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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3067Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.creator | Sanz, Yolanda | - |
| dc.creator | Toldrá Vilardell, Fidel | - |
| dc.date | 2008-02-25T10:40:28Z | - |
| dc.date | 2008-02-25T10:40:28Z | - |
| dc.date | 2001-04 | - |
| dc.date.accessioned | 2017-01-31T01:00:23Z | - |
| dc.date.available | 2017-01-31T01:00:23Z | - |
| dc.identifier | Applied and Environmental Microbiology 67 (4) : 1815-1820 (2001) | - |
| dc.identifier | http://hdl.handle.net/10261/3067 | - |
| dc.identifier.uri | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3067 | - |
| dc.description | 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,vith a subunit molecular mass of approximately 88 kDa, Optimal activity was shown at pH 7.5 and 55 degreesC. The enzyme was inhibited by serine proteinase inhibitors and several divalent cations (Cu2+, Hg2+, and Zn2+). 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 IJ M, respectively; those for Gly-Pro- and Ala-Pro-p-nitroanilide were 192 and 50 muM, 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. | - |
| dc.description | ALI97-0353 from CICYT (Spain) | - |
| dc.format | 513856 bytes | - |
| dc.format | 2459 bytes | - |
| dc.format | application/pdf | - |
| dc.format | text/plain | - |
| dc.language | eng | - |
| dc.publisher | American Society for Microbiology | - |
| dc.rights | closedAccess | - |
| dc.subject | X-prolyl-dipeptidyl peptidase | - |
| dc.subject | Lactobacillus sakei | - |
| dc.title | Purification and characterization of an X-prolyl-dipeptidyl peptidase from Lactobacillus sakei | - |
| dc.type | Artículo | - |
| Appears in Collections: | Digital Csic | |
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