로고
    • Thermal modification of sodium caseinate. 1. Influence of temperature and pH on selected physicochemical and functional properties
    • Lieske B., Konrad G. Thermal modification of sodium caseinate. 1. Influence of temperature and pH on selected physicochemical and functional properties. Milchwissenschaft 1994, 49:16-20.
    • (1994) Milchwissenschaft , vol.49 , pp. 16-20
    • Lieske, B.1    Konrad, G.2
  • 18
    • 46049093569 scopus 로고    scopus 로고
    • PH-dependent structures and properties of casein micelles
    • Liu Y., Guo R. pH-dependent structures and properties of casein micelles. Biophys. Chem 2008, 136:67-73.
    • (2008) Biophys. Chem , vol.136 , pp. 67-73
    • Liu, Y.1    Guo, R.2
  • 21
    • 0034643864 scopus 로고    scopus 로고
    • Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC
    • Micard V., Guilbert S. Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC. Int. J. Biol. Macromol 2000, 27:229-236.
    • (2000) Int. J. Biol. Macromol , vol.27 , pp. 229-236
    • Micard, V.1    Guilbert, S.2
  • 22
    • 41549146106 scopus 로고    scopus 로고
    • Functional properties of fish protein hydrolysates from Pacific whiting (Merluccius productus) muscle produced by a commercial protease
    • Pacheco-Aguilar R., Mazorra-Manzano M.A., Ramírez-Suárez J.C. Functional properties of fish protein hydrolysates from Pacific whiting (Merluccius productus) muscle produced by a commercial protease. Food Chem 2008, 109:782-789.
    • (2008) Food Chem , vol.109 , pp. 782-789
    • Pacheco-Aguilar, R.1    Mazorra-Manzano, M.A.2    Ramírez-Suárez, J.C.3
  • 23
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce K.N., Kinsella J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. J. Agric. Food Chem 1978, 26:716-723.
    • (1978) J. Agric. Food Chem , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 24
    • 0000529133 scopus 로고
    • Casein association and micelle formation
    • Elsevier Applied Science, Barking, UK, P.F. Fox (Ed.)
    • Rollema H.S. Casein association and micelle formation. Advanced Dairy Chemistry, Vol. 1: Proteins 1992, 111-140. Elsevier Applied Science, Barking, UK. P.F. Fox (Ed.).
    • (1992) Advanced Dairy Chemistry, Vol. 1: Proteins , pp. 111-140
    • Rollema, H.S.1
  • 25
    • 84863525829 scopus 로고    scopus 로고
    • Simple pH treatment as an effective tool to improve the functional properties of ovomucin
    • Shan Y., Ma M., Huang X., Guo Y., Jin G., Jin Y. Simple pH treatment as an effective tool to improve the functional properties of ovomucin. J. Food Sci 2012, 77:C740-C745.
    • (2012) J. Food Sci , vol.77
    • Shan, Y.1    Ma, M.2    Huang, X.3    Guo, Y.4    Jin, G.5    Jin, Y.6
  • 26
    • 0027310276 scopus 로고
    • Emulsifying properties of protein fractions prepared from heated milk
    • Singh H., Fox P.F., Cuddigan M. Emulsifying properties of protein fractions prepared from heated milk. Food Chem 1993, 47:1-6.
    • (1993) Food Chem , vol.47 , pp. 1-6
    • Singh, H.1    Fox, P.F.2    Cuddigan, M.3
  • 27
    • 0031434142 scopus 로고    scopus 로고
    • Heat capacity and thermodynamic characteristics of denaturation and glass transition of hydrated and anhydrous proteins
    • Sochava I.V. Heat capacity and thermodynamic characteristics of denaturation and glass transition of hydrated and anhydrous proteins. Biophys. Chem 1997, 69:31-41.
    • (1997) Biophys. Chem , vol.69 , pp. 31-41
    • Sochava, I.V.1
  • 28
    • 0036149125 scopus 로고    scopus 로고
    • Formation and stability of sodium caseinate emulsions: Influence of retorting (121 C for 15min) before or after emulsification
    • Srinivasan M., Singh H., Munro P.A. Formation and stability of sodium caseinate emulsions: Influence of retorting (121 C for 15min) before or after emulsification. Food Hydrocoll 2002, 16:153-160.
