Influence of Heat Treatment and Microfiltration on the Milk Proteins Properties

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Authors

  • Silvani Verruck Department of Food Science and Technology, Federal University of Santa Catarina (UFSC), Agricultural Science Center, Florianópolis, Santa Catarina, Brazil
  • Saionara Sartor Department of Food Science and Technology, Federal University of Santa Catarina (UFSC), Agricultural Science Center, Florianópolis, Santa Catarina, Brazil
  • Flávia Buss Marenda Department of Food Science and Technology, Federal University of Santa Catarina (UFSC), Agricultural Science Center, Florianópolis, Santa Catarina, Brazil
  • Eulália Lopes da Silva Barros Department of Chemical and Food Engineering, Federal University of Santa Catarina (UFSC),Technological Center, Florianópolis, Santa Catarina. Brazil
  • Callebe Camelo-Silva Department of Chemical and Food Engineering, Federal University of Santa Catarina (UFSC),Technological Center, Florianópolis, Santa Catarina. Brazil
  • Maria Helena Machado Canella Department of Food Science and Technology, Federal University of Santa Catarina (UFSC), Agricultural Science Center, Florianópolis, Santa Catarina, Brazil
  • Elane Schwinden Prudencio Department of Food Science and Technology, Federal University of Santa Catarina (UFSC), Agricultural Science Center, Florianópolis, Santa Catarina, Brazil; Department of Chemical and Food Engineering, Federal University of Santa Catarina (UFSC),Technological Center, Florianópolis, Santa Catarina. Brazil

DOI:

https://doi.org/10.17140/aftnsoj-5-157

Keywords:

Microfiltration, Heat treatment, Milk proteins

Abstract

Heat treatments are the established food technology for commercial processing of milk. However, degradation of valuable nutrients in milk (as proteins) and its sensory characteristics occur during these processes due to substantial heat exposure. The most important reactions that occur during milk heat treatment are the whey proteins denaturation, its interactions with the casein micelles and aggregation/dissociation of the casein micelles. Microfiltration represents an emerging food processing technology allowing gentle milk preservation at lower temperatures for similar, or better, nutritive value, microbial removal, and shelf stability. Thus, the aim of this work is to review the existing studies on the effects of microfiltration on milk proteins by comparing with the effects of heating treatments.

References

Fox PF. History of dairy chemistry. In: Fuquay JW, Fox PF, Mcsweeney PLH, eds. Encyclopedia of Dairy Sciences, 2nd ed. Cambridge, Massachusetts, USA: Academic Press; 2011: 18-25

Damodaran S. Aminoácido S, Peptídeos E Proteínas. In: Damodaran S, Parkin KL, Fennema OR, eds. Química De Alimentos De Fennema, 4th ed. Porto Alegre, Canada: Artmed; 2010

Foegeding EA, Davis JP, Doucet D, Mcguffey MK. Advances in modifying and understanding whey protein functionality. Trends in Food Science and Technology. 2002; 13: 151-159. doi: 10.1016/S0924- 2244(02)00111-5

Steinhauer T, Kühnl W, Kulozik U. Impact of protein interactions and transmembrane pressure on physical properties of filter cakes formed during filtrations of skim milk. Procedia Food Science. 2011; 1: 886-892. doi: 10.1016/j.profoo.2011.09.134

Fox PF, Mcsweeney PLH. Milk proteins. In: Fox PF, McSwee ney PLH. eds. Dairy Chemistry and Biochemistry. New York, USA: Blackie Academic & Professional; 1998: 146-237

Farrell HM. Casein nomenclature, structure, and association. In: Fuquay JW, Fox PF, Mcsweeney PLH, eds. Encyclopedia of Dairy Sciences. 2 nd ed. Cambridge, Massachusetts, USA: Academic Press; 2011: 765-771

Walstra P, Wouters JT, Geurts TJ. Dairy Science and Technology. 2nd ed. Oxfordshire, UK: Taylor & Francis Group; 2006

Burton H. Ultra-High-Temperature Processing of Milk and Milk Products. New York, USA: Elsevier Applied Science Publishers; 1988

Mottar J, Naudts M. La qualité du lait chauffé à ultrahaute température comparée à celle du lait pasteurisé et stérilisé dans la bouteille. Lait. 1979; 59: 476-488. doi: 10.1051/lait:197958823

