Journal of the Korean Society of Food Science and Nutrition (한국식품영양과학회지)

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
권호 표지

Effect of Deamidation with Neutrase on the Solubility of BSA, Egg Albumin, and Soy Protein Isolate

BSA, Egg Albumin, 분리대두단백질의 용해도에 미치는 Neutrase에 의한 탈아미드 효과

  • 강영주 (제주대학교 식품공학과) ;
  • 김효선 (제주대학교 식품공학과)
  • Published : 1995.10.01
Download PDF
⟨ Previous Next ⟩

Abstract

Effect of deamidation with Neutrase on the solubility of bovin serum albumin(BSA), egg albumin(EA), soy protein isolate(SPI) was investigated. Solubility of deamidated BSA in distilled water was decreased from 98% to 83% against native BSA at pH 4~8, minimum solubility of deamidated BSA was pH 6. Solubilities of native BSA and deamidated BSA in 0.2M NaCl solution were shown 100% as compared greately decreasing both solubilities in 1.0M NaCl at acidic pH. According to deamidation, solubility of EA in distilled water was increased below pH 4 and above pH 6, while solubility of EA in NaCl solution was decreased by deamidation at acidic pH. Solubility of SPI in distilled water was greately increased by deamidation at overall pH, deamidation was increased solubility in NaCl solution above pH 5. There was, however, no difference on solubility by deamidation below pH 5.

BSA, egg albumin (EA), 그리고 분리대두단백질(SPI)의 Neutrase에 의한 탈아미드화가 용해도에 미치는 영향을 조사하여 보았다. BSA는 탈아미드화로 pH 4~8 사이의 물에 대한 용해도가 천연 BSA에 비하여 98~83%로 감소하였으며, pH 6 부근에서 가장 낮은 용해도를 보았다. 천연 BSA와 탈아미드화된 BSA 모두 0.2M NaCl 용액에서는 100%의 용해도를 보였으나, 산성 1.0M NaCl용액에서는 용해도가 모두 크게 떨어졌다. EA의 용해도는 탈아미드화로 pH3 이하와 6 이상의 수용액에서는 증가하였으나, 산성 NaCl용액에서는 크게 감소하였다. SPI는 탈아미드화로 수용액에서의 용해도가 모든 pH 범위에서 크게 증가하였으나, NaCl용액에 대한 용해도는 pH 6 이상에서는 증가하였고, pH 5 이하에서는 변화가 없었다.

Keywords

References

  1. Food Proteins Relationships between structure and functional properties of food proteins Kinsella,J.E.;Fox,P.F.(ed.);Cordon,J.J.(ed.)
  2. J. Protein Chem. v.7 Effect of oxidative sulfitolysis of disulfitolysis of disulfide bonds of bovine serum albumin on its structural properties:A physicochemical study Kella,N.K.D.;Kang,Y.J.;Kinsella,J.E.
  3. New Protein Foods Physicochemical and functional properties of oil seed proteins with emphasis on soy protein Kinsella,J.E.;Damodaram,S.;German,B.
  4. J. Food Sci. v.53 Physicochemical and functional properties of winged bean flour and isolate compared with soy isolate Okezie,B.O.;Bello,A.B.
  5. J. Agric. Food Chem. v.39 Effects of deamidation with chymotrypsin at pH 10 on the functional properties of proteins Kato,A.;Tanaka,A.;Lee,Y.;Matsudomi,N.;Kobayashi,K.
  6. Agric. Biol. Chem. v.46 Comformation and surface properties of deamidation gluten Matsudomi,N.;Kato,A.;Kobayashi,K.
  7. J. Food Sci. v.56 Effect of anions on the deamidation of soy protein Shih,F.F.
  8. J. Agric. Food Chem. v.39 Deamidation of food proteins by protease in alkaline pH. Kato,A.;Tanaka,A.;Matsudomi,N.;Kobayashi,K.
  9. Meth. Enzymol. v.11 Detemination of amide residue by chemical methods Wilcox,R.E.
  10. Adverces in protein chemistry v.37 Serum albumin Peter,T.Jr.
  11. J. Food Sci. v.52 Functional properties of deamidated oat protein isolates Ma,C.;Khanzada,G.
  12. J. Agric. Food Chem. v.37 Effect of disulfide bonds cleavage on structural and interfacial properties of whey proteins Kella,N.K.D.;Yang,S.T.;Kinsella,J.E.
  13. J. Agric. Food Chem. v.41 Functional properties of the total proteins of sunflower(Helianthus annuus L.) Venktesh,A.;Prakash,V.
  14. J. Food Sci. v.54 Preparation and functional properties of enzymatically deamidated soy protein Hamada,J.S.;Marshell,W.E.
  15. J. Food Sci. v.54 Deamidation and functional properties of food proteins by the teatment with immobilized chymotrypsin at alkaline pH Kato,A.;Lee,Y.;Kobayashi,K.
  16. Kor. J. Food Sci. Tech. v.19 Enzymatic modification of soy proteins:effect of functional properties of soy isolate upon proteolytic hydrolysis Kang,Y.J.
  17. Protein Functionality in Foods;ACS Syposium series 147 Solubility and viscosity Shen,J.L.;Cherry,J.P.(ed.)