Proteomics in quality control: Whey protein-based supplements

Journal of Proteomics

Volumn 147, Issue , 2016, Pages 48-55

  Garrido, Bruno Carius ^a   Souza, Gustavo H M F ^b   Lourenço, Daniela C ^a   Fasciotti, Maíra ^a  

^a INSTITUTO NACIONAL DE METROLOGIA   (Brazil)

^b WATERS CORPORATION   (United States)

Author keywords

Mass spectrometry; Nutritional supplements; Proteomics; Quality control; Whey protein

Indexed keywords

WHEY PROTEIN;

ARTICLE; BOVINE; CHICKEN; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DIETARY SUPPLEMENT; MAIZE; MASS SPECTROMETRY; NONHUMAN; POTATO; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEOMICS; QUALITY CONTROL; RICE; SOYBEAN; WHEAT; WHEY; ANALYSIS; ANIMAL; FOOD CONTAMINATION; PROCEDURES; STANDARDS;

ANIMALS; CATTLE; DIETARY SUPPLEMENTS; FOOD CONTAMINATION; MASS SPECTROMETRY; PROTEOMICS; QUALITY CONTROL; WHEY PROTEINS;

EID: 84964374510     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2016.03.044     Document Type: Article

References (56)

1. [1] Cavalcanti, G.A., Leal, F.D., Garrido, B.C., Padilha, M.C., de Aquino Neto, F.R., Detection of designer steroid methylstenbolone in “nutritional supplement” using gas chromatography and tandem mass spectrometry: elucidation of its urinary metabolites. Steroids 78 (2013), 228–233.
2. [2] Crowley, R., FitzGerald, L.H., The impact of cGMP compliance on consumer confidence in dietary supplement products. Toxicology 221 (2006), 9–16.
3. [3] de Hon, O., Coumans, B., The continuing story of nutritional supplements and doping infractions. Br. J. Sports Med. 41 (2007), 800–805.
4. [4] Geyer, H., Parr, M.K., Koehler, K., Mareck, U., Schanzer, W., Thevis, M., Nutritional supplements cross-contaminated and faked with doping substances. J. Mass Spectr. JMS. 43 (2008), 892–902.
5. [5] Geyer, H., Parr, M.K., Mareck, U., Reinhart, U., Schrader, Y., Schänzer, W., Analysis of non-hormonal nutritional supplements for anabolic-androgenic steroids — results of an international study. Int. J. Sports Med. 25 (2004), 124–129.
6. [6] Judkins, C.M.G., Teale, P., Hall, D.J., The role of banned substance residue analysis in the control of dietary supplement contamination. Drug Test. Anal. 2 (2010), 417–420.
7. [7] Maughan, R.J., Contamination of dietary supplements and positive drug tests in sport. J. Sports Sci. 23 (2005), 883–889.
8. [8] Nasr, J., Ahmad, J., Severe cholestasis and renal failure associated with the use of the designer steroid superdrol™ (Methasteron™): a case report and literature review. Dig. Dis. Sci. 54 (2009), 1144–1146.
9. [9] Parr, M.K., Fußhöller, G., Schlörer, N., Opfermann, G., Geyer, H., Rodchenkov, G., et al. Detection of Δ6-methyltestosterone in a “dietary supplement” and GC–MS/MS investigations on its urinary metabolism. Toxicol. Lett. 201 (2011), 101–104.
10. [10] Petróczi, A., Naughton, D.P., Mazanov, J., Holloway, A., Bingham, J., Performance enhancement with supplements: incongruence between rationale and practice. J. Int. Soc. Sports Nutr., 4, 2007.
11. [11] Groziak, S.M., Miller, G.D., Natural bioactive substances in milk and colostrum: effects on the arterial blood pressure system. Br. J. Nutr. 84:Suppl. 1 (2000), S119–S125.
12. [12] Haraguchi, F.K., De Abreu, W.C., De Paula, H., Whey Protein: Composition, Nutritional Properties, Applications in Sports and Benefits for Human Health (Trans.) Proteínas do soro do leite: Composição, propriedades nutricionais, aplicações no esporte e benefícios para a saúde humana., Vol. 19, 2006, 479–488.
13. [13] Lönnerdal, B., Nutritional and physiologic significance of human milk proteins. Amer. J. Clin. Nutr. 77 (2003), 1537S–1543S.
14. [14] Abernethy, G., Higgs, K., Rapid detection of economic adulterants in fresh milk by liquid chromatography-tandem mass spectrometry. J. Chromatogr. A 1288 (2013), 10–20.
15. [15] Calvano, C.D., De Ceglie, C., Aresta, A., Facchini, L.A., Zambonin, C.G., MALDI-TOF mass spectrometric determination of intact phospholipids as markers of illegal bovine milk adulteration of high-quality milk. Anal. Bioanal. Chem. 405 (2013), 1641–1649.
