DOI QR코드

DOI QR Code

Effects of pH, Electrolyte Concentrations, and Alginate Molecular Weights on Surface Hydrophobicity of Soy Protein Isolates

pH, 전해질의 농도 및 알긴산 분자량이 분리콩단백질의 표면소수성에 미치는 영향

  • Lim, Yeong-Seon (Department of Food and Nutrition, Gangnung-Wonju National University) ;
  • Yoo, Byung-Jin (Department of Food and Nutrition, Gangnung-Wonju National University)
  • 임영선 (강릉원주대학교 식품영양학과) ;
  • 유병진 (강릉원주대학교 식품영양학과)
  • Received : 2016.05.16
  • Accepted : 2016.07.20
  • Published : 2016.09.30

Abstract

Changes in surface hydrophobicity of soy protein isolate (SPI), which plays an important role in the functional characteristics of protein, were measured according to various SPI concentrations, pH levels, electrolytes concentrations, and alginate molecular weights by using 1-anilino-8-naphthalene sulfonic acid as a fluorescent probe. SPI surface hydrophobicity decreased as SPI concentrations increased. SPI surface hydrophobicity reached a maximum at pH 7.0. SPI surface hydrophobicity rapidly increased as the NaCl concentration of SPI solution increased up to 100 mM, and showed no large increases above 100 mM. However, SPI surface hydrophobicity radically decreased until the $CaCl_2$ concentration reached 50 mM and revealed no large variations above 50 mM. A similar trend was exhibited in the case of $MgCl_2$. As both the concentration and molecular weight of sodium alginate increased, SPI surface hydrophobicity decreased. The increasing rate of SPI surface hydrophobicity decreased as the molecular weight of sodium alginate increased.

분리콩단백질(SPI, soy protein isolate) 농도, pH, 전해질의 종류와 농도, alginates의 농도와 분자량이 SPI의 표면소수성에 미치는 영향을 조사한 결과는 다음과 같다. SPI 농도가 증가할수록 표면소수성은 감소하였다. SPI의 표면소수성이 pH 7.0에서 최대값을 나타내었다가 pH가 7.0을 기준으로 증가 혹은 감소함에 따라 표면소수성이 감소하는 경향을 나타내었다. SPI의 표면소수성은 NaCl의 농도가 100 mM까지 증가함에 따라 급격히 증가하지만 더 이상의 농도에서는 변화가 없었다. $CaCl_2$$MgCl_2$의 농도가 각각 50 mM과 30 mM까지 증가할수록 SPI의 표면소수성이 급격히 감소하였지만, 그 이상의 농도에서는 큰 변화가 없었다. Na-alginate의 농도와 분자량의 증가함에 따라 SPI의 표면소수성이 감소한 것으로 나타났다. Na-alginate의 분자량이 증가함에 따라 표면소수성의 증가속도가 감소하였다.

