Structure-Antibacterial Activity Relationship of Enterocin A

Abstract

Abstract: In order to analyze the relationship between molecular structure and antilisterial activity of enterocin A, MBP-enterocin A mutants (C14S, K46E or K46Q, and C47W) with serine, glutamic acid or glutamine, and tryptophane as a substitute for cysteine (at position 14), lysine (at position 46) and cysteine (at position 47) respectively were created and expressed in Escherichia coli fusion expression systems. The mutants K46E and K46Q showed similar anti-Listeria ivanovii LIV2 activity to MBP-enterocin A, while the mutants C14S and C47W had no inhibitory effect on Listeria ivanovii LIV2. Therefore, the residues C14 and C47 rather than K46 were essential for the antibacterial function of enterocin A.

Key words: enterocin A, mutant, antilisterial activity

CLC Number:

TS201.3

References

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