    • (2002) Food Hydrocoll , vol.16 , pp. 153-160
    • Srinivasan, M.1    Singh, H.2    Munro, P.A.3
  • 29
    • 24144467835 scopus 로고    scopus 로고
    • Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase
    • Tang C., Yang X.-Q., Chen Z., Wu H., Peng Z.-Y. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. J. Food Biochem 2005, 29:402-421.
    • (2005) J. Food Biochem , vol.29 , pp. 402-421
    • Tang, C.1    Yang, X.-Q.2    Chen, Z.3    Wu, H.4    Peng, Z.-Y.5
  • 30
    • 33751222558 scopus 로고    scopus 로고
    • Solvent-mediated disruption of bovine casein micelles at alkaline pH
    • Vaia B., Smiddy M.A., Kelly A.L. Solvent-mediated disruption of bovine casein micelles at alkaline pH. J. Agric. Food Chem 2006, 54:8288-8293.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 8288-8293
    • Vaia, B.1    Smiddy, M.A.2    Kelly, A.L.3
  • 31
    • 0001558145 scopus 로고
    • PH-induced physicochemical changes of casein micelles in milk and their effect on renneting 1. Effect of acidification on physicochemical properties
    • van Hooydonk A.C.M., Hagedoorn H.G., Boerrigter J. pH-induced physicochemical changes of casein micelles in milk and their effect on renneting 1. Effect of acidification on physicochemical properties. Neth. Milk Dairy J 1986, 40:281-296.
    • (1986) Neth. Milk Dairy J , vol.40 , pp. 281-296
    • van Hooydonk, A.C.M.1    Hagedoorn, H.G.2    Boerrigter, J.3
  • 32
    • 1842421102 scopus 로고    scopus 로고
    • Phosphorylation of proteins and their functional and structural properties
    • American Chemical Society Press. Washington, DC, N. Parris, A. Kato, L.K. Creamer, J. Pearce (Eds.)
    • Vojdani F., Whitaker J.R. Phosphorylation of proteins and their functional and structural properties. Macromolecular Interactions in Food Technology 1996, 650:210-229. American Chemical Society Press. Washington, DC. N. Parris, A. Kato, L.K. Creamer, J. Pearce (Eds.).
    • (1996) Macromolecular Interactions in Food Technology , vol.650 , pp. 210-229
    • Vojdani, F.1    Whitaker, J.R.2
  • 33
    • 38849139630 scopus 로고    scopus 로고
    • Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates
    • Wang X.-S., Tang C.-H., Li B.-S., Yang X.-Q., Li L., Ma C.-Y. Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocoll 2008, 22:560-567.
    • (2008) Food Hydrocoll , vol.22 , pp. 560-567
    • Wang, X.-S.1    Tang, C.-H.2    Li, B.-S.3    Yang, X.-Q.4    Li, L.5    Ma, C.-Y.6
  • 34
    • 22044452941 scopus 로고
    • Changes occurring in proteins in alkaline solutions
    • American Chemical Society Press, Washington, DC, J.R. Whitaker, M. Fujimaki (Eds.)
    • Whitaker J.R. Changes occurring in proteins in alkaline solutions. Chemical Deterioration of Proteins 1980, 123:146-160. American Chemical Society Press, Washington, DC. J.R. Whitaker, M. Fujimaki (Eds.).
    • (1980) Chemical Deterioration of Proteins , vol.123 , pp. 146-160
    • Whitaker, J.R.1
  • 35
    • 84882868096 scopus 로고    scopus 로고
    • Study on browning factors and process optimization of casein purified from Qula
    • Harbin Institute of Technol., Harbin, China
    • Yu M. Study on browning factors and process optimization of casein purified from Qula. MS Thesis 2008, Harbin Institute of Technol., Harbin, China.
    • (2008) MS Thesis
    • Yu, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.