Temperature dependent membrane fouling during filtration of whey and whey proteins

Journal of Membrane Science

Volumn 492, Issue , 2015, Pages 364-370

  Steinhauer, Tim ^a   Hanély, Sabrina ^a   Bogendörfer, Kerstin ^a   Kulozik, Ulrich ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Membrane fouling; Temperature; Whey; Whey protein; lactoglobulin

Indexed keywords

CROSSLINKING; MEMBRANE FOULING; MEMBRANES; MICROFILTRATION; PORE SIZE; PROCESSING; PROTEINS; SPOILAGE; TEMPERATURE;

FILTRATION PERFORMANCE; IMPACT OF TEMPERATURES; INCREASING TEMPERATURES; LACTOGLOBULIN; PROCESSING TEMPERATURE; ULTRA-FILTRATION MEMBRANES; WHEY; WHEY PROTEINS;

DAIRIES;

CALCIUM; DISULFIDE; MILK PROTEIN; PROTEIN; THIOL;

ADSORPTION; ARTICLE; CROSS LINKING; FILTRATION; FOULING CONTROL; HEIGHT; MICROFILTRATION; PH; PRIORITY JOURNAL; PROCESSING; TEMPERATURE DEPENDENCE; ULTRAFILTRATION; WHEY;

EID: 84935000194     PISSN: 03767388     EISSN: 18733123     Source Type: Journal    
DOI: 10.1016/j.memsci.2015.05.053     Document Type: Article

References (49)

