Warianty tytułu
Języki publikacji
Abstrakty
Purified proline-specific amino peptidases from Lactobacillus curvatus and from Lactococcus lactis were active on both X-proline dipeptidyl aminopeptidase (PepX) substrates, Gly-Pro-AMC or Gly-PropNA and on proline endopepetidase (PEP) substrates Suc-Gly-Pro-Leu-Gly-Pro, Suc-Gly-Pro-AMC, Z-Gly-Pro-AMC or Suc-Gly-Pro-pNA, however; activity on PEP substrates was markedly less than that on PepX substrates. The enzymes from Lactobacillus and Lactococcus hydrolyzed a number of oligopeptides containing 7-11 amino acids residues and proline at the penultimate position from N-terminus, but hydrolysis of natural PEP oligopeptide substrates containing proline residues at internal positions was negligible. The two proline-specific enzymes were strongly stimulated by NaCl and inhibited by phenylmethylsulfonyl fluoride and organic solvents.
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Opis fizyczny
http://www.ejpau.media.pl/series/volume2/issue2/food/art-05.html
Twórcy
autor
- Agricultural University of Norway, 1432 Aas, Norway
Bibliografia
- Augustyns, K., Borloo, M., Belyaev, A., Rajan, P., Goosens, F., Hendriks, D., Sharpe, S., Haemers, A. 1995. Bioorganic & Medical Chem. Lett., 5:1265-1270.
- Habibi-Najafi, M.B., Lee, H.B. 1994. J. Dairy Sci., 77:385-392.
- Law., J., Haandrikman, A. 1997. Int.Dairy J. 7:1-11
- Lee Wong A.C.. 1998. J. Dairy Sci., 81, 2765-2770
- Park, S.Y., Gibs, B.F., Lee, B.H. 1995. Food Res. Intern., 28:43-49.
- Polgár, L. 1994. Methods in Enzymol., 244:188-200.
- Steinmetzer, T., Silberring, J., Mrestani-Klaus, C., Fittakau, S., Barth, A., Demuth, H.U. 1993. J. Enzyme Inhibition, 7:77-85
- Stepaniak, L. 2000. Nahrung/Food, 44(2) In press.
- Stepaniak, L., Gobbetti, M., Pripp, A.H., Sorhaug, T.1995. Ital. J. Food Sci., 5:699-713.
- 10.Virgilli, R., Schivazappa, C., Parolari, G., Bordini, C.S.,Degni, M. 1998. J. Food Biochem., 22:53-64.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-725208b3-1daf-4670-987a-c1128731f774