On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase

Biochim Biophys Acta. 1995 Oct 5;1258(3):272-6. doi: 10.1016/0005-2760(95)00131-u.


The interfacial activation of Candida antarctica lipase A (CALA) and B (CALB) has been investigated and compared with that of Humicola lanuginosa lipase (HLL). CALB displayed no interfacial activation towards p-nitrophenyl butyrate (PNPB) when exceeding the solubility limit of the substrate. No activation was observed towards p-nitrophenyl acetate (PNPA) at the addition of sodium dodecyl sulfate (SDS) nor in the presence 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 absence of a lid that regulates the access to the active site. In contrast to CALB, CALA expressed interfacial activation, but the activation was not as prominent as for Humicola lanuginosa lipase (HLL). The structural basis for the activation of CALA is unknown.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Binding Sites
  • Butyrates / metabolism
  • Candida / enzymology*
  • Enzyme Activation
  • Lipase / chemistry
  • Lipase / metabolism*
  • Mitosporic Fungi / enzymology*
  • Nitrophenols / metabolism
  • Protein Conformation
  • Protein Structure, Secondary
  • Sodium Dodecyl Sulfate / pharmacology
  • Surface Properties
  • Triglycerides / metabolism


  • Butyrates
  • Nitrophenols
  • Triglycerides
  • 4-nitrophenyl butyrate
  • Sodium Dodecyl Sulfate
  • 4-nitrophenyl acetate
  • Lipase
  • tributyrin