Abstract:
Trypsin protease is a crucial enzyme with diverse applications across
various industries, including food, pharmaceuticals, and biotechnology. While extensively studied in
eukaryotes, the trypsin from Lactobacillus plantarum VF3 presents intriguing differences in its
structural and functional properties.
Objectives: This study aims to identify and characterize the gene encoding trypsin protease in
L. Plantarum VF3, highlighting its distinct enzymatic features.
Methods: The L. plantarum VF3 strain, isolated from cow milk, was identified using the 16S
rRNA gene method. Specific primers were employed for PCR analysis of the tlp gene, and the resulting
products were sequenced using the BigDye™ Terminator v3.1 Cycle Sequencing Kit. The I-TASSER
server was utilized for protein structure prediction and functional analysis.
Results and discussion: The investigation confirmed the presence of the tlp gene within the
genome of L. plantarum VF3, highlighting a notable difference in its amino acid sequence compared
to human trypsin. This divergence in sequence correlates with distinct catalytic properties, where
lactobacillus trypsin displays enhanced specificity for substrates. These findings emphasize the
distinctiveness of L. plantarum VF3 trypsin in its potential applications within the biotechnology and
food industries, paving the way for novel enzymatic solutions with tailored properties.
Conclusion: This study elucidates trypsin protease's genetic basis and distinctive characteristics
in L. plantarum VF3. The observed differences in sequence and catalytic properties compared to
eukaryotic trypsin open exciting possibilities for exploiting this enzyme in various industrial
applications, ranging from food processing to biotechnology. Further research in harnessing these
unique features promises innovative solutions in enzyme technology.
Keywords: Trypsin, Lactobacillus plantarum, 16S rRNA, PCR, I-TASSER, enzyme technology
