Abstract
Cider contains low amount of proteins that, nonetheless, can affect its stability, foam formation and potential allergenicity. At present, scarce information is available on cider proteins, probably due to the lack of methods for their recovery and analysis. The aim of the present study was to set up a method for recovering and quantifying cider proteins. To this purpose, the proteins from 13 Italian commercial ciders were recovered by dialysis, gel filtration, trichloroacetic acid/acetone (TCA/acetone) and potassium dodecyl sulfate (KDS) precipitation. The protein content of the samples was then determined by bicinchoninic acid (BCA), Bradford and o-phthaldialdehyde (OPA) assays. The results were compared to quantitative data obtained by densitometry of electrophoretic gels. The most reliable protocol resulted in the KDS method followed by OPA assay. KDS, in addition, allowed also to separate proteins from glycocompounds. KDS/OPA is the method of choice for cider proteins precipitation and quantification.
References
Alberti A, Braga CM, Jaster H, Nogueira A (2014) Dissolved oxygen content in apple must: technological implications in cider processing. J Inst Brew 120:65–70
Anton MJ, Suarez Valles B, Garcia Hevia A, Picinelli Lobo A (2014) Aromatic profile of ciders by chemical quantitative, gas chromatography-olfactometry, and sensory analysis. J Food Sci 79:S92–S99
Symoneaux R, Guichard H, Le Quéré JM, Baron A, Chollet S (2015) Could cider aroma modify cider mouthfeel properties? Food Qual Prefer 45:11–17
Blanco-Gomis D, Exposito-Cimadevilla Y, Junco-Corujedo S, Gutierrez Alvarez MD (2003) Fractionation and characterization of soluble proteins from cider. Food Chem 83:507–513
Blanco-Gomis D, Mangas-Alonso JJ, Junco-Corujedo S, Gutierrez Alvarez MD (2007) Cider proteins and foam characteristics: a contribution to their characterization. J Agric Food Chem 55:2526–2531
Blanco D, Junco S, Exposito Y, Gutierrez MD (2004) Study of various treatments to isolate low levels of cider proteins to be analyzed by capillary sieving electrophoresis. J Liq Chromatogr Relat Technol 27:1523–1539
Le Bourse D, Jègou S, Conreux A, Villaume S, Jeandet P (2010) Review of preparative and analytical procedures for the study of proteins in grape juice and wine. Anal Chim Acta 667:33–42
Desportes C, Charpentier M, Duteurtre B, Maujean A, Duchiron F (2001) Isolation, identification, and organoleptic characterization of low-molecular-weight peptides from white wine. Am J Enol Vitic 52:376–380
Jones PR, Gawel R, Francis IL, Waters EJ (2008) The influence of interactions between major white wine components on the aroma, flavour and texture of model white wine. Food Qual Prefer 19:596–607
Fusi M, Mainente F, Rizzi C, Zoccatelli G, Simonato B (2010) Wine hazing: a predictive assay based on protein and glycoprotein independent recovery and quantification. Food Control 21:830–834
Siebert KJ (2006) Haze formation in beverages. LWT Food Sci Technol 39:987–994
Siebert KJ, Lynn PY (1997) Haze-active protein and polyphenols in apple juice assessed by turbidimetry. J Food Sci 62:79–84
Bamforth CW (1985) The foaming properties of beer. J Inst Brew 91:370–383
Depraetere SA, Delvaux F, Coghe S, Delvaux FR (2004) Wheat variety and barley malt properties: influence on haze intensity and foam stability of wheat beer. J Inst Brew 110:200–206
Osman AM, Coverdale SM, Onley-Watson K, Bell D, Healy P (2003) The gel filtration chromatographic-profiles of proteins and peptides of wort and beer: effects of processing—malting, mashing, kettle boiling, fermentation and filtering. J Inst Brew 109:41–50
Mills ENC, Sancho AI, Rigby NM, Jenkins JA, Mackie AR (2009) Impact of food processing on the structural and allergenic properties of food allergens. Mol Nutr Food Res 53:963–969
Pocock KF, Waters EJ (2006) Protein haze in bottled white wines: how well do stability tests and bentonite fining trials predict haze formation during storage and transport? Aust J Grape Wine Res 12:212–220
Barros A, Cosme F (2013) Allergenic proteins in foods and beverages. Food Technol Biotechnol 51:153–158
Vincenzi S, Mosconi S, Zoccatelli G, Dalla Pellegrina C, Veneri G, Chignola R, Peruffo A, Curioni A, Rizzi C (2005) Development of a new procedure for protein recovery and quantification in wine. Am J Enol Vitic 56:182–187
Smith MR, Penner MH, Bennett SE, Bakalinsky AT (2011) Quantitative colorimetric assay for total protein applied to the red wine pinot noir. J Agric Food Chem 59:6871–6876
Veneri G, Zoccatelli G, Mosconi S, Dalla Pellegrina C, Chignola R, Rizzi C (2006) A rapid method for the recovery, quantification and electrophoretic analysis of proteins from beer. J Inst Brew 112:25–27
Gazzola D, Vincenzi S, Pasini G, Lomolino G, Curioni A (2015) Advantages of the KDS/BCA assay over the bradford assay for protein quantification in white wine and grape juice. Am J Enol Vitic 66:227–233
Moreno-Arribas MV, Pueyo E, Polo MC (2002) Analytical methods for the characterization of proteins and peptides in wines. Anal Chim Acta 458:63–75
