Purification and characterization of two distinct lipases from Candida cylindracea.
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.
Rúa
L
L
Instituto de Catálisis, CSIC, Universidad Autónoma, Madrid, Spain.
Díaz-Mauriño
T
T
Fernández
V M
VM
Otero
C
C
Ballesteros
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002175:Candida / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012997:Solvents; D013379:Substrate Specificity; D013696:Temperature; D014304:Triolein / Q000378:metabolism
D000596:Amino Acids; D007527:Isoenzymes; D012997:Solvents; D014304:Triolein; D008049:Lipase