Purification and characterization of two distinct lipases from Candida cylindracea

  • Biochim Biophys Acta. 1993 Feb 13;1156(2):181-9. doi: 10.1016/0304-4165(93)90134-t.
L Rúa  1 ,  T Díaz-Mauriño ,  V M Fernández ,  C Otero ,  A Ballesteros
Affiliations
  • 1. Instituto de Catálisis, CSIC, Universidad Autónoma, Madrid, Spain.
PMID: 8427877 DOI: 10.1016/0304-4165(93)90134-t
Abstract

We have purified and characterized two isoenzymes from a commercial Lipase preparation of Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and Lipase B were purified 11-fold with a 5% and 21% recovery in activity, respectively. The Enzymes have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content, hydrophobicity, presence of isoforms and stability to pH and temperature. They also show some differences in the substrate specificity.

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