Abstract
Successful utilization of commercial zein products for certain food, pharmaceutical, cosmetic and medical applications requires a decolorized/deodorized zein of high purity that can be achieved by column filtration of commercial yellow zein solutions through Zeolite 5A and activated carbon. The objective of this investigation was to devise a combination of methodologies to assess purity and degree of deodorization and decolorization. Off-odor removal is defined by a UV spectroscopic ratio of 280:325 nm where diferuloylputrescine is the major contributor. Removal of yellow color, attributed to xanthophylls in zein, was followed by visible spectroscopic assays of a series of dilutions at 448 nm. SDS-PAGE analysis demonstrated removal of β-zein in combination with diminished sulfur content by sulfur analysis. Zein purity was assessed by Dumas nitrogen and FTIR of commercial zein before and after column filtration. Spectral differences were observed in the amide I (1,650 cm−1) peak, amide II region (1,530 and 1,550 cm−1) and the amide III peak at 1,240 cm−1, where ratio of the dominant peaks were strongly dependent on purity of sample. Circular dichroism (CD) analyses validated the FTIR results by showing increased α-helical content for the column purified zeins. Combinations of these methodologies can be used to define zein products as a quality control measure for a commercial operation.
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References
Esen A (1986) Separation of alcohol-soluble proteins (zeins) from maize into three fractions by differential solubility. Plant Physiol 80:623–627
Padua GW, Wang Q (2002) Formation and properties of corn zein films and coatings. In: Gennadios A (ed) Protein based films and coatings. CRC Press, Florida, pp 43–67
Parris N, Dickey L (2003) Adhesive properties of corn zein formulation on glass surfaces. J Agric Food Chem 51:3892–3894
Sessa DJ, Mohamed A, Byars JA (2008) Chemistry and physical properties of melt-processed and solution-cross-linked corn zein. J Agric Food Chem 56:7067–7075
Sessa DJ, Eller FJ, Palmquist DE, Lawton JW (2003) Improved methods for decolorizing corn zein. Ind Crops Prod 18:55–65
Sessa DJ, Palmquist DE (2008) Effect of heat on the adsorption capacity of an activated carbon for decolorizing/deodorizing yellow zein. Bioresource Technol 99:6360–6364
Sessa DJ, Palmquist DE (2009) Decolorization/deodorization of zein via activated carbons and molecular sieves. Ind Crops Prod 30:162–164
Sessa DJ (2008) Decolorization/deodorization of corn zein products. US Patent Application 20080242842
Kelly SM, Price NC (2000) The use of circular dichroism in the investigation of protein structure and function. Current Protein Peptide Sci 1:349–384
Tatham AS, Field JM, Morris VJ, I’Anson KJ, Cardle L, Dufton MJ, Shewry PR (1993) Solution conformational analysis of the α-zein proteins of maize. J. Biol. Chem 268:26253–26259
Forato LA, Bicudo T, Colnago LA (2003) Conformation of α zeins in solid state by Fourier transform IR. Biopolymers Biospectrosc Section 72:421–426
Bugs MR, Forato LA, Bortoleto-Bugs RK, Fischer H, Mascarenhas YP, Ward RJ, Colnago LA (2004) Spectroscopic characterization and structural modeling of prolamine from maize and pear millet. Eur Biophys J 33:335–343
Barth A (2007) Infrared spectroscopy of proteins. Biochim Biophys Acta 1767:1073–1101
Kretschmer CB (1957) Infrared spectroscopy and optical rotary dispersion of zein, wheat gluten and gliadin. J Phys Chem 61:1627–1631
Forato LA, Bernardes-Filho R, Colnago LA (1998) Protein structure in KBr pellets by infrared spectroscopy. Anal Biochem 259:136–141
Goormaghtigh E, Cabiaux V, Ruysschaert J-M (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures. Subcell Biochem 23:405–450
Silverstein RM, Bassler GC, Morill TC (1981) Infrared spectrometry. Spectrometric identification of organic compounds, 4th edn. Wiley, New York, pp 124–126
Anderle G, Mendelsohn R (1987) Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region. Biophys J 52:69–74
Kaiden K, Matsui T, Tanaka S (1987) Study of the amide III band by FTIR spectrometry of the secondary structure of albumin, myoglobin, and gamma-globulin. Appl Spectrosc 41:180–184
Cai S, Singh BR (1999) Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins. Biophys Chem 80:7–20
Selling GW, Hamaker SAH, Sessa DJ (2007) Effect of solvent and temperature on secondary and tertiary structure of zein by circular dichroism. Cereal Chem 84:27–265
Cabra V, Vazquez-Contreres E, Moreno A, Arrequin-Espinosa R (2008) The effect of sulfhydryl groups and disulphide linkage in the thermal aggregation of Z19 α-zein. Biochim Biophys Acta Proteins Proteomics 1784:1028–1036
Cabra V, Arrequin R, Galvez A, Quirasco M, Vazquez-Duhalt R, Farres A (2005) Characterization of a 19 kDa α-zein of high purity. J Agric Food Chem 53:725–729
Sreerama N, Woody RW (2004) Computation and analysis of protein circular dichroism spectra. Meth Enzymol 383:318–351
Acknowledgments
We thank Global Protein Products, Waterville, ME and Biotechnology Research and Development Corporation, Peoria, IL for funding this research commencing 07/01/2008 to completion date 06/30/2010.
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Names are necessary to report factually on available data; however, the USDA neither guarantees nor warrants the standard of the product and the use of the name by the USDA implies no approval of the product to the exclusion of others that may also be suitable.
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Sessa, D.J., Woods, K.K. Purity Assessment of Commercial Zein Products After Purification. J Am Oil Chem Soc 88, 1037–1043 (2011). https://doi.org/10.1007/s11746-011-1765-4
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DOI: https://doi.org/10.1007/s11746-011-1765-4