Characterization and Complete Sequence of Lactonase Enzyme from <i>Bacillus weihenstephanensis</i> Isolate P65 with Potential Activity against Acyl Homoserine Lactone Signal Molecules

<table class="table-group" id="tab1"><tr><td><table class="table"><tr><td class="thead-hr" colspan="2"><hr/></td></tr><tr class="thead"><td align="left">Substrate</td><td align="center">Lactonase activity units/mg total protein</td></tr><tr><td class="thead-hr" colspan="2"><hr/></td></tr><tr><td align="left">C4-HSL</td><td align="center">30.16 U/mg</td></tr><tr><td align="left">C6-HSL</td><td align="center">36.3 U/mg</td></tr><tr><td align="left">C7-HSL</td><td align="center">32.02 U/mg</td></tr><tr><td align="left">C8-HSL</td><td align="center">21.2 U/mg</td></tr><tr class="table-tr"><td colspan="2"><hr class="tbody-hr"/></td></tr></table></td></tr></table>

Hydrolytic activity on different AHL standards.

BioMed Research International

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Table 1

Table 1: Characterization and Complete Sequence of Lactonase Enzyme from <i>Bacillus weihenstephanensis</i> Isolate P65 with Potential Activity against Acyl Homoserine Lactone Signal Molecules 

Table 1 | Characterization and Complete Sequence of Lactonase Enzyme from Bacillus weihenstephanensis Isolate P65 with Potential Activity against Acyl Homoserine Lactone Signal Molecules 