| dc.contributor.author |
Anastasiou, R |
en |
| dc.contributor.author |
Papadelli, M |
en |
| dc.contributor.author |
Georgalaki, MD |
en |
| dc.contributor.author |
Kalantzopoulos, G |
en |
| dc.contributor.author |
Tsakalidou, E |
en |
| dc.date.accessioned |
2014-06-06T06:45:00Z |
|
| dc.date.available |
2014-06-06T06:45:00Z |
|
| dc.date.issued |
2002 |
en |
| dc.identifier.issn |
13645072 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1046/j.1365-2672.2002.01659.x |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/2202 |
|
| dc.subject.other |
amino acid |
en |
| dc.subject.other |
aminopeptidase |
en |
| dc.subject.other |
nucleotide |
en |
| dc.subject.other |
serine |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
x prolyldipeptidylaminopeptidase |
en |
| dc.subject.other |
gene |
en |
| dc.subject.other |
amino acid sequence |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
bacterial strain |
en |
| dc.subject.other |
calculation |
en |
| dc.subject.other |
cheese ripening |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
DNA template |
en |
| dc.subject.other |
enzyme active site |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
enzyme purification |
en |
| dc.subject.other |
enzyme structure |
en |
| dc.subject.other |
gel filtration |
en |
| dc.subject.other |
lactic acid bacterium |
en |
| dc.subject.other |
molecular cloning |
en |
| dc.subject.other |
molecular weight |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
nucleotide sequence |
en |
| dc.subject.other |
open reading frame |
en |
| dc.subject.other |
polyacrylamide gel electrophoresis |
en |
| dc.subject.other |
polymerase chain reaction |
en |
| dc.subject.other |
protein degradation |
en |
| dc.subject.other |
protein family |
en |
| dc.subject.other |
protein motif |
en |
| dc.subject.other |
sequence analysis |
en |
| dc.subject.other |
sequence homology |
en |
| dc.subject.other |
species difference |
en |
| dc.subject.other |
Streptococcus thermophilus |
en |
| dc.subject.other |
Cheese |
en |
| dc.subject.other |
Cloning, Molecular |
en |
| dc.subject.other |
Dipeptidyl Peptidases |
en |
| dc.subject.other |
DNA Primers |
en |
| dc.subject.other |
DNA, Bacterial |
en |
| dc.subject.other |
Molecular Sequence Data |
en |
| dc.subject.other |
Sequence Analysis, DNA |
en |
| dc.subject.other |
Sequence Homology, Amino Acid |
en |
| dc.subject.other |
Streptococcus |
en |
| dc.subject.other |
Bacteria (microorganisms) |
en |
| dc.subject.other |
Posibacteria |
en |
| dc.subject.other |
Streptococcus |
en |
| dc.subject.other |
Streptococcus thermophilus |
en |
| dc.title |
Cloning and sequencing of the gene encoding X-prolyl-dipeptidyl aminopeptidase (PepX) from Streptococcus thermophilus strain ACA-DC 4 |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1046/j.1365-2672.2002.01659.x |
en |
| heal.publicationDate |
2002 |
en |
| heal.abstract |
Aims: To clone and sequence the pepX gene from Streptococcus thermophilus. Methods and Results: Three pairs of primers were used in polymerase chain reactions using as template the total DNA from Strep. thermophilus ACA-DC 4 in order to amplify, clone and sequence the pepX gene. Sequence analysis revealed an open reading frame of 2268 nucleotides encoding a protein of 755 amino acids. The calculated molecular mass of 85 632 Da agreed well with the apparent molecular mass of 80 000 Da previously determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and gel filtration for the monomeric form of the purified enzyme. Conclusions: The pepX gene from Strep. thermophilus ACA-DC 4 was cloned and sequenced. The PepX protein showed significant sequence similarity with PepX enzymes from other lactic acid bacteria and contained a motif which was almost identical with the active site motif of the serine-dependent PepX family. Significance and Impact of the Study: There are economic and technological incentives for accelerating and controlling the process of cheese ripening. To achieve this, starters may be modified by introducing appropriate genes from other food-grade bacteria. New or additional peptidase activities may alter or improve the proteolytic properties of lactic acid bacteria. |
en |
| heal.journalName |
Journal of Applied Microbiology |
en |
| dc.identifier.issue |
1 |
en |
| dc.identifier.volume |
93 |
en |
| dc.identifier.doi |
10.1046/j.1365-2672.2002.01659.x |
en |
| dc.identifier.spage |
52 |
en |
| dc.identifier.epage |
59 |
en |