16. [16] Chen, H., Hsieh, C., Classification of different adulteration ratios of reconstituted milk in raw milk and fresh milk by using Vis/NIR spectroscopy. Int. Agric. Eng. J. 20 (2011), 50–61.
17. [17] Cordewener, J.H.G., Luykx, D.M.A.M., Frankhuizen, R., Bremer, M.G.E.G., Hooijerink, H., America, A.H.P., Untargeted LC-Q-TOF mass spectrometry method for the detection of adulterations in skimmed-milk powder. J. Sep. Sci. 32 (2009), 1216–1223.
18. [18] Neelima, Rao P.S., Sharma, R., YS, Rajput, Direct estimation of sialic acid in milk and milk products by fluorimetry and its application in detection of sweet whey adulteration in milk. J. Diary Res. 79 (2012), 495–501.
19. [19] Vallejo-Cordoba, B., A chemometric approach to the detection of milk adulteration based on protein profiles determined by capillary electrophoresis. J. Capillary Electr. Micro. Technol. 5 (1998), 133–137.
20. [20] Finete, VdLM, Gouvêa, M.M., FFdC, Marques, ADP, Netto, Is it possible to screen for milk or whey protein adulteration with melamine, urea and ammonium sulphate, combining Kjeldahl and classical spectrophotometric methods?. Food Chem. 141 (2013), 3649–3655.
21. [21] PricePlow, Amino Acid Spiking Scam: Is Your Protein Really PROTEIN?. 2014.
22. [22] D'Amato, A., Bachi, A., Fasoli, E., Boschetti, E., Peltre, G., Sénéchal, H., et al. In-depth exploration of cow's whey proteome via combinatorial peptide ligand libraries. J. Proteome Res. 8 (2009), 3925–3936.
23. [23] Hogarth, C.J., Fitzpatrick, J.L., Nolan, A.M., Young, F.J., Pitt, A., Eckersall, P.D., Differential protein composition of bovine whey: a comparison of whey from healthy animals and from those with clinical mastitis. Proteomics 4 (2004), 2094–2100.
24. [24] Le, A., Barton, L.D., Sanders, J.T., Zhang, Q., Exploration of bovine milk proteome in colostral and mature whey using an ion-exchange approach. J. Proteome Res. 10 (2011), 692–704.
25. [25] Nissen, A., Bendixen, E., Ingvartsen, K.L., Rontved, C.M., Expanding the bovine milk proteome through extensive fractionation. J. Dairy Sci., 17, 2013, 00719-4.
26. [26] Yang, Y., Zhao, X., Yu, S., Cao, S., Quantitative proteomic analysis of whey proteins in the colostrum and mature milk of yak (Bos grunniens). J. Sci. Food Agric. 95 (2014), 592–597.
27. [27] Ahmad, S., Ashfaq, A., Detection of microbial contamination in foods with advanced techniques. Asian J. Microbiol. Biotechnol. Environ. Sci. 13 (2011), 263–266.
28. [28] D'Alessandro, A., Zolla, L., Food safety and quality control: hints from proteomics. Food Technol. Biotechnol. 50 (2012), 275–285.
29. [29] D'Alessandro, A., Zolla, L., We are what we eat: food safety and proteomics. J. Proteome Res. 11 (2012), 26–36.
30. [30] Gallardo, J.M., Ortea, I., Carrera, M., Proteomics and its applications for food authentication and food-technology research. TrAC Trends Anal. Chem. 52 (2013), 135–141.
31. [31] Gašo-Sokač, D., Kovač, S., Josić, D., Application of proteomics in food technology and food biotechnology: process development, quality control and product safety. Food Technol. Biotechnol. 48 (2010), 284–295.
32. [32] Gašo-Sokač, D., Kovač, S., Josić, D., Use of proteomic methodology in optimization of processing and quality control of food of animal origin. Food Technol. Biotechnol. 49 (2011), 397–412.
33. [33] Piñeiro, C., Barros-Velázquez, J., Vázquez, J., Figueras, A., Gallardo, J.M., Proteomics as a tool for the investigation of seafood and other marine products. J. Proteome Res. 2 (2003), 127–135.
34. [34] Murad, A.M., Souza, G.H., Garcia, J.S., Rech, E.L., Detection and expression analysis of recombinant proteins in plant-derived complex mixtures using nanoUPLC-MS(E). J. Sep. Sci. 34 (2011), 2618–2630.
35. [35] Wu, C., Siems, W.F., Klasmeier, J., Hill, H.H., Separation of isomeric peptides using electrospray ionization/high-resolution ion mobility spectrometry. Anal. Chem. 72 (2000), 391–395.