Burton, H. Reviews of the progress of dairy science: the bacteriological, chemical, biochemical and physical changes that oc cur in milk at temperatures of 100-150 degrees C. Journal of Dairy Research. 1984; 51: 341-363

Cheeseman GC, Knight DC. The nature of casein aggregates in heated and stored milk. Journal of Dairy Research. 1974; 41: 359- 366. doi: 10.1017/S0022029900019804

Douglas FW, Greenberg Jr. R, Farrell Jr, HM, Edmondson LF. Effects of ultra-high-temperature pasteurization on milk proteins. Journal of Agricultural and Food Chemistry. 1981; 29: 11-15. doi: 10.1021/jf00103a004

Singh H, Latham JM. Heat stability of milk: Aggregation and dissociation of protein at ultra-high temperatures. International Dairy Journal. 1993; 3: 225-237. doi: 10.1016/0958- 6946(93)90066-9

Cosio MS, Mannino S, Buratti S. Electrochemical sensor 61 Review | Volume 5 | Number 2| Adv Food Technol Nutr Sci Open J. 2019; 5(2): 54-66. doi: 10.17140/AFTNSOJ-5-157 Verruck S, et al detecting free sulfhydryl groups: Evaluation of milk heat treat ment. J Dairy Sci. 2000; 83: 1933-1938. doi: 10.3168/jds.S0022- 0302(00)75068-5

Elliott AJ, Datta N, Amenu B, Deeth HC. Heat-induced and other chemical changes in commercial UHT milks. J Dairy Res. 2005; 72: 442-446. doi: 10.1017/S002202990500138X

Pellegrino L, De Noni I, Resmini P. Coupling of lactulose and furosine indices for quality evaluation of sterilized milk. International Dairy Journal. 1995; 5: 647-659. doi: 10.1016/0958- 6946(95)00036-3

Borcherding K, Lorenzen PC, Hoffmann W, Schrader K. Effect of foaming temperature and varying time/temperature conditions of pre-heating on the foaming properties of skimmed milk. International Dairy Journal. 2008; 18: 349-358. doi: 10.1016/j. idairyj.2007.11.016

Krasaekoopt W, Bhandari B, Deeth H. Yogurt from UHT milk: A review. Australian Journal of Dairy Technology. 2003; 58: 26- 29

Parnell-Clunies E, Kakuda Y, Deman JM, Cazzola F. Gelation profiles of yogurt as affected by heat treatment of milk. J Dairy Sci. 1988; 71: 582-588. doi: 10.3168/jds.S0022-0302(88)79594-6

Wang Q, Bulca S, Kulozik U. A comparison of low-intensity ultrasound and oscillating rheology to assess the renneting properties of casein solutions after UHT heat pre-treatment. International Dairy Journal. 2007; 17: 50-58. doi: 10.1016/j.idairyj.2005.12.008

Al-Akoum O, Ding LH, Jaffrin MY. Microfiltration and ultrafiltration of UHT skim milk with a vibrating membrane module. Separation and Purification Technology. 2002; 28: 219-234. doi: 10.1016/S1383-5866(02)00076-X

Amornkul Y, Henning DR. Utilization of microfiltration or lactoperoxidase system or both for manufacture of cheddar cheese from raw milk. J Dairy Sci. 2007; 90: 4988-5000. doi: 10.3168/jds.2007-0281

Carvalho AF, Maubois JL. Applications of membrane technologies in the dairy industry. In: Coimbra JSR, Teixeira JA, eds. Engineering Aspects of Milk and Dairy Products. Boca Raton, Florida, USA: CRC Press; 2009: 33-56

Elwell MW, Barbano DM. Use of microfiltration to improve fluid milk quality. J Dairy Sci. 2006; 89: 20-30. doi: 10.3168/jds. S0022-0302(06)72361-X

Fritsch J, Moraru CI. Development and optimization of car bon dioxideaided cold microfiltration process for the physical removal of microorganisms and somatic cells from skim milk. J Dairy Sci. 2008; 91: 3744-3760. doi: 10.3168/jds.2007-0899

Larsen PH. Microfiltration for pasteurised milk. In: Fox PF, ed. Heat Treatments and Alternative Methods. Belgium: International Dairy Federation; 1995: 232-239

Meershon M. Nitrate free cheesemaking with bactocatch. North European Food Dairy Journal. 1989; 55: 108-113

