Sanz_2001_Appl.Environ.Microbiol_67_1815

Reference

Title : Purification and characterization of an X-prolyl-dipeptidyl peptidase from Lactobacillus sakei - Sanz_2001_Appl.Environ.Microbiol_67_1815
Author(s) : Sanz Y , Toldra F
Ref : Applied Environmental Microbiology , 67 :1815 , 2001
Abstract :

An X-prolyl-dipeptidyl peptidase has been purified from Lactobacillus sakei by ammonium sulfate fractionation and five chromatographic steps, which included hydrophobic interaction, anion-exchange chromatography, and gel filtration chromatography. This procedure resulted in a recovery yield of 7% and an increase in specificity of 737-fold. The enzyme appeared to be a dimer with a subunit molecular mass of approximately 88 kDa. Optimal activity was shown at pH 7.5 and 55 degrees C. The enzyme was inhibited by serine proteinase inhibitors and several divalent cations (Cu(2+), Hg(2+), and Zn(2+)). The enzyme almost exclusively hydrolyzed X-Pro from the N terminus of each peptide as well as fluorescent and colorimetric substrates; it also hydrolyzed X-Ala at the N terminus, albeit at lower rates. K(m) s for Gly-Pro- and Lys-Ala-7-amido-4-methylcoumarin were 29 and 88 microM, respectively; those for Gly-Pro- and Ala-Pro-p-nitroanilide were 192 and 50 microM, respectively. Among peptides, beta-casomorphin 1-3 was hydrolyzed at the highest rates, while the relative hydrolysis of the other tested peptides was only 1 to 12%. The potential role of the purified enzyme in the proteolytic pathway by catalyzing the hydrolysis of peptide bonds involving proline is discussed.

PubMedSearch : Sanz_2001_Appl.Environ.Microbiol_67_1815
PubMedID: 11282638

Related information

Citations formats

Sanz Y, Toldra F (2001)
Purification and characterization of an X-prolyl-dipeptidyl peptidase from Lactobacillus sakei
Applied Environmental Microbiology 67 :1815

Sanz Y, Toldra F (2001)
Applied Environmental Microbiology 67 :1815