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. 2012 Sep 28;7(9):e46493. doi: 10.1371/journal.pone.0046493

Table 1. Substrate specificity of recombinant Lip-HSL proteins.

Substrate chain length/specific activitiesa (U/mg)
pNP estersb Vinyl estersc TAGd
Protein Best Up to Best Up to Best Up to
LipC [18] C4/0.12 C10/0.02 n.d n.d n.d n.d
LipF C4/0.18 C10/0.02 n.d n.d n.d n.d
LipH [20] C4/13.5 ND C3/1600 C4/1100 C3/1350 C4/450
LipI C4/15.7 ND C4/73 C4/73 C3/30 C4/27
LipN C4/7.2 C14/0.04 C4/1390 C4/1390 C3/350 C4/240
LipR C8/0.53 C12/0.27 n.d n.d n.d n.d
LipU C8/0.48 C14/0.04 n.d n.d n.d n.d
LipW C4/1600 C14/0.04 n.d n.d n.d n.d
LipY C4/46.3 C14/5.2 C4/300 C8/35 C4/208 C18:3/4.0
a

All activities were performed beyond the substrate solubility limit (except for pomegranate oil, which was directly coated on the plate) and 1 unit (U) corresponds to 1 µmol of fatty acid released per min.

b

Chain lengths tested include C4, C5, C8, C10, C12 and C14.

c

Chain lengths tested include C4, C6 and C8.

d

Chain lengths tested include C3, C4, C8, C18:1 (olive oil) and C18:3 (pomegranate oil).

ND not determined.

n.d not detected.