Saboya LV, Maubois JL. Current developments of microfiltration technology in the dairy industry. Lait. 2000; 80: 541-553. doi: 10.1051/lait:2000144

Trouve E, Maubois JL, Piot M, et al. Rètention de différentesespécesmicrobienneslors de l’epuration du lait par microfiltration en flux tangentiel. Lait. 1991; 71: 1-13

Amelia I, Barbano DM. Production of an 18% protein liquid micellar casein concentrate with a long refrigerated shelf life. J Dairy Sci. 2013; 96: 3340-3349. doi: 10.3168/jds.2012-6033

Brans G, Schroën CGPH, Van Der Sman RGM, Boom RM. Membrane fractionation of milk: State of the art and challenges. Journal of Membrane Science. 2004; 243: 263-272

Papadatos A, Neocleous M, Berger AM, Barbano DM. Economic feasibility evaluation of microfiltration of milk prior to cheesemaking. J Dairy Sci. 2003; 86: 1564-1577. doi: 10.3168/jds. S0022-0302(03)73742-4

Messens W, Camp V, Huyghebaert A. The use of high pressure to modify the functionality of food proteins. Trends in Food Science and Technology. 1997; 8: 107-112. doi: 10.1016/S0924- 2244(97)01015-7

Foegeding EA, Davis JP. Food protein functionality: A comprehensive approach. Food Hydrocolloids. 2011; 25: 1853-1864. doi: 10.1016/j.foodhyd.2011.05.008

Swaisgood HE. Características do leite. In: Damodaran S, Parkin KL, Fennema OR, eds. Química De Alimentos De Fennema. 4 th ed. Porto Alegre: Artmed. 2010

De Kruif CG, Huppertz T, Urban VS, Petukhov AV. Casein micelles and their internal structure. Adv Colloid Interface Sci. 2012; 171: 36-52. doi: 10.1016/j.cis.2012.01.002

De Kruif CG, Holt C. Casein micelle structure, functions and interactions. In: Fox PF, McSweeney PLH, eds. Advanced Dairy Chemistry, 3 rd ed. New York, USA: Kluwer Academic/Plenum Publishers; 2003: 233-276

Swaisgood HE. Symposium: Genetic perspectives on milk proteins: Comparative studies and nomenclature. Review and update of casein chemistry. J Dairy Sci. 1993; 76: 3054-3060

Raikos V. Effect of heat treatment on milk protein functionality at emulsion interfaces: A review. Food Hydrocolloids. 2010; 24: 259-265. doi: 10.1016/j.foodhyd.2009.10.014 62Review | Volume 5 | Number 2| Adv Food Technol Nutr Sci Open J. 2019; 5(2): 54-66. doi: 10.17140/AFTNSOJ-5-157 Verruck S, et al

Baier D, Schmitt C, Knorr D. Effect of high pressure-low temperature processing on composition and colloidal stability of casein micelles and whey proteins. International Dairy Journal. 2015; 43: 51-60. doi: 10.1016/j.idairyj.2014.11.008

Crowley P, O’Brien CM, Slattery H, Chapman D, Arendt EK, Stanton C. Functional properties of casein hydrolysates in bakery applications. European Food Research and Technology. 2002; 215: 131- 137. doi: 10.1007/s00217-002-0510-5

Erdem YK. Modification of casein micelle structure caused by ultrafiltration and heat treatment: A spectrofluorimetric and kinetic approach. Journal of Food Engineering. 2006; 74: 536-541. doi: 10.1016/j.jfoodeng.2005.03.041

Considine T, Patel HA, Anema SG, Singh H, Creamer LK. Interactions of milk proteins during heat and high hydrostatic pressure treatments-A review. Innovative Food Science and Emerging Technologies. 2007; 8: 1-23. doi: 10.1016/j.ifset.2006.08.003

Kuwajima K, Ikeguchi M, Sugawara T, Hiraoka Y, Sugai S. Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the cys6-cys120 disulfide bond. Biochemistry. 1990; 29: 8240-8249. doi: 10.1021/ bi00488a007

Wijayanti HB, Bansal N, Deeth HC. Stability of whey proteins during thermal processing: A review. Comprehensives Reviews in Food Science and Food Safety. 2014; 13: 1235-1251. doi: 10.1111/1541- 4337.12105