Jégou S, Conreux A, Villaume S, Hovasse A, Schaeffer C, Cilindre C, Van Dorsselaer A, Jeandet P (2009) One step purification of the grape vacuolar invertase. Anal Chim Acta 638:75–78
Moreno-Arribas MV, Cabello F, Polo MC, Martìn-Alvarez PJ, Pueyo E (1999) Assessment of the native electrophoretic analysis of total grape must proteins for the characterization of Vitis vinifera L. cultivars. J Agric Food Chem 47:114–120
Waters EJ, Wallace W, Williams PJ (1992) Identification of heat-unstable wine proteins and their resistance to peptidases. J Agric Food Chem 40:1514–1519
Fic E, Kedracka-Krok S, Jankowska U, Pirog A, Dziedzicka-Wasylewska M (2010) Comparison of protein precipitation methods for various rat brain structures prior to proteomic analysis. Electrophoresis 31:3573–3579
Carraro U, Rizzi C, Sandri M (1991) Effective recovery by KCl precipitation of highly diluted muscle proteins solubilized with sodium dodecyl sulfate. Electrophoresis 12:1005–1010
Mainente F, Simonato B, Zoccatelli G, Rizzi C (2011) A method for the preparative separation of beer proteins and glycocompounds. J Inst Brew 117:435–439
Marchal R, Seguin V, Maujean A (1997) Quantification of interferences in the direct measurement of proteins in wines from the Champagne region using the Bradford method. Am J Enol Vitic 48:303–309
Compton SJ, Jones CG (1985) Mechanism of dye response and interference in the Bradford protein assay. Anal Biochem 151:369–374
Ferreira RB, Picarra-Pereira MA, Monteiro S, Loureiro VB, Teixeira AR (2001) The wine proteins. Trends Food Sci Technol 12:230–239
Drilleau JF (1993) Cider processing: nitrogen and fermentation; phenol compounds and oxydation. Rev Pomme á cidre 33:24–25
Wall KM, Tait VM, Eastwell KC, Reid CA, Beveridge THJ (1996) Protein in varietally derived apple juices. J Agric Food Chem 44:3413–3415
Church FC, Swaisgood HE, Porter DH, Catignani GL (1983) Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J Dairy Sci 66:1219–1227
Fasoli E, Aldini G, Regazzoni L, Kravchuk AV, Citterio A, Righetti PG (2010) Les Maitres de l’Orge: the proteome content of your beer mug. J Proteome Res 9:5262–5269
Mainente F, Zoccatelli G, Lorenzini M, Cecconi D, Vincenzi S, Rizzi C, Simonato B (2014) Red wine proteins: two dimensional (2-D) electrophoresis and mass spectrometry analysis. Food Chem 164:413–417
Singleton VL, Rossi JA (1965) Colorimetry of total phenolics with phosphomolybdic-phosphotungstic acid reagents. Am J Enol Vitic 16:144–158
Patton WF (2006) Fluorescence detection of proteins in gels using SYPRO dyes. In: Perkin-Elmer LAS (ed) Cell biology, four volume set. Academic Press, Boston, USA
Thornton DJ, Carlstedt I, Sheehan JK (1996) Identification of glycoproteins on nitrocellulose membranes and gels. Mol Biotechnol 5:171–176
Dinnella C, Gargaro MT, Rossano R, Monteleone E (2002) Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein. Food Chem 78:363–368
Simonato B, Mainente F, Tolin S, Pasini G (2011) Immunochemical and mass spectrometry detection of residual proteins in gluten fined red wine. J Agric Food Chem 59:3101–3110
Tolin S, Pasini G, Simonato B, Mainente F, Arrigoni G (2012) Analysis of commercial wines by LC-MS/MS reveals the presence of residual milk and egg white allergens. Food Control 28:321–326
Tolin S, Pasini G, Curioni A, Arrigoni G, Masi A, Mainente F, Simonato B (2012) Mass spectrometry detection of egg proteins in red wines treated with egg white. Food Control 23:87–94
Walker JM (2002) The bicinchoninic acid (BCA) assay for protein quantitation. In: The protein protocols handbook. Humana Press, Totowa, USA
Waters EJ, Wallace W, Williams PJ (1991) Heat haze characteristics of fractionated wine proteins. Am J Enol Vitic 42:123–127
Toldrà F, Nollet LM (2012) Proteomics in foods: principles and applications. Springer Science & Business Media, New York
Garcia A, Wichers JH, Wichers HJ (2007) Decrease of the IgE-binding by Mal d 1, the major apple allergen, by means of polyphenol oxidase and peroxidase treatments. Food Chem 103:94–100
Rizzi C, Mainente F, Pasini G, Simonato B (2016) Hidden exogenous proteins in wine: problems, methods of detection and related legislation—a review. Czech J Food Sci 34:93–104
Acknowledgments
We thank L.M. di Maria Lucia Melchiori and C. s.n.c. and Maley s.r.l. for having kindly supplied cider samples.
Funding
This work was supported by University of Padova (Grant Number CPDA148173 and 60A08-1950/15).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
None.
Compliance with ethics requirements
This article does not contain any studies with human or animal subjects.
Electronic supplementary material
Below is the link to the electronic supplementary material.
Rights and permissions
About this article
Cite this article
Mainente, F., Rizzi, C., Zoccatelli, G. et al. Setup of a procedure for cider proteins recovery and quantification. Eur Food Res Technol 242, 1803–1811 (2016). https://doi.org/10.1007/s00217-016-2724-y
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00217-016-2724-y