메뉴 건너뛰기




Volumn 66, Issue , 2014, Pages 365-372

Effects of ozone processing on chemical, structural and functional properties of whey protein isolate

Author keywords

Functional properties; Gaseous ozone; Oxidation; Whey protein isolate

Indexed keywords

CHEMICAL ANALYSIS; DAIRIES; FLEXIBLE STRUCTURES; HYDROPHOBICITY; OXIDATION; OZONE; OZONIZATION; PROTEINS; SOLUBILITY; SULFUR COMPOUNDS; TURBIDITY;

EID: 84908268567     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2014.10.002     Document Type: Article
Times cited : (130)

References (63)
  • 1
    • 30944462757 scopus 로고    scopus 로고
    • Effect of cyclic exposure to ozone gas on physicochemical, sensorial and microbial quality of whole and sliced tomatoes
    • Aguayo E., Escalona V.H., Artés F. Effect of cyclic exposure to ozone gas on physicochemical, sensorial and microbial quality of whole and sliced tomatoes. Postharvest Biology and Technology 2006, 39(2):169-177.
    • (2006) Postharvest Biology and Technology , vol.39 , Issue.2 , pp. 169-177
    • Aguayo, E.1    Escalona, V.H.2    Artés, F.3
  • 2
    • 79954419026 scopus 로고    scopus 로고
    • Influence of aqueous ozone, blanching and combined treatments on microbial load of red bell peppers, strawberries and watercress
    • Alexandre E.M.C., Santos-Pedro D.M., Brandão T.R.S., Silva C.L.M. Influence of aqueous ozone, blanching and combined treatments on microbial load of red bell peppers, strawberries and watercress. Journal of Food Engineering 2011, 105(2):277-282.
    • (2011) Journal of Food Engineering , vol.105 , Issue.2 , pp. 277-282
    • Alexandre, E.M.C.1    Santos-Pedro, D.M.2    Brandão, T.R.S.3    Silva, C.L.M.4
  • 3
    • 0033550064 scopus 로고    scopus 로고
    • 8-Anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions
    • Ali V., Prakash K., Kulkarni S., Ahmad A., Madhusudan K.P., Bhakuni V. 8-Anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions. Biochemistry 1999, 39:13635-13642.
    • (1999) Biochemistry , vol.39 , pp. 13635-13642
    • Ali, V.1    Prakash, K.2    Kulkarni, S.3    Ahmad, A.4    Madhusudan, K.P.5    Bhakuni, V.6
  • 6
    • 85032119438 scopus 로고
    • Determination of free SH- and SS-groups in some food proteins using Ellman's reagent
    • Beveridge T., Toma S.J., Nakai S. Determination of free SH- and SS-groups in some food proteins using Ellman's reagent. Journal of Food Science 1974, 39:49-51.
    • (1974) Journal of Food Science , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.3
  • 8
    • 84872413885 scopus 로고    scopus 로고
    • Bran-induced changes in water structure and gluten conformation in model gluten dough studied by Fourier transform infrared spectroscopy
    • Bock J.E., Damodaran S. Bran-induced changes in water structure and gluten conformation in model gluten dough studied by Fourier transform infrared spectroscopy. Food Hydrocolloids 2013, 31(2):146-155.
    • (2013) Food Hydrocolloids , vol.31 , Issue.2 , pp. 146-155
    • Bock, J.E.1    Damodaran, S.2
  • 9
    • 30344478568 scopus 로고    scopus 로고
    • Functional properties of whey proteins as affected by dynamic high-pressure treatment
    • Bouaouina H., Desrumaux A., Loisel C., Legrand J. Functional properties of whey proteins as affected by dynamic high-pressure treatment. International Dairy Journal 2006, 16(4):275-284.
    • (2006) International Dairy Journal , vol.16 , Issue.4 , pp. 275-284
    • Bouaouina, H.1    Desrumaux, A.2    Loisel, C.3    Legrand, J.4
  • 10
    • 0041509039 scopus 로고    scopus 로고
    • On the action of ozone on proteins
    • Cataldo F. On the action of ozone on proteins. Polymer Degradation and Stability 2003, 82(1):105-114.