Angel CR, Dalgleish DG. Structures and some properties of soluble protein complexes formed by the heating of reconstituted skim milk powder. Food Research International. 2006; 39: 472- 479. doi: 10.1016/j.foodres.2005.09.010

Gani A, Broadway AA, Ahamd M, et al. Effect of whey and casein protein hydrolysates on rheological, textural and sensory properties of cookies. J Food Sci Technol. 2014; 35: 1-9. doi: 10.1007/s13197-014-1649-3

Singh H, Waungana A. Influence of heat treatment of milk on cheesemaking properties. International Dairy Journal. 2001; 11: 543-551. doi: 10.1016/S0958-6946(01)00085-1

Nicorescu I, Loisel C, Vial C, et al. Combined effect of dynamic heat treatment and ionic strength on the properties of whey protein foams–Part II. Food Research International. 2008; 41: 980-988. doi: 10.1016/j.foodres.2008.08.003

Jelen P, Rattray W. Thermal denaturation of whey proteins. In: Fox PF, ed. Heat-Induced Changes in Milk. 2 nd ed. Belgium: International Dairy Federation; 1995: 66-85

Pellegrino L, Cattaneo S, De Noni I. Effects of processing on protein quality of milk and milk products. In: Fuquay JW, Fox PF, Mcsweeney PLH, eds. Encyclopedia of Dairy Sciences. 2 nd ed. Cambridge, Massachusetts, USA: Academic Press; 2011: 226-234

Kinsella JE. Relationships between structure and functional properties of food proteins. In: Fox PF, Condon JJ. Food Proteins. New York, USA: Applied Science; 1982: 51-103

Corredig M, Dalgleish DG. Effect of different heat treat ments on the strong binding interactions between whey proteins and milk fat globules in whole milk. Journal of Dairy Research. 1996; 63: 441-449. doi: 10.1017/S0022029900031940

Jeanson S, Dupont D, Grattard N, Rolet-Répécaud O. Char acterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured α-Lactalbumin. J Agric Food Chem. 1999; 47: 2249-2254. doi: 10.1021/jf9809232

Patel HA, Singh H, Anema SG, Creamer LK. Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk. J Agric Food Chem. 2006; 54: 3409-3420. doi: 10.1021/jf052834c

Dannenberg F, Kessler HG. Reaction kinetics of the denaturation of whey proteins in milk. Journal of Food Science. 1998; 53: 258-263. doi: 10.1111/j.1365-2621.1988.tb10223.x

Oldfield DJ, Singh H, Taylor MW, Pearce KN. Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-hight temperature (UHT) pilot plant. International Dairy Journal. 1998; 8: 311-318. doi: 10.1016/S0958-6946(98)00089-2

Singh H, Creamer LK. Heat stability of milk. In: FOX PF. Advanced Dairy Chemistry. 2 nd ed. Barking, London: Elsevier Applied Science; 1992: 621-656

Wolfschoon-Pombo AF, Fernandes RM, Granzinolli GGM. Efeitos da pasteurizacao-HTST e da fervura domestica sobre a proteína do leite [In: French]. Revista do Instituto de Laticínios Cândido Tostes. 1982; 37: 3-7

Claeys WL, Ludikhuyze LR, Van Loey AM, Hendrickx ME. Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation kinetics of β-lactoglobulin in raw milk under isothermal and dynamic temperature conditions. J Dairy Res. 2001; 68: 95-107

Oldfield DJ, Singh H, Taylor MW. Association of β-lactoglobulin and α-lactalbumin whit the casein micelles in skim milk heated in an ultra-hight temperature plant. International Dairy Journal. 1998; 8: 765-770. doi: 10.1016/S0958-6946(98)00127-7

Walkling-Ribeiro M, Rodríguez-González O, Jayaram S, Griffiths MW. Microbial inactivation and shelf life comparison of ‘cold’ hurdle processing with pulsed electric fields and microfiltration, and conventional thermal pasteurisation in skim milk. Int J Food Microbiol. 2011; 144: 379-386. doi: 10.1016/j.ijfoodmicro.2010.10.023 63 Review | Volume 5 | Number 2| Adv Food Technol Nutr Sci Open J. 2019; 5(2): 54-66. doi: 10.17140/AFTNSOJ-5-157 Verruck S, et al

