SUMMARY: Sakacin A, a bacteriocin produced by Lb706 and which inhibits the growth of , was purified to homogeneity by ammonium sulphate precipitation and ion-exchange, hydrophobic-interaction and reversed-phase chromatography. The complete amino acid sequence of sakacin A was determined by Edman degradation. The bacteriocin consisted of 41 amino acid residues and had a calculated of 4308.7, which is in good agreement with the value determined by mass spectrometry. The structural gene encoding sakacin A () was cloned and sequenced. The gene encoded a primary translation product of 59 amino acid residues which was cleaved between amino acids 18 and 19 to yield the active sakacin A. Sakacin A shared some sequence similarities with other bacteriocins.


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