1. Gésan-Guiziou G., Boyaval E., Daufin G. Critical stability conditions in crossflow microfiltration of skimmed milk: transition to irreversible deposition. J. Memb. Sci. 1999, 158:211-222.
2. Jimenez-Lopez A.J., Leconte N., Dehainault O., Geneste C., Fromont L., Gésan-Guiziou G. Role of milk constituents on critical conditions and deposit structure in skimmilk microfiltration (0.1μm). Sep. Purif. Technol. 2008, 61:33-43.
3. Le Berre O., Daufin G. Skimmilk crossflow microfiltration performance versus permeation flux to wall shear stress ratio. J. Memb. Sci. 1996, 117:261-270.
4. Piry A., Kühnl W., Grein T., Tolkach A., Ripperger S., Kulozik U. Length dependency of flux and protein permeation in crossflow microfiltration of skimmed milk. J. Memb. Sci. 2008, 325:887-894.
5. Lee D.N., Merson R.L. Prefiltration of cottage cheese whey to reduce fouling of ultrafiltration membranes. J. Food Sci. 1976, 41:403-410.
6. Merin U. Bacteriological aspects of microfiltration of cheese whey. J. Dairy Sci. 1986, 69:326-328.
7. Piot M., Maubois J.-L., Schaegis P., Veyre R., Luccioni M. Microfiltration en flux tangentiel des lactosérums de fromagerie. Lait 1984, 64:102-120.
8. Pouliot M., Pouliot Y., Britten M., Rodrigue N. Microfiltration de lactosérum doux sur membranes d[U+05F3]alumine: influence des conditions hydrodynamiques sur le colmatage. Lait 1995, 75:117-131.
9. Steinhauer T., Schwing J., Krauß S., Kulozik U. Enhancement of ultrafiltration-performance and improvement of hygienic quality during the production of whey concentrates. Int. Dairy J. 2015.
10. Daly C. The use of mesophilic cultures in the dairy industry. Antonie van Leeuwenhoek 1983, 49:297-312.
11. Milch und Milchprodukte 2006, Behr, Hamburg. 2nd ed. H. Weber (Ed.).
12. Daufin G., Labbé J.-P., Quemerais A., Michel F., Merin U. Optimizing clarified whey ultrafiltration: influence of pH. J. Dairy Res. 1994, 61:355.
13. Labbé J.-P., Quemerais A., Michel F., Daufin G. Fouling of inorganic membranes during whey ultrafiltration: analytical methodology. J. Memb. Sci. 1990, 51:293-307.
14. Mourouzidis-Mourouzis S., Karabelas A. Whey protein fouling of microfiltration ceramic membranes-Pressure effects. J. Memb. Sci. 2006, 282:124-132.
15. Gésan G., Daufin G., Merin U., Labbé J.-P., Quemerais A. Microfiltration performance: physicochemical aspects of whey pretreatment. J. Dairy Res. 1995, 62:269.
16. M.W. Hickey, R.D. Hill, B.R. Smith, Investigations into the ultrafiltration and reverse osmosis of wheys, M.W., Hickey, (repr.), 1980.
17. Musale D.A., Kulkarni S.S. Effect of whey composition on ultrafiltration performance. J. Agric. Food Chem. 1998, 46:4717-4722.
18. Ramachandra Rao H.G. Mechanisms of flux decline during ultrafiltration of dairy products and influence of pH on flux rates of whey and buttermilk. Desalination 2002, 144:319-324.
19. Tsuge H., Tanaka Y., Hisamatsu N. Fouling of cheese whey during reverse osmosis and precipitation of calcium phosphate. Bioseparation Engineering 2000, 47-52. Elsevier Science BV, Amsterdam, The Netherlands. I. Endo, T. Nagamune, S. Katoh, T. Yonemoto (Eds.).
20. Campbell M.J., Walter R.P., McLoughlin R., Knowles C.J. Effect of temperature on protein conformation and activity during ultrafiltration. J. Memb. Sci. 1993, 78:35-43.
21. Monahan F.J., German J.B., Kinsella J.E. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J. Agric. Food Chem. 1995, 43:46-52.
22. Barukčić I., Božanić R., Kulozik U. Effect of pore size and process temperature on flux, microbial reduction and fouling mechanisms during sweet whey cross-flow microfiltration by ceramic membranes. Int. Dairy J. 2014, 39:8-15.
23. Muthukumaran S., Kentish S., Ashokkumar M., Stevens G. Mechanisms for the ultrasonic enhancement of dairy whey ultrafiltration. J. Memb. Sci. 2005, 258:106-114.
24. Christensen M.L., Sedin P., Theliander H., Keiding K. Pressure and concentration profiles in filter cake consisting of core/shell latex particle. Colloids Surf. A: Physicochem. Eng. Asp. 2006, 290:295-303.
25. Hwang K.-J., Wang Y.-T., Iritani E., Katagiri N. Effects of porous gel particle compression properties on microfiltration characteristics. J. Memb. Sci. 2009, 341:286-293.
26. Privalov P.L., Makhatadze G.I. Heat capacity of proteins. J. Mol. Biol. 1990, 213:385-391.
27. de Wit J.N. Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150°C. A review. Trends Food Sci. Technol. 2009, 20:27-34.
28. Meireles M., Aimar P., Sanchez V. Albumin denaturation during ultrafiltration: effects of operating conditions and consequences on membrane fouling. Biotechnol. Bioeng. 1991, 38:528-534.
29. 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 Sc. 2011, 1:886-892.
30. Ingham K., Busby T., Sahlestrom Y., Castino F. Separation of macromolecules by ultrafiltration: influence of protein adsorption, protein-protein interactions, and concentration polarization. Ultrafiltration Membranes and Applications 1980, 141-158. Springer, US. A. Cooper (Ed.).
31. Wahlgren M. Protein adsorption to solid surfaces. Trends Biotechnol. 1991, 9:201-208.
32. Wu X., Narsimhan G. Characterization of secondary and tertiary conformational changes of beta-lactoglobulin adsorbed on silica nanoparticle surfaces. Langmuir ACS J. Surf. Colloids 2008, 24:4989-4998.
33. Toro-Sierra J., Tolkach A., Kulozik U. Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale. Food Bioprocess Technol. 2013, 6:1032-1043.
34. Hanemaaijer J.H., Robbertsen T., van den Boomgaard Th., Gunnink J.W. Fouling of ultrafiltration membranes. The role of protein adsorption and salt precipitation. J. Memb. Sci. 1989, 40:199-217.
35. Voswinkel L., Kulozik U. Fractionation of whey proteins by means of membrane adsorption chromatography. Procedia Food Sci. 2011, 1:900-907.
36. Wang X.-M., Waite T.D. Impact of gel layer formation on colloid retention in membrane filtration processes. J. Memb. Sci. 2008, 325:486-494.
37. Tanford C., Bunville L.G., Nozaki Y. The reversible transformation of β-lactoglobulin at pH 7.5 1. J. Am. Chem. Soc. 1959, 81:4032-4036.
38. Tanford C., Taggart V.G. Ionization-linked changes in protein conformation. II. The N→R transition in β-lactoglobulin. J. Am. Chem. Soc. 1961, 83:1634-1638.
39. Dunnill P., Green D.W. Sulphydryl groups and the N→R conformational change in β-lactoglobulin. J. Mol. Biol. 1966, 15:147-151.
40. Steinhauer T., Marx M., Bogendörfer K., Kulozik U. Membrane fouling during ultra- and microfiltration of whey and whey proteins at different environmental conditions: the role of aggregated whey proteins as fouling initiators. J. Memb. Sci. 2015, 489:20-27.
41. 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.
42. Sakurai K., Goto Y. Dynamics and mechanism of the Tanford transition of bovine beta-lactoglobulin studied using heteronuclear NMR spectroscopy. J. Mol. Biol. 2006, 356:483-496.
43. Kelly S.T., Zydney A.L. Protein fouling during microfiltration: comparative behavior of different model proteins. Biotechnol. Bioeng. 1997, 55:91-100.
44. 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. J. Memb. Sci. 2010, 352:107-115.
45. 2+-induced gelation of pre-heated whey protein isolate. J. Food Sci. 1993, 58:867-871.
46. Marshall A.D., Munro P.A., Trägårdh G. Influence of ionic calcium concentration on fouling during the cross-flow microfiltration of β-lactoglobulin solutions. J. Memb. Sci. 2003, 217:131-140.
47. Xiong Y.L., Dawson K.A., Wan L. Thermal aggregation of β-lactoglobulin: effect of pH, ionic environment, and thiol reagent. J. Dairy Sci. 1993, 76:70-77.
48. Furukawa T., Kokubo K., Nakamura K., Matsumoto K. Modeling of the permeate flux decline during MF and UF cross-flow filtration of soy sauce lees. J. Memb. Sci. 2008, 322:491-502.
49. Alting A.C., Hamer R.J., Kruif de, Cornelus G., Paques M., Visschers R.W. Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels. Food Hydrocolloids 2003, 17:469-479.