Hoffmann W, Kiesner C, Clawin-Raedecker I, et al. Processing of extended shelf life milk using microfiltration. International Journal of Dairy Technology. 2006; 59: 229-235. doi: 10.1111/j.1471- 0307.2006.00275.x

Kaufmann V, Kulozik U. Kombination von mikrofiltration und thermischen verfahrenzur haltbarkeits verlängerung von lebensmitteln. Chemie Ingenieur Technik. 2006; 78: 1647-1654. doi: 10.1002/cite.200600094

Fernández García L, Álvarez Blanco S, Riera Rodríguez FA. Microfiltration applied to dairy streams: Removal of bacteria. J Sci Food Agric. 2013; 93(2): 187-196. doi: 10.1002/jsfa.5935

Fromm HI, Boor KJ. Characterization of pasteurized fluid milk shelf-life attributes. Journal of Food Science. 2004; 69: 207-214. doi: 10.1111/j.1365-2621.2004.tb09889.x

Barbano DM, Ma Y, Santos MV. Influence of raw milk quality on fluid milk shelf life. J Dairy Sci. 2006; 89 Suppl 1: E15-19. doi: 10.3168/jds.S0022-0302(06)72360-8

Gesan-Guiziou G. Removal of bacteria, spores and somatic cells from milk by centrifugation and microfiltration techniques. In: Griffiths MW, ed. Improving the Safety and Quality of Milk. Sawston, Cambridge: Woodhead Publishing; 2010: 349-372

Pouliot Y. Membrane processes in dairy technology—From a simple idea to worldwide panacea. International Dairy Journal. 2008; 18: 735-740. doi: 10.1016/j.idairyj.2008.03.005

Baker RW. Membrane Technology and Applications. 2 nd ed. New York, USA: John Wiley and Sons; 2004: 538

Rosenberg M. Current and future applications for membrane processes in the dairy industry. Trends in Food and Technology. 1995; 6: 12-19. doi: 10.1016/S0924-2244(00)88912-8

Wiston WS, Sirkar KK. Membrane Handbook. New York, USA: Springer Publishers; 1992: 3-16

Avalli A, Povolo M, Carminati D, Contarini GA. Significance of 2-heptanone in evaluating the effect of microfiltration/pasteurisation applied to goats’ milk. International Dairy Journal. 2004; 14: 915-921. doi: 10.1016/j.idairyj.2004.03.004

Azzara CD, Dimick PS. Lipoprotein lipase activity of milk from cows with prolonged subclinical mastitis. J Dairy Sci. 1985; 68: 3171-3175. doi: 10.3168/jds.S0022-0302(85)81223-6

Ma Y, Ryan C, Barbano DM, et al. Effects of somatic cell count on quality and shelf-life of pasteurized fluid milk. J Dairy Sci. 2000; 83: 264-274. doi: 10.3168/jds.S0022-0302(00)74873-9

Te Giffel MC, Van Der Horst HC. Comparison between bac tofugation and microfiltration regarding efficiency of somatic cell and bacteria removal. Bulletin of the International Dairy Federation. 2004; 389: 49-53

Verdi RJ, Barbano DM. Preliminary investigation of the properties of somatic cell proteases. J Dairy Sci. 1988; 71: 534-538. doi: 10.3168/jds.S0022-0302(88)79586-7

Tan TJ, Wang D, Moraru CI. A physicochemical investigation of membrane fouling in cold microfiltration of skim milk. J Dairy Sci. 2014; 97(8): 4759-4771. doi: 10.3168/jds.2014-7957

Fuente EBL, Torrestiana-Sanchez B, Martínez-Gonzalez E, Mainou-Sierra JM. Microfiltration of whole milk with silicon microsieves: Effect of process variables. Chemical Engineering Research and Design. 2010; 88: 653-660. doi: 10.1016/j.cherd.2009.09.014

James BJ, Jing Y, Chen XD. Membrane fouling during filtration of milk—A microstructural study. Journal of Food Engineering. 2003; 60: 431-437. doi: 10.1016/S0260-8774(03)00066-9

Dickinson, E. Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology. Colloids and Surfaces B: Biointerfaces. 1999; 15: 161-176. doi: 10.1016/S0927-7765(99)00042-9

Nakanishi K, Sakiyama T, Imamura K. On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J Biosci Bioeng. 2001; 91(3): 233-244. doi: 10.1016/ S1389-1723(01)80127-4