36. [36] Ruotolo, B.T., Giles, K., Campuzano, I., Sandercock, A.M., Bateman, R.H., Robinson, C.V., Evidence for macromolecular protein rings in the absence of bulk water. Science 310 (2005), 1658–1661.
37. [37] Geromanos, S.J., Vissers, J.P., Silva, J.C., Dorschel, C.A., Li, G.Z., Gorenstein, M.V., et al. The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS. Proteomics 9 (2009), 1683–1695.
38. [38] Chakraborty, A.B., Berger, S.J., Gebler, J.C., Use of an integrated MS–multiplexed MS/MS data acquisition strategy for high-coverage peptide mapping studies. Rapid Commun. Mass Spectr. RCM. 21 (2007), 730–744.
39. [39] Yu, Y.Q., Gilar, M., Lee, P.J., Bouvier, E.S., Gebler, J.C., Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal. Chem. 75 (2003), 6023–6028.
40. [40] Lalli, P.M., Corilo, Y.E., Fasciotti, M., Riccio, M.F., de Sa, G.F., Daroda, R.J., et al. Baseline resolution of isomers by traveling wave ion mobility mass spectrometry: investigating the effects of polarizable drift gases and ionic charge distribution. J. Mass Spectr. JMS. 48 (2013), 989–997.
41. [41] Giles, K., Williams, J.P., Campuzano, I., Enhancements in travelling wave ion mobility resolution. Rapid Commun. Mass Spectr. RCM. 25 (2011), 1559–1566.
42. [42] Silva, J.C., Denny, R., Dorschel, C.A., Gorenstein, M., Kass, I.J., Li, G.Z., et al. Quantitative proteomic analysis by accurate mass retention time pairs. Anal. Chem. 77 (2005), 2187–2200.
43. [43] Silva, J.C., Gorenstein, M.V., Li, G.Z., Vissers, J.P., Geromanos, S.J., Absolute quantification of proteins by LCMSE: a virtue of parallel MS acquisition. Mol. Cell. Proteomics 5 (2006), 144–156.
44. [44] Li, G.Z., Vissers, J.P., Silva, J.C., Golick, D., Gorenstein, M.V., Geromanos, S.J., Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures. Proteomics 9 (2009), 1696–1719.
45. [45] Morris, H.R., Paxton, T., Dell, A., Langhorne, J., Berg, M., Bordoli, R.S., et al. High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer. Rapid Commun. mass Spectr. RCM. 10 (1996), 889–896.
46. [46] Morr, C.V., Ha, E.Y., Whey protein concentrates and isolates: processing and functional properties. Crit. Rev. Food Sci. Nutr. 33 (1993), 431–476.
47. [47] Bislev, S.L., Deutsch, E.W., Sun, Z., Farrah, T., Aebersold, R., Moritz, R.L., et al. A Bovine PeptideAtlas of milk and mammary gland proteomes. Proteomics 12 (2012), 2895–2899.
48. [48] Zhang, Q., C., Carpenter, Proteomics in milk and milk processing. Toldrá, F., LML, Nollet, (eds.) Proteomics., 2013, Foods Springer US, 223–245.
49. [49] Golinelli, L.P., Conte-Junior, C.A., Paschoalin, V.M.F., Silva, J.T., Proteomic analysis of whey from bovine colostrum and mature milk. Braz. Arch. Biol. Technol. 54 (2011), 761–768.
50. [50] Jayaprakasha, H.M., Yoon, Y.C., Production of functional whey protein concentrate by monitoring the process of ultrafiltration. Asian Austr. J. Anim. Sci. 18 (2005), 433–438.
51. [51] Renner, E., El-Salam, A., Application of Ultrafiltration in the Dairy Industry. 1991, Elsevier Applied Science, London, New york.
52. [52] Wu, C.C., MacCoss, M.J., Shotgun proteomics: tools for the analysis of complex biological systems. Curr. Opin. Mol. Ther. 4 (2002), 242–250.
53. [53] Meissner, F., Mann, M., Quantitative shotgun proteomics: considerations for a high-quality workflow in immunology. Nat. Immunol. 15 (2014), 112–117.
54. [54] Christensen, J.B., Dionisio, G., Poulsen, H.D., Brinch-Pedersen, H., Effect of pH and recombinant barley (Hordeum vulgare L.) endoprotease B2 on degradation of proteins in soaked barley. J. Agric. Food Chem. 62 (2014), 8562–8570.
55. [55] Nishikawa, K., Iwaya, K., Kinoshita, M., Fujiwara, Y., Akao, M., Sonoda, M., et al. Resveratrol increases CD68(+) Kupffer cells colocalized with adipose differentiation-related protein and ameliorates high-fat-diet-induced fatty liver in mice. Mol. Nutr. Food Res. 59 (2015), 1155–1170.
56. [56] Folkard, D.L., Melchini, A., Traka, M.H., Al-Bakheit, A., Saha, S., Mulholland, F., et al. Suppression of LPS-induced transcription and cytokine secretion by the dietary isothiocyanate sulforaphane. Mol. Nutr. Food Res. 58 (2014), 2286–2296.