Dipeptidyl peptidase-II from probiotic Pediococcus acidilactici: Purification and functional characterization

Area of Science:

• Biochemistry
• Enzymology
• Microbiology

Background:

• Dipeptidylpeptidase-II (DPP-II) is an exopeptidase with limited characterization.
• Probiotic microorganisms like Pediococcus acidilactici are sources of novel enzymes.

Purpose of the Study:

• To purify and characterize DPP-II from Pediococcus acidilactici.
• To investigate the potential applications of DPP-II in food processing, specifically meat tenderization.

Main Methods:

• Enzyme purification using a two-step procedure.
• Biochemical characterization including optimal pH, temperature, and kinetic parameters (K M, Vmax).
• In-silico analysis for structural and evolutionary insights, and functional studies using TLC, HPLC, SDS-PAGE, and microscopy.

Main Results:

• DPP-II was purified 15.4-fold with high specific activity and yield.
• The enzyme is a 38.7KDa homodimeric serine peptidase, optimally active at pH 7.0 and 37°C, stable up to 50°C.
• In-silico studies suggested evolutionary links to prokaryotic phosphate binding proteins; functional assays demonstrated collagen hydrolysis and myofibril degradation in chicken meat, indicating tenderization potential.

Conclusions:

• Purified DPP-II from Pediococcus acidilactici exhibits favorable biochemical properties for industrial applications.
• The enzyme's ability to hydrolyze meat proteins suggests a role in meat tenderization, with potential for safe application due to its origin from lactic acid bacteria.