    • (2003) Polymer Degradation and Stability , vol.82 , Issue.1 , pp. 105-114
    • Cataldo, F.1
  • 11
    • 5644286427 scopus 로고    scopus 로고
    • On the action of ozone on methaemoglobin
    • Cataldo F. On the action of ozone on methaemoglobin. Polymer Degradation and Stability 2004, 86(3):473-481.
    • (2004) Polymer Degradation and Stability , vol.86 , Issue.3 , pp. 473-481
    • Cataldo, F.1
  • 13
    • 0002591498 scopus 로고    scopus 로고
    • Structure-function relationships of whey proteins
    • Marcel Dekker Inc., New York, USA, M. Dekker (Ed.)
    • Cayot P., Lorient D. Structure-function relationships of whey proteins. Food proteins and their applications 1997, Marcel Dekker Inc., New York, USA. M. Dekker (Ed.).
    • (1997) Food proteins and their applications
    • Cayot, P.1    Lorient, D.2
  • 14
    • 79956344900 scopus 로고    scopus 로고
    • Ultrasonics sonochemistry effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate
    • Chandrapala J., Zisu B., Palmer M., Kentish S., Ashokkumar M. Ultrasonics sonochemistry effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrasonics Sonochemistry 2011, 18(5):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
  • 17
    • 83455246381 scopus 로고    scopus 로고
    • Application of ozone sprays as a strategy to improve the microbial safety and quality of salmon fillets
    • Crowe K.M., Skonberg D., Bushway A., Baxter S. Application of ozone sprays as a strategy to improve the microbial safety and quality of salmon fillets. Food Control 2012, 25(2):464-468.
    • (2012) Food Control , vol.25 , Issue.2 , pp. 464-468
    • Crowe, K.M.1    Skonberg, D.2    Bushway, A.3    Baxter, S.4
  • 18
    • 84864405464 scopus 로고    scopus 로고
    • Hydroxyl radical-stressed whey protein isolate: chemical and structural properties
    • Cui X., Xiong Y.L., Kong B., Zhao X., Liu N. Hydroxyl radical-stressed whey protein isolate: chemical and structural properties. Food and Bioprocess Technology 2012, 5(6):2454-2461.
    • (2012) Food and Bioprocess Technology , vol.5 , Issue.6 , pp. 2454-2461
    • Cui, X.1    Xiong, Y.L.2    Kong, B.3    Zhao, X.4    Liu, N.5
  • 19
    • 33846003115 scopus 로고    scopus 로고
    • HPLC of proteose peptones for evaluating ageing of packaged pasteurized milk
    • De Noni I., Pellegrino L., Cattaneo S., Resmini P. HPLC of proteose peptones for evaluating ageing of packaged pasteurized milk. International Dairy Journal 2007, 17(1):12-19.
    • (2007) International Dairy Journal , vol.17 , Issue.1 , pp. 12-19
    • De Noni, I.1    Pellegrino, L.2    Cattaneo, S.3    Resmini, P.4
  • 20
    • 0002939524 scopus 로고
    • Functional properties of whey proteins
    • Elsevier Science Publishers Ltd, UK, P.F. Fox (Ed.)
    • De Wit J.N. Functional properties of whey proteins. Developments in dairy chemistry. 4. Functional milk proteins 1989, 285-321. Elsevier Science Publishers Ltd, UK. P.F. Fox (Ed.).
    • (1989) Developments in dairy chemistry. 4. Functional milk proteins , pp. 285-321
    • De Wit, J.N.1
  • 21
    • 0024900359 scopus 로고
    • Food colloids - an overview
    • Dickinson E. Food colloids - an overview. Colloids and Surfaces 1989, 42:191-204.
    • (1989) Colloids and Surfaces , vol.42 , pp. 191-204
    • Dickinson, E.1
  • 22
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • Dissanayake M., Vasiljevic T. Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science 2009, 92(4):1387-1397.
