Production and membrane fractionation of bioactive peptides from a whey protein concentrate

Journal of Food Engineering

Volumn 184, Issue , 2016, Pages 1-9

  Arrutia, Fátima ^a   Rubio, Rocío ^a   Riera, Francisco A ^a  

^a UNIVERSITY OF OVIEDO   (Spain)

Author keywords

Bioactive peptides; Nanofiltration; Peptide fractionation; Ultrafiltration; Whey protein hydrolysate

Indexed keywords

ELASTICITY; HYDRATION; NUCLEAR MAGNETIC RESONANCE; RHEOLOGY;

ENHANCED SURFACE; INTERACTION POTENTIALS; MICRO-PARTICLES; MICROPARTICULATED WHEY PROTEINS; PARTICLE CHARACTERISTICS; PROTEIN MICROPARTICLES; SPIN-SPIN RELAXATION; YOGHURT;

PROTEINS;

EID: 85010868082     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2016.03.010     Document Type: Article

References (50)

1. Adjonu, R., Doran, G., Torley, P., Agboola, S., Screening of whey protein isolate hydrolysates for their dual functionality: influence of heat pre-treatment and enzyme specificity. Food Chem. 136:3 (2013), 1435–1443.
2. Adler-Nissen, J., Enzymic Hydrolysis of Food Proteins. 1986, Elsevier Applied Science Publishers, Essex, UK.
3. Burns, D.B., Zydney, A.L., Effect of solution pH on protein transport through ultrafiltration membranes. Biotechnol. Bioeng. 64:1 (1999), 27–37.
4. Butylina, S., Luque, S., Nyström, M., Fractionation of whey-derived peptides using a combination of ultrafiltration and nanofiltration. J. Membr. Sci. 280:1 (2006), 418–426.
5. Cheison, S.C., Bor, E.K., Faraj, A.K., Kulozik, U., Selective hydrolysis of α-lactalbumin by Acid Protease A offers potential for β-lactoglobulin purification in whey proteins. LWT-Food Sci. Technol. 49:1 (2012), 117–122.
6. Cheison, S.C., Wang, Z., Xu, S.-Y., Hydrolysis of whey protein isolate in a tangential flow filter membrane reactor: I. Characterisation of permeate flux and product recovery by multivariate data analysis. J. Membr. Sci. 283:1 (2006), 45–56.
7. Cheryan, M., Ultrafiltration and Microfiltration Handbook. 1998, CRC press.
8. Da Costa, E.L., Da Rocha Gontijo, J.A., Netto, F.M., Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates. Int. Dairy J. 17:6 (2007), 632–640.
9. Demers-Mathieu, V., Gauthier, S.F., Britten, M., Fliss, I., Robitaille, G., Jean, J., Antibacterial activity of peptides extracted from tryptic hydrolyzate of whey protein by nanofiltration. Int. Dairy J. 28:2 (2013), 94–101.
10. Doyen, A., Husson, E., Bazinet, L., Use of an electrodialytic reactor for the simultaneous β-lactoglobulin enzymatic hydrolysis and fractionation of generated bioactive peptides. Food Chem 136:3 (2013), 1193–1202.
11. Fernández, A., Suárez, A., Zhu, Y., FitzGerald, R.J., Riera, F.A., Membrane fractionation of a β-lactoglobulin tryptic digest: effect of the pH. J. Food Eng. 114:1 (2013), 83–89.
12. Fernández, A., Zhu, Y., FitzGerald, R.J., Riera, F.A., Membrane fractionation of a β-lactoglobulin tryptic digest: effect of the membrane characteristics. J. Chem. Technol. Biotechnol. 89:4 (2014), 508–515.
13. Ferreira, I., Pinho, O., Mota, M., Tavares, P., Pereira, A., Goncalves, M., Torres, D., Rocha, C., Teixeira, J., Preparation of ingredients containing an ACE-inhibitory peptide by tryptic hydrolysis of whey protein concentrates. Int. Dairy J. 17:5 (2007), 481–487.
14. FitzGerald, R., Meisel, H., Lactokinins: Whey protein – derived ACE inhibitory peptides. Food/Nahrung 43:3 (1999), 165–167.
