DOI QR코드

DOI QR Code

Effect of Trichloroacetic Acid on the Solubility of Caseinomacropeptide

  • 발행 : 2002.03.01

초록

Crude caseinomacropeptide (CMP) was prepared from Na-caseinate using a commercial renneting enzyme. Most of the crude CMP was released from the Na-caseinate by hydrolyzing with the enzyme for 40 min. The hydrolysis of the k-casein with carbohydrate was slower than that of the k-casein without carbohydrate, as shown by the analyses of the sialic acid content and the tricine-SDS-polyacrylamide gel electrophoresis. The yield of crude CMP from Na-caseinate was 3.7%. Cation exchange chromatography showed that the crude CMP consisted of 40.5% CMP and 59.5% caseinogylcomacropetide (CGP). The effect of the TCA concentration on the solubility of CMP and CGP was determined by using crude CMP. The amounts of crude CMP and sialic acid decreased in the proportion to the increase of trichloroacetic acid (TCA) concentration from 2 to 12%, suggesting that the CGP containing carbohydrate, as well as the CMP having no carbohydrate, was precipitated in a range of 4 to 12%, depending on the TCA concentration. This result supports the hypothesis that the different non-glycosylated and glycosylated forms of CMP have different sensitivities to TCA precipitation.

키워드

참고문헌

  1. Int Dairy Journal v.6 Characteristic and potential uses of the caseinomacropeptide Abd EL Salam,M.H.;El Shibiny,S.;Buchheim,W. https://doi.org/10.1016/0958-6946(95)00026-7
  2. J Agric Bio Chem v.48 Bifidus growth-promoting activity of a glycomacropeptide derived from human k-casein Azuma,N.;Yamauch,K.;Mitsuoka,T.
  3. Biull Eksp Biol Med v.102 Amino acid composition and biological action of a peptide bioregulator from bovine k-casein Stan,C.Y.;Zhuravlev,B.V.
  4. Vopr Med Khim v.33 Peptidic bioregulator from bovine k-casein Stan,C.Y.;Elkimovskii,A.P.
  5. Biochem J v.271 Liberation of tryptic fragments from caseinomacropeptide of bovine k-casein involved in platelet function Leonil,J.;Molle,D.
  6. Eur J Biochem v.158 Analogy between fibrinogen and casein Jolle,P.;Levy Toledano,S.;Fiat,A.M.;Soria,C.;Gillessen,D.;Thomaidis,A.;Dunn,F.W.;Caen,J.P. https://doi.org/10.1111/j.1432-1033.1986.tb09764.x
  7. Eur Patent Appl EP Caseinoglycopeptides as dental plaque and dental caries inhibiting agents Neeser,J.R.
  8. Infec Immunity v.56 Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives Neeser,J.R.;Chambez,A.;Delvedova,S.;Prigent,M.I.;Guggenheim,B.
  9. J Agric Food Chem v.39 Bovine milk k-casein trypsin digest is a growth enhancer for the genus Bifidobacterium Poch,M.;Bezkorovainy,A. https://doi.org/10.1021/jf00001a013
  10. Biosci Biotech Biochem v.57 Inhibition by k-casein glycomacropeptide and lactoferrin of influenza virus haemagglutination Kawasaki,Y.;Isoda,H.;Shinmoto,H.;Tanimoto,M.;Dosaka,S.;Idora,T.;Nakajima,I. https://doi.org/10.1271/bbb.57.1214
  11. Igaku to seibutsugaku v.115 Effect of bovine k-casein on the growth of lactic acid bacteria Ito,O.;Kamato,S.;Yamano,W.;Yokojama,K.
  12. Le Lait v.73 Growth promoting activity of tryptic digest of caseinomacropeptide for Lactococcus lactis ssp. lactis Bouhallab,S.;Favrot,C.;Maubois,J.L. https://doi.org/10.1051/lait:199314
  13. Milchwissenschaft v.53 Immunomodificatory effect of dietary bovine k-caseinoglycopeptide on serum antibody levels and proliferative responses of lymphocytes in mice Monnai,M.;Horimoto,Y.;Otani,H.
  14. Biosci Biotech Biochem v.56 Large-scale preparation of k-casein glycomacropeptide from rennet casein whey Tanimoto,M.;Kawasaki,Y.;Dasako,S.;Ahiko,K.;Nakajima,I. https://doi.org/10.1271/bbb.56.140
  15. Milchwissenschaft v.51 Isolation of glycomacropeptide from sodium caseinate hydrolyzate solution by ultrafiltration Chu,L.;Macleod,A.;Ozimek,L.
  16. J Dairy Sci v.74 A new isolation method of caseinomacropeptide from sweet cheese whey Saito,T.;Yamaji,A.;Itoh,T. https://doi.org/10.3168/jds.S0022-0302(91)78463-4
  17. Milchwissenschaft v.47 Determination of k-casein glycomacropeptide by high performance liquid chroatography without trichloroacetic acid pretreatment Kawakami,H.;Kawakami,Y.;Dosako,S.;Tanimoto,M.;Nakajima,I.
  18. J Food Sci v.53 Fractionation and characterization of glycomacropeptide from caseinate and skim milk hydrolysates Morr,C.V.;Seo,A. https://doi.org/10.1111/j.1365-2621.1988.tb10182.x
  19. J Dairy Res v.58 A method for determination of macropeptide by cation-exchange fast protein liquid chromatography and its use for following the action of chymosin in milk Leonil,J.;Molle,D. https://doi.org/10.1017/S0022029900029897
  20. J Dairy Res v.63 Comparative study of methods for the isolation and purification of bovine k-casein and its hydrolysis by chymosin Coolbear,K.P.;Elgar,D.F.;Coolbear,T.;Ayers,J.S. https://doi.org/10.1017/S002202990003154X
  21. J Chromatogra A v.708 Heterogeneity of the bovine k-casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry Molle,D.;Leonil,J. https://doi.org/10.1016/0021-9673(95)00386-2
  22. Anal Biochem v.166 Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Schagger,H.;Von Jagow,G. https://doi.org/10.1016/0003-2697(87)90587-2
  23. J Biol Chem v.234 The thiobarbituric acid assay of sialic acids Warren,L.
  24. Milchwissenschaft v.510 A new method to estimate caseinomacropeptide and glycomacropeptide from trichloroacetic acid filtrate Lieske,B.;Konrad,G.

피인용 문헌

  1. Body weight reducing effects of crude caseinomacropeptide prepared from Na-caseinate vol.20, pp.3, 2011, https://doi.org/10.1007/s10068-011-0087-5