Keywords

References

  1. Damodaran S. 1996. Amino acids, peptides, and proteins. In Food Chemistry. Fennema OR, ed. Marcel Dekker, New York, NY, USA. p 321-429.
  2. Galazka VB, Smith D, Ledward DA, Dickinson E. 1999. Complexes of bovine serum albumin with sulphated polysaccharides: effects of pH, ionic strength and high pressure treatment. Food Chem 64: 303-310. https://doi.org/10.1016/S0308-8146(98)00104-6
  3. Thomas WR. 1992. Carrageenan. In Thickening and Gelling Agents for Food. Imeson A, ed. Blackie Academic and Professional, Cambridge, MA, USA. p 24-39.
  4. Drohan DD, Tziboula A, McNulty D, Horne DS. 1977. Milk protein-carrageenan interactions. Food Hydrocolloids 11: 101-107.
  5. Frederick FS. 1994. Interaction of soy isolate with polysaccharide and its effect on film properties. J Am Oil Chem Soc 71: 1281-1285. https://doi.org/10.1007/BF02540552
  6. Noh BS, Kim SS, Jang PS, Lee HG, Park WJ, Song GB, Lee HS, LEE SB, Hwang GT. 2011. Processing soybean. In Food Processing & Preservation. 2nd ed. Suhaksa Publishing Company Inc., Seoul, Korea. p 245-270.
  7. Gennadios A, Brandenburg AH, Weller CL, Testin RF. 1993. Effect of pH on properties of wheat gluten and soy protein isolate films. J Agric Food Chem 41: 1835-1839. https://doi.org/10.1021/jf00035a006
  8. Campbell LJ, Gu X, Dewar SJ, Euston SR. 2009. Effects of heat treatment and glucono-${\delta}$-lactone-induced acidification on characteristics of soy protein isolate. Food Hydrocolloids 23: 344-351. https://doi.org/10.1016/j.foodhyd.2008.03.004
  9. Hayakawa S, Nakai S. 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J Food Sci 50: 486-491.
  10. Hua Y, Cui SW, Wang Q, Mine Y, Poysa V. 2005. Heat induced gelling properties of soy protein isolates prepared from different defatted soybean flours. Food Res Int 38: 377-385. https://doi.org/10.1016/j.foodres.2004.10.006
  11. Dickinson E, Stainsby G. 1988. Emulsion stability. In Advances in Food Emulsions and Foams. Dickinson E, Stainsby E, eds. Elsevier Applied Science, Cambridge, MA, USA. p 1-44.
  12. Nakai S. 1983. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J Agric Food Chem 31: 676-683. https://doi.org/10.1021/jf00118a001
  13. Harwalker VR, Ma CY. 1989. Effects of medium composition, preheating, and chemical modification upon thermal behaviour of oat globulin and ${\beta}$-lactoglobulin. In Food Proteins. Kinsella JF, Soucie WG, eds. American Oil Chemists' Society, Champaign, IL, USA. p 210-251.
  14. Koning MMG, Visser H. 1992. Protein interactions. An overview. In Protein interaction. Visser H, ed. VCH Publishers, New York, NY, USA. p 1-24.
  15. Bonomi F, Mora G, Pagani MA, Iametti S. 2004. Probing structural features of water-insoluble proteins by front-face fluorescence. Anal Biochem 329: 104-111. https://doi.org/10.1016/j.ab.2004.02.016
  16. Chapman VJ, Chapman DJ. 1980. Algin and alginate. In Seaweeds and Their Uses. Chapman and Hall, New York, NY, USA. p 194-225.
  17. You BJ, Im YS, Jeong IH, Lee KH. 1997. Effect extraction conditions on bile acids binding capacity in vitro of alginate extracted from sea tangle (Laminaria spp.). J Korean Fish Soc 30: 31-38.
  18. You BJ, Lim YS, Ryu HS. 2004. Effects of hot water treatment and dialysis on measuring the average molecular weight of alginates. J Kor Fish Soc 37: 1-6.
  19. Lim YS, You BJ. 2006. Effects of hydrolysis pH on distribution of molecular weights of alginates of sea tangle Laminaria japonica. J Kor Fish Soc 39: 313-317.
  20. Meloan CE, Pomeranz Y. 1973. Food analysis laboratory experiments. The Avi Publishing Company Inc., Westport, CT, USA. p 79-110.
  21. Somogyi M. 1952. Notes on sugar determination. J Biol Chem 195: 19-23.
  22. Hirst EL, Percival E, Wold JK. 1964. The structure of alginic acid. Part IV. Partial hydrolysis of the reduced polysaccharide. J Chem Soc 8: 1493-1499.
  23. Kato A, Nakai S. 1980. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim Biophys Acta 624: 13-20. https://doi.org/10.1016/0005-2795(80)90220-2
  24. SPSS. 2004. SPSS base 12.0 for window. SPSS Inc., Chicago, IL, USA.
  25. Lim YS, You BJ. 2007. Effects of hydrolysis temperature on the distribution of the molecular weights of alginates prepared from sea tangle, Laminaria japonica. J Kor Fish Soc 40: 187-192.
  26. Winnik FM. 1993. Photophysics of preassociated pyrenes in aqueous polymer solutions and in other organized media. Chem Rev 93: 587-614. https://doi.org/10.1021/cr00018a001
  27. Li-Chan E, Nakai S, Wood DF. 1984. Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties. J Food Sci 49: 345-350. https://doi.org/10.1111/j.1365-2621.1984.tb12418.x
  28. Voutsinas LP, Cheung E, Nakai S. 1983. Relationships of hydrophobicity to emulsifying properties of heat denatured proteins. J Food Sci 49: 26-32.
  29. Kundu B, Guptasarma P. 2002. Use of a hydrophobic dye to indirectly probe the structural organization and conformational plasticity of molecules in amorphous aggregates of carbonic anhydrase. Biochem Biophys Res Commun 293: 572-577. https://doi.org/10.1016/S0006-291X(02)00257-7
  30. Wolf WJ. 1970. Soybean proteins: their functional, chemical, and physical properties. J Agric Food Chem 18: 969-976. https://doi.org/10.1021/jf60172a025
  31. Chan MYY, Bell DJ, Dunnil P. 1982. The relationship between the zeta potential and the size of soya protein acid precipitate particles. Biotechnol Bioeng 24: 1897-1990. https://doi.org/10.1002/bit.260240817
  32. Uruakpa FO, Arntfield SD. 2006. Surface hydrophobicity of commercial canola proteins mixed with ${\kappa}$-carrageenan or guar gum. Food Chem 95: 255-263. https://doi.org/10.1016/j.foodchem.2005.01.030
  33. Goddard ED. 1986. Polymer-surfactant interaction part II. Polymer and surfactant of opposite charge. Colloids Surf 19: 301-329. https://doi.org/10.1016/0166-6622(86)80341-9
  34. Ren B, Gao Y, Lu L, Liu X, Tong Z. 2006. Aggregates of alginates binding with surfactants of single and twin alkyl chains in aqueous solutions: Fluorescence and dynamic light scattering studies. Carbohydr Polym 66: 266-273. https://doi.org/10.1016/j.carbpol.2006.03.012
  35. Fioramonti SA, Perez AA, Aringoli EE, Rubiolo AC, Santiago LG. 2014. Design and characterization of soluble biopolymer complexes produced by electrostatic self-assembly of a whey protein isolate and sodium alginate. Food Hydrocolloids 35: 129-136. https://doi.org/10.1016/j.foodhyd.2013.05.001

Cited by

  1. 글루텐의 표면소수성에 미치는 전해질, pH 및 다시마(Sacchrina japonicas) 알긴산나트륨의 분자량의 영향 vol.54, pp.4, 2016, https://doi.org/10.5657/kfas.2021.0543