Characterization of Trypsin-Like Protease of Lactobacillus plantarum FNCC 0270
Trypsin is an enzyme that has a unique mechanism of cutting peptide bonds specifically at the carboxyl side of lysine or arginine amino acids, with another amino acid. This study aims to analyze a trypsin-like protease (TLP) found in Lactobacillus plantarum FNCC 0270, by performing partial proteomic tests, i.e. MALDI-TOF/TOF, and standard bioinformatics tools. SDS-PAGE analysis showed 4 protein bands. Two bands of the (P1 and P2) showed molecular weights equivalent to 47.35 and 38.42 kD, each generating 8 and 11 peptide fragments respectively. According to information in www.ncbi.nlm.nih.gov/genbank/structures, the structure of serine protease HtrA (subs. plantarum L. plantarum ST–III) consists of three domains. Using Clone Manager® software by aligning two sequences we obtained eleven. The Lactobacillus produces of the trypsin-like serine protease has 40-90% similarity. Using the Clustal W2 software we passed the 11 sequences through multiple alignments, and found that the isolate L. plantarum is closely related to L. buchneri, L. brevis, and L. malefermentans on the phylogenetic tree. Alignment analysis results showed that all 8 peptide fragments of band 1 and 11 peptide fragments of band 2, of the SDS-PAGE, were located in the active domain region of the fourth trypsin-like serine protease producing Lactobacilli.
Starting Vol. 25 No. 1, HAYATI J Biosci article's license is CC-BY. This license lets others distribute, remix, tweak, and build upon author's work, even commercially, as long as they credit the original creation.
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
- Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).