15. Groleau, P.E., Lapointe, J.-F., Gauthier, S.F., Pouliot, Y., Effect of aggregating peptides on the fractionation of β-LG tryptic hydrolysate by nanofiltration membrane. J. Membr. Sci. 234:1 (2004), 121–129.
16. Guadix, A., Camacho, F., Guadix, E.M., Production of whey protein hydrolysates with reduced allergenicity in a stable membrane reactor. J. Food Eng. 72:4 (2006), 398–405.
17. Hernández-Ledesma, B., Recio, I., Amigo, L., β-Lactoglobulin as source of bioactive peptides. Amino Acids 35:2 (2008), 257–265.
18. Huisman, I.H., Prádanos, P., Hernández, A., The effect of protein–protein and protein–membrane interactions on membrane fouling in ultrafiltration. J. Membr. Sci. 179:1 (2000), 79–90.
19. Jacquot, A., Gauthier, S.F., Drouin, R., Boutin, Y., Proliferative effects of synthetic peptides from β-lactoglobulin and α-lactalbumin on murine splenocytes. Int. Dairy J 20:8 (2010), 514–521.
20. Kitts, D.D., Weiler, K., Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. Curr. Pharm. Des. 9:16 (2003), 1309–1323.
21. Konrad, G., Kleinschmidt, T., A new method for isolation of native α-lactalbumin from sweet whey. Int. Dairy J. 18:1 (2008), 47–54.
22. Lacroix, I.M., Li-Chan, E.C., Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. Int. Dairy J 25:2 (2012), 97–102.
23. Lapointe, J.-F., Gauthier, S.F., Pouliot, Y., Bouchard, C., Effect of hydrodynamic conditions on fractionation of β-lactoglobulin tryptic peptides using nanofiltration membranes. J. Membr. Sci. 212:1 (2003), 55–67.
24. Lapointe, J.-F., Gauthier, S.F., Pouliot, Y., Bouchard, C., Characterization of interactions between β-lactoglobulin tryptic peptides and a nanofiltration membrane: impact on the surface membrane properties as determined by contact angle measurements. J. Membr. Sci. 261:1 (2005), 36–48.
25. Lapointe, J.-F., Gauthier, S.F., Pouliot, Y., Bouchard, C., Fouling of a nanofiltration membrane by a β-lactoglobulin tryptic hydrolysate: impact on the membrane sieving and electrostatic properties. J. Membr. Sci. 253:1 (2005), 89–102.
26. Lau, D.C., Yan, H., Dhillon, B., Metabolic syndrome: a marker of patients at high cardiovascular risk. Can. J. Cardiol. 22 (2006), 85B–90B.
27. Madureira, A., Tavares, T., Gomes, A.M.P., Pintado, M., Malcata, F.X., Invited review: physiological properties of bioactive peptides obtained from whey proteins. J. Dairy Sci. 93:2 (2010), 437–455.
28. Martin-Orue, C., Bouhallab, S., Garem, A., Nanofiltration of amino acid and peptide solutions: mechanisms of separation. J. Membr. Sci. 142:2 (1998), 225–233.
29. Minkiewicz, P., Dziuba, J., Iwaniak, A., Dziuba, M., Darewicz, M., BIOPEP database and other programs for processing bioactive peptide sequences. J. AOAC Int. 91:4 (2008), 965–980.
30. Mota, M., Ferreira, I., Oliveira, M., Rocha, C., Teixeira, J., Torres, D., Gonçalves, M., Trypsin hydrolysis of whey protein concentrates: characterization using multivariate data analysis. Food Chem. 94:2 (2006), 278–286.
31. Mullally, M.M., Meisel, H., FitzGerald, R.J., Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins. Int. Dairy J. 7:5 (1997), 299–303.
32. Murakami, M., Tonouchi, H., Takahashi, R., Kitazawa, H., Kawai, Y., Negishi, H., Saito, T., Structural analysis of a new anti-hypertensive peptide (β-lactosin B) isolated from a commercial whey product. J. Dairy Sci. 87:7 (2004), 1967–1974.
