Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Functional and Film-forming Properties of Fractionated Barley Proteins

  • Cho, Seung-Yong (Institute of Life Sciences and Biotechnology, College of Life Sciences and Biotechnology, Korea University) ;
  • Rhee, Chul (Division of Food Bioscience and Technology, College of Life Sciences and Biotechnology, Korea University)
  • Published : 2009.08.31
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Abstract

Barley proteins are expected to have unique functional properties due to their high content of alcohol soluble protein, hordein. Since the barley proteins obtained by conventional isoelectric precipitation method cannot represent hordein fraction, barley proteins were fractionated to albumin, globulin, glutelin, and hordein with respect to extraction solvents. Functional properties and film-forming properties of solubility-fractionated barley proteins were investigated to explore their potential for human food ingredient and industrial usage. The 100 g of total barley protein comprised 5 g albumin, 23 g globulin, 45 g glutelin, and 27 g hordein. Water-binding capacities of barley protein isolates ranged from 140-183 mL water/100 g solid. Hordein showed the highest oil absorption capacity (136 mL oil/100 g), and glutelin showed the highest gelation property among the fractionated proteins. In general, the barley protein fractions formed brittle and weak films as indicated by low tensile strength (TS) and percent elongation at break (E) values. The salt-soluble globulin fraction produced film with the lowest TS value. Although films made from glutelin and hordein were dark-colored and had lower E values, they could be used as excellent barriers against water transmission.

