Identification and Isolation of Glycine, Alanine and Asparagine Rich Secretory Protein With Antibacterial Efficiency From Donax Cuneatus

Abstract

The crude protein was extracted from marine edible bivalve Donax cuneatus, precipitated and further dialysed against PBS in dialysis membrane having MW cut off of 3 KDa. The extract was evaluated for its antimicrobial activity against highly pathogenic Gram positive and Gram negative bacteria. It was found to be active against Pseudomonas aeruginosa and Staphylococcus aureus. The purified fractions obtained from anion-exchange column were evaluated for their activity against the aforesaid bacteria. The highly active fraction against Staphylococus aureus with the zone of inhibition of 12 mm was identified and further purified and characterised. The active fraction was enriched with glycine, alanine and asparagine aminoacids.