Fane AG, Chang S. Techniques to enhance performance of membrane processes. In: Pabby AK, Rizvi SSH, Sastre AM. Handbook of Membrane Separations: Chemical, Pharmaceutical, Food, and Biotechnological Applications. Boca Raton, Florida: CRC Press; 2009: 193-232

Gesan-Guiziou G, Boyaval E, Daufin G. Critical stability conditions in crossflow microfiltration of skim milk: Transition to irreversible fouling. Journal of Membrane Science. 1999; 158: 211-222. doi: 10.1016/S0376-7388(99)00017-4

Wang K, Zhou C, HongY, Zhang X. A review of protein adsorption on bioceramics. Interface Focus. 2012; 2: 259-277. doi: 10.1098/rsfs.2012.0012

Gao N, Li M, Jing W, Fan Y, Xu N. Improving the filtration performance of ZrO2 membrane in non-polar organic solvents by surface hydrophobic modification. Journal of Membrane Science. 2011; 375: 276-283. doi: 10.1016/j.memsci.2011.03.056

Chandavarkar AS. Dynamics of fouling of microporous membranes by proteins. United States. Massachusetts Institute of Technology. 1990; 274-284

Kim KJ, Chen V, Fane AG. Some factors determining protein aggregation during ultrafiltration. Biotechnol Bioeng. 1993; 42: 260- 265. doi: 10.1002/bit.260420216

Jaspe J, Hagen SJ. Do protein molecules unfold in a simple 64Review | Volume 5 | Number 2| Adv Food Technol Nutr Sci Open J. 2019; 5(2): 54-66. doi: 10.17140/AFTNSOJ-5-157 Verruck S, et al shear flow? Biophys J. 2006; 91: 3415-3424. doi: 10.1529/biophysj.106.089367

Kelly ST, Opong WS, Zydney AL. The influence of protein aggregates on the fouling of microfiltration membranes during stirred cell filtration. Journal of Membrane Science. 1993; 80: 175- 187. doi: 10.1016/0376-7388(93)85142-J

Kelly ST, Zydney AL. Effects of intermolecular thiol–disulfide interchange reactions on BSA fouling during microfiltration. Biotechnol Bioeng. 1994; 44: 972-982. doi: 10.1002/bit.260440814

Kelly ST, Zydney AL. Mechanisms for BSA fouling during microfiltration. Journal of Membrane Science. 1995; 107: 115-127. doi: 10.1016/0376-7388(95)00108-O

Kelly ST, Zydney AL. Protein fouling during microfiltration: Comparative behavior of different model proteins. Biotechnol Bioeng, 1997; 55: 91-100. doi: 10.1002/(SICI)1097- 0290(19970705)55:1<91::AID-BIT11>3.0.CO;2-6

Wit JN. Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150C. A review. Trends in Food Science Technology. 2009; 20: 27-34. doi: 10.1016/j.tifs.2008.09.012

Barbut S, Foegeding EA. Ca2+ -induced gelation of pre-heated whey protein isolate. Journal of Food Science. 1993; 58: 867-871. doi: 10.1111/j.1365-2621.1993.tb09379.x

Xiong YL, Dawson KA, Wan L. Thermal aggregation of β-lactoglobulin: Effect of pH, ionic environment, and thiol reagent. J Dairy Sci. 1993; 76: 70-77. doi: 10.3168/jds.S0022- 0302(93)77324-5

Marshall AD, Munro PA, Trägårdh G. Influence of ionic calcium concentration on fouling during the cross-flow microfiltration of β-lactoglobulin solutions. Journal of Membrane Science. 2003; 217: 131-140. doi: 10.1016/S0376-7388(03)00085-1

Edwards PB, Creamer LK, Jameson GB. Structure and stability of whey proteins. In: Boland M, Singh H, Thompson A. Milk Proteins. Amsterdam, Netherlands: Elsevier; 2008: 163-203

Kühnl W, Piry A, Kaufmann V, Grein T, Ripperger S, Kulozik U. Impact of colloidal interactions on the flux in cross-flow microfiltration of milk at different pH values: A surface energy approach. Journal of Membrane Science. 2010; 352: 107-115. doi: 10.1016/j.memsci.2010.02.006

