Abstract
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-DT) 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.
Highlights
According to Jellouli et al 2009, trypsin is one member of a large family of serine proteases which hydrolyse proteins and peptides at the carboxyl group of arginine and lysine residues
The Lactic Acid bacteria used to obtain trypsin-like protease (TLP) was from a collection of L. plantarum FNCC 0270 in the Laboratory for Technology Development of Agro-Biomedical Industries (LAPTIAB)-BPP Technology
To obtain TLP we followed a process of several stages: (Pato et al 2005; Wulansari et al 2012; Suri et al 2013) namely, the “rejuvenated ” of L. plantarum FNCC 0270 isolates in a media broth [Deman ROGOSA and Sharp broth (MRSB ) 5.2%] which was incubated at 37 oC, pH 8, and agitated at 50 rpm for 24 h, named culture
Summary
According to Jellouli et al 2009, trypsin is one member of a large family of serine proteases which hydrolyse proteins and peptides at the carboxyl group of arginine and lysine residues. The trypsin enzyme serves to convert trypsinogen into active trypsin, and to hydrolize the protein produced in the pancreas in the digestion process. Much research has been conducted on the isolation of trypsin from various species of fish including pomfret fish, bigeye snapper, red snapper, chinook salmon, monterey sardines, mandarin fish, and skipjack (Khantaphan & Benjakul 2010). Trypsin can be isolated from pork and beef. Isolation from these sources may be problematic because there is a fear the spread of bovine spongiform enchephalopathy (mad cow disease). LAB produce a variety of exopolysaccharide (EPS) that
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