M. Martinelle et al., ON THE INTERFACIAL ACTIVATION OF CANDIDA-ANTARCTICA LIPASE-A AND LIPASE-B AS COMPARED WITH HUMICOLA-LANUGINOSA LIPASE, Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1258(3), 1995, pp. 272-276
The interfacial activation of Candida antarctica lipase A (CALA) and B
(CALB) has been investigated and compared with that of Humicola lanug
inosa lipase (HLL). CALB displayed no interfacial activation towards p
-nitrophenyl butyrate (PNPB) when exceeding the solubility limit of th
e substrate. No activation was observed towards p-nitrophenyl acetate
(PNPA) at the addition of sodium dodecyl sulfate (SDS) nor in the pres
ence of a solid polystyrene surface. The catalytic action of CALB was
very different from that of Humicola lanuginosa lipase, which showed a
pronounced interfacial activation with the same substrates. The basis
for the anomalous behaviour of CALB is proposed to be due to the abse
nce of a lid that regulates the access to the active site. in contrast
to CALB, CALA expressed interfacial activation, but the activation wa
s not as prominent as for Humicola lanuginosa lipase (HLL). The struct
ural basis for the activation of CALA is unknown.