Keywords

References

  1. Jadhav SJ, Lutz SE, Ghorpade VM, Salunkhe DK. Barley: Chemistry and value-added processing. Crit. Rev. Food Sci. 38: 123-171 (1998) https://doi.org/10.1080/10408699891274183
  2. MacGregor AW. Barley. p. 308. In: Encyclopaedia of Food Science, Food Technology, and Nutrition. Macrae R, Robinson RK, Sadler MJ (eds). Academic Press, New York, NY, USA (1993)
  3. Kim J-S, Kim Z-U. An extraction of barley protein and a comparison of the protein composition of some barleys. I. Extraction of barley protein. J. Korean Agric. Chem. Soc. 29: 51-56 (1986)
  4. Shewry PR, Franklin J, Parmar S, Smith SJ, Miflin BJ. The effects of sulfur starvation on the amino acid and protein compositions of barley-grain. J. Cereal Sci. 1: 21-31 (1983) https://doi.org/10.1016/S0733-5210(83)80005-8
  5. Howard KA, Gayler KR, Eagles HA, Halloran GM. The relationship between D hordein and malting quality in barley. J. Cereal Sci. 24: 47-53 (1996) https://doi.org/10.1006/jcrs.1996.0036
  6. Yal$\c{c}$in E, $\c{C}$elik S. Solubility properties of barley flour, protein isolates and hydrolysates. Food Chem. 104: 1641-1647 (2007) https://doi.org/10.1016/j.foodchem.2007.03.029
  7. Bilgi B, $\c{C}$elik S. Solubility and emulsifying properties of barley protein concentrate. Eur. Food Res. Technol. 218: 437-441 (2004) https://doi.org/10.1007/s00217-004-0895-4
  8. Mohamed A, Hojilla-Evangelista MP, Peterson SC, Biresaw G Barley protein isolate: Thermal, functional, rheological, and surface properties. J. Am. Oil Chem. Soc. 84: 281-288 (2007) https://doi.org/10.1007/s11746-006-1027-z
  9. Gennadios A, Weller CL. Edible films and coatings from wheat and corn proteins. Food Technol.-Chicago 44: 63-69 (1990)
  10. Eswaranandam S, Hettiarachchy NS, Johnson MG. Antimicrobial activity of citric, lactic, malic, or tartaric acids and nisinincorporated soy protein film against Listeria monocytogenes, Escherichia coli O157:H7, and Salmonella gaminara. J. Food Sci. 69: FMS79-FMS84 (2004) https://doi.org/10.1111/j.1365-2621.2004.tb13375.x
  11. Kim KM, Lee BY, Kim YT, Choi SG, Lee J, Cho SY, Choi WS. Development of antimicrobial edible film incorporated with green tea extract. Food Sci. Biotechnol. 15: 478-481 (2006)
  12. Pruneda E, Peralta-Hernandez JM, Esquivel K, Lee SY, Godinez LA, Mendoza S. Water vapor permeability, mechanical properties, and antioxidant effect of Mexican oregano-soy based edible films. J. Food Sci. 73: C488-C493 (2008) https://doi.org/10.1111/j.1750-3841.2008.00843.x
  13. Herald TJ, Hachmeister KA, Huang S, Bowers JR. Corn zein packaging materials for cooked turkey. J. Food Sci. 61: 415-418 (1996) https://doi.org/10.1111/j.1365-2621.1996.tb14206.x
  14. Wu Y, Rhim JW, Weller CL, Hamouz F, Cuppett S, Schnepf M. Moisture loss and lipid oxidation for precooked beef patties stored in edible coatings and films. J. Food Sci. 65: 300-304 (2000) https://doi.org/10.1111/j.1365-2621.2000.tb15997.x
  15. Cho SY, Park JW, Rhee C. Edible films from protein concentrates of rice wine meal. Korean J. Food Sci. Technol. 30: 1097-1106 (1999)
  16. Lai H-M, Padua GW. Water vapor barrier properties of zein films plasticized with oleic acid. Cereal Chem. 75: 194-199 (1998) https://doi.org/10.1094/CCHEM.1998.75.2.194
  17. Wang Y, Padua GW. Tensile properties of extruded zein sheets and extrusion blown films. Macromol. Mater. Eng. 288: 886-893 (2003) https://doi.org/10.1002/mame.200300069
  18. AOAC. Official Methods of Analysis of AOAC International. $17^{th}$ ed. Method 979.09. AOAC International, Gaithersburg, MD, USA (2000)
  19. Bae SH, Rhee C. Influences of extraction pH on the functionality of soybean protein isolate. Korean J. Food Sci. Technol. 30: 557-561 (1998)
  20. Beuchat LR. Functional and electroporetic characteristics of succinylated peanut flour protein. J. Agr. Food Chem. 25: 258-292 (1977) https://doi.org/10.1021/jf60210a044
  21. Lawal OS. Functionality of African locust bean (Parkia biglobossa) protein isolate: Effects of pH, ionic strength, and various protein concentrations. Food Chem. 86: 345-355 (2004) https://doi.org/10.1016/j.foodchem.2003.09.036
  22. ASTM. Standard test methods for tensile properties of thin plastic sheeting (D 882-01). pp. 162-170. In: Annual Book of ASTM Standards. 08.01. American Society for Testing and Materials, Philadelphia, PA, USA (2002)
  23. ASTM. Standard test methods for water vapor transmission of materials (E 96-00). pp. 1048-1053. In: Annual Book of ASTM Standards. 15.09. American Society for Testing and Materials, Philadelphia, PA, USA (2002)
  24. McHugh TH, Avena-Bustillos R, Krochta JM. Hydrophilic edible films: Modified procedure for water vapor permeability and explanation of thickness effects. J. Food Sci. 58: 899-903 (1993) https://doi.org/10.1111/j.1365-2621.1993.tb09387.x
  25. L$\'{a}$sztity R. The Chemistry of Cereal Proteins. $2^{nd}$ ed. CRC Press, Inc., Boca Raton, FL, USA. pp. 143-159 (1996)
  26. Kirkman MA, Shewry PR, Miflin BJ. The effect of nitrogen nutrition on the lysine content and protein composition of barley seeds. J. Sci. Food Agr. 33: 115-127 (1982) https://doi.org/10.1002/jsfa.2740330203
  27. Qi JC, Zhang GP, Zhou MX. Protein and hordein content in barley seeds as affected by nitrogen level and their relationship to betaamylase activity. J. Cereal Sci. 43: 102-107 (2006) https://doi.org/10.1016/j.jcs.2005.08.005
  28. Chavan UD, McKenzie DB, Shahidi F. Functional properties of protein isolates from beach pea (Lathyrus maritimus L.). Food Chem. 74: 177-187 (2001) https://doi.org/10.1016/S0308-8146(01)00123-6
  29. Mwasaru MA, Muhammad K, Bakar J, Man YBC. Effects of isolation technique and conditions on the extractability, physicochemical and functional properties of pigeonpea (Cajanus cajan) and cowpea (Vigna unguiculata) protein isolates. I. Physicochemical properties. Food Chem. 67: 435-443 (1999) https://doi.org/10.1016/S0308-8146(99)00150-8
  30. Lin CS, Zayas JF. Functionality of defatted corn germ proteins in a model system: Fat binding capacity and water retention. J. Food Sci. 52: 1308-1311 (1987) https://doi.org/10.1111/j.1365-2621.1987.tb14070.x
  31. Brandt A. Endosperm protein formation during kernel development of wild type and high-lysine barley mutant. Cereal Chem. 53: 890-901 (1976)
  32. Subirade M, Kelly I, Gueguen J, Pezolet M. Molecular basis of film formation from a soybean protein: Comparison between the conformation of glycinin in aqueous solution and in films. Int. J. Biol. Macromol. 23: 241-249 (1998) https://doi.org/10.1016/S0141-8130(98)00052-X
  33. Park SK, Rhee CO, Bae DH, Hettiarachchy NS. Mechanical properties and water-vapor permeability of soy-protein films affected by calcium salts and glucono-delta-lactone. J. Agr. Food Chem. 49: 2308-2312 (2001) https://doi.org/10.1021/jf0007479