    • (2009) Journal of Dairy Science , vol.92 , Issue.4 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 23
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A., Huang P., Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 1990, 29(13):3303-3308.
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 26
    • 25844500998 scopus 로고    scopus 로고
    • Factors determining the physical properties of protein foams
    • Foegeding E.A., Luck P.J., Davis J.P. Factors determining the physical properties of protein foams. Food Hydrocolloids 2006, 20(2-3):284-292.
    • (2006) Food Hydrocolloids , vol.20 , Issue.2-3 , pp. 284-292
    • Foegeding, E.A.1    Luck, P.J.2    Davis, J.P.3
  • 27
    • 0036189807 scopus 로고    scopus 로고
    • Proteoso-peptone whey fraction as emulsifier in ice-cream preparation
    • Innocente N., Comparin D., Corradini C. Proteoso-peptone whey fraction as emulsifier in ice-cream preparation. International Dairy Journal 2002, 12:69-74.
    • (2002) International Dairy Journal , vol.12 , pp. 69-74
    • Innocente, N.1    Comparin, D.2    Corradini, C.3
  • 28
    • 0347596683 scopus 로고    scopus 로고
    • Dynamic surface properties of the proteoso-peptone fraction of bovine milk
    • Innocente N., Corradini C., Blecker C., Paquot M. Dynamic surface properties of the proteoso-peptone fraction of bovine milk. Journal of Dairy Science 1998, 81:1833-1839.
    • (1998) Journal of Dairy Science , vol.81 , pp. 1833-1839
    • Innocente, N.1    Corradini, C.2    Blecker, C.3    Paquot, M.4
  • 29
    • 0345504757 scopus 로고    scopus 로고
    • Emulsifying properties of the total fraction and the hydrophobic fraction of bovine milk proteoso-peptones
    • Innocente N., Corradini C., Blecker C., Paquot M. Emulsifying properties of the total fraction and the hydrophobic fraction of bovine milk proteoso-peptones. International Dairy Journal 1998, 8:981-985.
    • (1998) International Dairy Journal , vol.8 , pp. 981-985
    • Innocente, N.1    Corradini, C.2    Blecker, C.3    Paquot, M.4
  • 30
    • 77956610446 scopus 로고    scopus 로고
    • Feasibility of the SPME method for the determination of the aroma retention capacity of proteoso-peptone milk protein fraction at different pH values
    • Innocente N., Marchesini G., Biasutti M. Feasibility of the SPME method for the determination of the aroma retention capacity of proteoso-peptone milk protein fraction at different pH values. Food Chemistry 2011, 124:1249-1257.
    • (2011) Food Chemistry , vol.124 , pp. 1249-1257
    • Innocente, N.1    Marchesini, G.2    Biasutti, M.3
  • 32
  • 33
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe
    • Kato A., Nakai S. Hydrophobicity determined by a fluorescence probe. Biochimica et Biophysica Acta 1980, 624:13-20.
    • (1980) Biochimica et Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 34
    • 0346731071 scopus 로고    scopus 로고
    • Protein oxidation at the air-lung interface
    • Kelly F.J., Mudway I.S. Protein oxidation at the air-lung interface. Amino Acids 2003, 25(3-4):375-396.
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 375-396
    • Kelly, F.J.1    Mudway, I.S.2
  • 35
    • 0035665477 scopus 로고    scopus 로고
    • Microbiological aspects of ozone applications in food. A review
    • Khadre M.A., Yousef A.E., Kim J. Microbiological aspects of ozone applications in food. A review. Journal of Food Science 2001, 6:1242-1252.
    • (2001) Journal of Food Science , vol.6 , pp. 1242-1252
    • Khadre, M.A.1    Yousef, A.E.2    Kim, J.3
  • 36
    • 84908279933 scopus 로고    scopus 로고
    • Whey proteins
    • Woodhead Limited Publishing, Cambridge, England, R.Y. Yada (Ed.)
