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Antibacterial cysteine protease from Cissus quadrangularis L.

Sakthivel Muthu1, Venkatesh Babu Gopal1, Narayan Karthik S1

  • 1Centre for Advanced Studies in Botany, University of Madras, Guindy Campus, Chennai 600025, Tamilnadu, India.

International Journal of Biological Macromolecules
|May 26, 2017
PubMed
Summary

A novel antibacterial enzyme (Cp) from Cissus quadrangularis exhibits potent activity against pathogenic bacteria by degrading their peptidoglycan layer. This purified enzyme shows stability across a wide pH range and optimal activity at 50°C.

Keywords:
Antibacterial activityCissus quadrangularisCysteine protease

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Area of Science:

  • Biochemistry
  • Microbiology
  • Pharmacology

Background:

  • Cissus quadrangularis is a medicinal plant with various therapeutic properties.
  • Antibacterial agents are crucial for combating pathogenic bacteria.
  • Enzymes with antibacterial activity represent a promising area of research.

Purpose of the Study:

  • To extract, purify, and characterize an antibacterial enzyme (Cp) from Cissus quadrangularis.
  • To evaluate the enzymatic and antibacterial properties of the purified Cp.
  • To investigate the mechanism of antibacterial action of Cp.

Main Methods:

  • Extraction and purification of Cp from Cissus quadrangularis stem.
  • Enzyme characterization using SDS-PAGE, Native-PAGE, optimum pH, and temperature determination.
  • Antibacterial activity assay against Bacillus cereus and Bacillus megaterium using zone of inhibition.
  • Transmission electron microscopy to confirm peptidoglycan degradation.

Main Results:

  • Cp was purified with a 5.39-fold increase in specific activity and 8.67% recovery.
  • The purified enzyme has a molecular weight of 39kDa and showed optimal activity at pH 6.0 and 50°C.
  • Cp demonstrated significant antibacterial activity against Bacillus cereus (21mm zone of inhibition) and Bacillus megaterium (20mm zone of inhibition).
  • Transmission electron microscopy confirmed Cp's ability to degrade the bacterial peptidoglycan layer.

Conclusions:

  • The purified Cp from Cissus quadrangularis possesses significant antibacterial properties.
  • Cp acts by degrading the bacterial peptidoglycan layer, offering a novel mechanism of action.
  • This enzyme holds potential as a therapeutic agent against bacterial infections.