Electronic Journal of Polish Agricultural Universities (EJPAU) founded by all Polish Agriculture Universities presents original papers and review articles relevant to all aspects of agricultural sciences. It is target for persons working both in science and industry,regulatory agencies or teaching in agricultural sector. Covered by IFIS Publishing (Food Science and Technology Abstracts), ELSEVIER Science - Food Science and Technology Program, CAS USA (Chemical Abstracts), CABI Publishing UK and ALPSP (Association of Learned and Professional Society Publisher - full membership). Presented in the Master List of Thomson ISI.

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Stepaniak L. 1999. PURIFICATION AND CHARACTERIZATION OF PROLINE-SPECIFIC PEPTIDASES FROM LACTOCOCCUS AND LACTOBACILLUS, EJPAU 2/issue2/volume2(2), #05.
Available Online: http://www.ejpau.media.pl/volume2/issue2/volume2/issue2/food/abs-05.html

ABSTRACT

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.

Key words: lactococcus, lactobacillus, proline, enzymes..

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