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. 2022 Mar 16;78(6):2215–2227. doi: 10.1002/ps.6846

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© 2022 The Authors. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Identification of the E. faecalis LX10 protein (enterococcin LX) by LC–MS/MS. (A) Analysis of the amino acid sequence of the enterococcin LX protein by MS/MS. Amino acid sequence of the enterococcin LX protein deduced from the draft Enterococcus genome sequence. Peptide sequences matching the LC–MS/MS results are highlighted in red. (B) Effect of pH (5‐10) on the activity of crude proteins (3–10 K). (C) The effect of temperature on the inhibitory substance was tested by heating the supernatant at 40, 60, 80, and 100 °C. (D) Peptides identified with LC–MS/MS.