Svanborg S, Johansen AG, Abrahamsen RK, Skeie SB. Initial pasteurization effects on the protein fractionation of skimmed milk by microfiltration. International Dairy Journal. 2014; 37: 26-30. doi: 10.1016/j.idairyj.2014.02.004

McMahon DJ, Paulson B, Oberg CJ. Influence of calcium, pH, and moisture on protein matrix structure and functionality in direct-acidified nonfat Mozzarella cheese. J Dairy Sci. 2005; 88: 3754-3763. doi: 10.3168/jds.S0022-0302(05)73061-7

Kaombe DD, Du YH, Lewis MJ. Mineral partitioning in milk and milk permeates at high temperature. J Dairy Res. 2012; 79: 1-6. doi: 10.1017/S0022029911000616

Morison KR, Mackay FM. Viscosity of lactose and whey protein solutions. International Journal of Food Properties. 2001; 4: 441-454. doi: 10.1081/JFP-100108647

Hurt EE, Adams MC, Barbano DM. Microfiltration of skim milk and modified skim milk using a 0.1-µm ceramic uniform transmembrane pressure system at temperatures of 50, 55, 60, and 65 °C. J Dairy Sci. 2015; 98(2): 765-780. doi: 10.3168/ jds.2014-8775

Long JE, Van Winkle Q, Gould JA. Heat-induced interaction between crude κ-casein and β-lactoglobulin. J Dairy Sci. 1963; 46: 1393-1396. doi: 10.3168/jds.S0022-0302(63)89276-0

Dalgleish DG, Senaratne V, Francois S. Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation. Journal of Agricultural and Food Chemistry. 1997; 45: 3459-3464. doi: 10.1021/jf970113a

Moro A, Gatti C, Delorenzi N. Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties. J Agric Food Chem. 2001; 49: 4784-4789. doi: 10.1021/jf001132e

Wu X, Narsimhan G. Characterization of secondary and tertiary conformational changes of beta-lactoglobulin adsorbed on silica nanoparticle surfaces. Langmuir. 2008; 24: 4989-4998. doi: 10.1021/la703349c

Steinhauer T, Schwing J, Krauß S, Kulozik U. Enhancement of ultrafiltration performance and improvement of hygienic quality during the production of whey concentrates. International Dairy Journal. 2015; 45: 8-14. doi: 10.1016/j.idairyj.2015.01.010

Marshall AD, Munro PA, Trägårdh G. Influence of permeate flux on fouling during the microfiltration of β-lactoglobulin solutions under cross-flow conditions. Journal of Membrane Science. 1997; 130: 23-30. doi: 10.1016/S0376-7388(97)00004-5

Mourouzidis-Mourouzis S, Karabelas A. Whey protein fouling of microfiltration ceramic membranes—pressure effects. Journal of Membrane Science. 2006; 282: 124-132. doi: 10.1016/j. memsci.2006.05.012

Mourouzidis-Mourouzis S, Karabelas A. Whey protein fouling of large poresize ceramic microfiltration membranes at small cross-flow velocity. Journal of Membrane Science. 2008; 323: 17-27. doi: 10.1016/j.memsci.2008.05.053

Pinto MS, Pires ACS, Sant’ana HMP, Soares NFF, Carvalho AF. Influence of multilayer packaging and microfiltration process 65 Review | Volume 5 | Number 2| Adv Food Technol Nutr Sci Open J. 2019; 5(2): 54-66. doi: 10.17140/AFTNSOJ-5-157 Verruck S, et al on milk shelf life. Food Packaging and Shelf Life. 2014; 1: 151-159. doi: 10.1016/j.fpsl.2014.01.006

Lewis M. Improving pasteurized and extended shelf-life milk. In: Griffiths MW, ed. Improving the Safety and Quality of Milk. Sawston, Cambridge: Woodhead Publishing; 2010: 277-301. Submit your article to this journal | https://openventio.org/submit-manuscript/ 66Review | Volume 5 | Number 2|

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2019-06-14

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Silvani Verruck, Saionara Sartor, Flávia Buss Marenda, Eulália Lopes da Silva Barros, Callebe Camelo-Silva, Maria Helena Machado Canella, & Elane Schwinden Prudencio. (2019). Influence of Heat Treatment and Microfiltration on the Milk Proteins Properties. Advances in Food Technology and Nutrition Sciences, 5(2), 54–66. https://doi.org/10.17140/aftnsoj-5-157

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