33. Nagaoka, S., Futamura, Y., Miwa, K., Awano, T., Yamauchi, K., Kanamaru, Y., Tadashi, K., Kuwata, T., Identification of novel hypocholesterolemic peptides derived from bovine milk β-lactoglobulin. Biochem. Biophys. Res. Commun. 281:1 (2001), 11–17.
34. Nielsen, P., Petersen, D., Dambmann, C., Improved method for determining food protein degree of hydrolysis. J. Food Sci. 66:5 (2001), 642–646.
35. O'Keeffe, M.B., FitzGerald, R.J., Antioxidant effects of enzymatic hydrolysates of whey protein concentrate on cultured human endothelial cells. Int. Dairy J. 36:2 (2014), 128–135.
36. Pan, D., Cao, J., Guo, H., Zhao, B., Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate. Food Chem. 130:1 (2012), 121–126.
37. Pellegrini, A., Dettling, C., Thomas, U., Hunziker, P., Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochim. Biophys. Acta (BBA)-General Subj. 1526:2 (2001), 131–140.
38. Pihlanto-Leppälä, A., Rokka, T., Korhonen, H., Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins. Int. Dairy J. 8:4 (1998), 325–331.
39. Pouliot, Y., Gauthier, S.F., L'Heureux, J., Effect of peptide distribution on the fractionation of whey protein hydrolysates by nanofiltration membranes. Le. Lait. 80:1 (2000), 113–120.
40. Pouliot, Y., Wijers, M., Gauthier, S., Nadeau, L., Fractionation of whey protein hydrolysates using charged UF/NF membranes. J. Membr. Sci. 158:1 (1999), 105–114.
41. Power, O., Fernández, A., Norris, R., Riera, F., FitzGerald, R., Selective enrichment of bioactive properties during ultrafiltration of a tryptic digest of β-lactoglobulin. J. Funct. Foods 9 (2014), 38–47.
42. Schmidt, D., Poll, J., Enzymatic hydrolysis of whey proteins. Hydrolysis of α-lactalbumin and β-lactoglobulin in buffer solutions by proteolytic enzymes. Ned. melk Zuiveltijdschr. 45:4 (1991), 225–240.
43. Silveira, S.T., Martínez-Maqueda, D., Recio, I., Hernández-Ledesma, B., Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin. Food Chem 141:2 (2013), 1072–1077.
44. Smithers, G.W., Whey and whey proteins—from ‘gutter-to-gold’. Int. Dairy J. 18:7 (2008), 695–704.
45. Susanto, H., Ulbricht, M., Influence of ultrafiltration membrane characteristics on adsorptive fouling with dextrans. J. Membr. Sci. 266:1 (2005), 132–142.
46. Tavares, T.G., Amorim, M., Gomes, D., Pintado, M.E., Pereira, C.D., Malcata, F.X., Manufacture of bioactive peptide-rich concentrates from Whey: characterization of pilot process. J. Food Eng. 110:4 (2012), 547–552.
47. Tulipano, G., Faggi, L., Nardone, A., Cocchi, D., Caroli, A.M., Characterisation of the potential of β-lactoglobulin and α-lactalbumin as sources of bioactive peptides affecting incretin function: in silico and in vitro comparative studies. Int. Dairy J. 48 (2015), 66–72.
48. Urista, C.M., Fernández, R.Á., Rodriguez, F.R., Cuenca, A.A., Jurado, A.T., Review: production and functionality of active peptides from milk. Food Sci. Technol. Int. 17:4 (2011), 293–317.
49. Wada, Y., Lönnerdal, B., Bioactive peptides derived from human milk proteins—mechanisms of action. J. Nutr. Biochem. 25:5 (2014), 503–514.
50. Zeman, L., Wales, M., Steric rejection of polymeric solutes by membranes with uniform pore size distribution. Sep. Sci. Technol. 16:3 (1981), 275–290.