    • Kilara A., Vaghela M.N. Whey proteins. Proteins in food processing 2000, Woodhead Limited Publishing, Cambridge, England. R.Y. Yada (Ed.).
    • (2000) Proteins in food processing
    • Kilara, A.1    Vaghela, M.N.2
  • 37
    • 0032926433 scopus 로고    scopus 로고
    • Use of ozone to inactivate microorganisms on lattuce
    • Kim J., Yousef A.E., Chism G.W. Use of ozone to inactivate microorganisms on lattuce. Journal of Food Safety 1998, 19(1):17-34.
    • (1998) Journal of Food Safety , vol.19 , Issue.1 , pp. 17-34
    • Kim, J.1    Yousef, A.E.2    Chism, G.W.3
  • 40
    • 84871712931 scopus 로고    scopus 로고
    • Hydroxyl radical-stressed whey protein Isolate: Functional and rheological properties
    • Kong B., Xiong L.Y., Cui X., Zhao X. Hydroxyl radical-stressed whey protein Isolate: Functional and rheological properties. Food and Bioprocess Technology 2013, 6:169-176.
    • (2013) Food and Bioprocess Technology , vol.6 , pp. 169-176
    • Kong, B.1    Xiong, L.Y.2    Cui, X.3    Zhao, X.4
  • 41
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong J., Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica 2007, 39(8):549-559.
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 42
    • 84862573582 scopus 로고    scopus 로고
    • Structural changes imposed on whey proteins by UV irradiation in a continuous UV light reactor
    • Kristo E., Hazizaj A., Corredig M. Structural changes imposed on whey proteins by UV irradiation in a continuous UV light reactor. Journal of Agricultural and Food Chemistry 2012, 60:6204-6209.
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , pp. 6204-6209
    • Kristo, E.1    Hazizaj, A.2    Corredig, M.3
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of 339 bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of 339 bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 44
    • 46749110034 scopus 로고    scopus 로고
    • FactoMineR: An R package for multivariate analysis
    • Lê S., Josse J., Husson F. FactoMineR: An R package for multivariate analysis. Journal of Statistical Software 2008, 25(1):1-18.
    • (2008) Journal of Statistical Software , vol.25 , Issue.1 , pp. 1-18
    • Lê, S.1    Josse, J.2    Husson, F.3
  • 45
    • 29144447015 scopus 로고    scopus 로고
    • Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating
    • Li C.P., Enomoto H., Ohki S., Ohtomo H., Aoki T. Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating. Journal of Dairy Science 2005, 88(12):4137-4145.
    • (2005) Journal of Dairy Science , vol.88 , Issue.12 , pp. 4137-4145
    • Li, C.P.1    Enomoto, H.2    Ohki, S.3    Ohtomo, H.4    Aoki, T.5
  • 47
    • 0001090313 scopus 로고
    • Thermal denaturation and heat-induced gelation properties of β-lactoglobulin. Effects of some chemical parameters
    • Liu T.X., Relkin P., Launay B. Thermal denaturation and heat-induced gelation properties of β-lactoglobulin. Effects of some chemical parameters. Thermochimica Acta 1994, 246:387-403.
    • (1994) Thermochimica Acta , vol.246 , pp. 387-403
    • Liu, T.X.1    Relkin, P.2    Launay, B.3
  • 48
    • 0034284184 scopus 로고    scopus 로고
    • Oxidatively induced chemical changes and interactions of mixed myosin, b-lactoglobulin, and Soy 7S globulin
    • Liu G., Xiong Y.L. Oxidatively induced chemical changes and interactions of mixed myosin, b-lactoglobulin, and Soy 7S globulin. Journal of the Science of Food and Agriculture 2000, 80(99):1601-1607.
    • (2000) Journal of the Science of Food and Agriculture , vol.80 , Issue.99 , pp. 1601-1607
    • Liu, G.1    Xiong, Y.L.2
  • 49
    • 0033827809 scopus 로고    scopus 로고
    • Properties of oxidized myofibrils and whey- and soy-protein Isolates
    • Liu G., Xiong Y.L., Butterfield D.A. Properties of oxidized myofibrils and whey- and soy-protein Isolates. Journal of Food Science 2000, 65(5):811-818.
    • (2000) Journal of Food Science , vol.65 , Issue.5 , pp. 811-818
    • Liu, G.1    Xiong, Y.L.2    Butterfield, D.A.3
  • 50
    • 84882484578 scopus 로고    scopus 로고
    • Using proteins as additives in foods: An introduction
    • Woodhead, Cambridge, R.Y. Yada (Ed.)
    • Luyten J.M.J.G., Vereijken J.M., Buecking M. Using proteins as additives in foods: An introduction. Proteins in food processing 2004, 421-441. Woodhead, Cambridge. R.Y. Yada (Ed.).
    • (2004) Proteins in food processing , pp. 421-441
    • Luyten, J.M.J.G.1    Vereijken, J.M.2    Buecking, M.3
  • 52
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey
    • Monahan F.J., German J.B., Kinsellat J.E. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey. Proteins 1995, 43(1):46-52.
    • (1995) Proteins , vol.43 , Issue.1 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsellat, J.E.3
  • 53
    • 33845550183 scopus 로고
    • Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity
    • Nakai S. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. Journal of Agricultural and Food Chemistry 1983, 31:676-683.
    • (1983) Journal of Agricultural and Food Chemistry , vol.31 , pp. 676-683
    • Nakai, S.1
  • 54
    • 57849101027 scopus 로고    scopus 로고
    • Effect of dynamic heat treatment on the physical properties of whey protein foams
    • Nicorescu I., Loisel C., Riaublanc A., Vial C., Djelveh G., Cuvelier G., et al. Effect of dynamic heat treatment on the physical properties of whey protein foams. Food Hydrocolloids 2009, 23(4):1209-1219.
    • (2009) Food Hydrocolloids , vol.23 , Issue.4 , pp. 1209-1219
    • Nicorescu, I.1    Loisel, C.2    Riaublanc, A.3    Vial, C.4    Djelveh, G.5    Cuvelier, G.6
  • 56
    • 0032923417 scopus 로고    scopus 로고
    • Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin
    • Qin B.Y., Bewley M.C., Creamer L.K., Baker E.N., Jameson G.B. Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin. Protein Science 1999, 8(1):75-83.
    • (1999) Protein Science , vol.8 , Issue.1 , pp. 75-83
    • Qin, B.Y.1    Bewley, M.C.2    Creamer, L.K.3    Baker, E.N.4    Jameson, G.B.5
  • 58
  • 60
    • 33745242338 scopus 로고    scopus 로고
    • Foaming properties of sweet whey solutions as modified by thermal treatment
    • Tosi E., Canna L., Lucero H., Ré E. Foaming properties of sweet whey solutions as modified by thermal treatment. Food Chemistry 2007, 100(2):794-799.
    • (2007) Food Chemistry , vol.100 , Issue.2 , pp. 794-799
    • Tosi, E.1    Canna, L.2    Lucero, H.3    Ré, E.4
  • 61
    • 84860297622 scopus 로고    scopus 로고
    • Effects of ozone on functional properties of proteins
    • Uzun H., Ibanoglu E., Catal H., Ibanoglu S. Effects of ozone on functional properties of proteins. Food Chemistry 2012, 134(2):647-654.
    • (2012) Food Chemistry , vol.134 , Issue.2 , pp. 647-654
    • Uzun, H.1    Ibanoglu, E.2    Catal, H.3    Ibanoglu, S.4
  • 62
    • 77949277907 scopus 로고    scopus 로고
    • Dynamic high pressure-induced gelation in milk protein model systems
    • Venir E., Marchesini G., Biasutti M., Innocente N. Dynamic high pressure-induced gelation in milk protein model systems. Journal of Dairy Science 2010, 93(2):483-494.
    • (2010) Journal of Dairy Science , vol.93 , Issue.2 , pp. 483-494
    • Venir, E.1    Marchesini, G.2    Biasutti, M.3    Innocente, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.