Purification and characterization of two distinct lipases from Candida cylindracea

• Published in: Biochimica et biophysica acta Vol. 1156; no. 2; pp. 181 - 189
• Main Authors: Rúa, M.Luisa, Díaz-Mauriño, Teresa, Fernández, Victor M., Otero, Cristina, Ballesteros, Antonio
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 13.02.1993; Elsevier
• Subjects: Amino Acid Sequence; Amino Acids - analysis; Biological and medical sciences; Candida - enzymology; Candida cylindracea; Candida rugosa; Enzyme characterization; Enzyme purification; Fundamental and applied biological sciences. Psychology; Growth, nutrition, metabolism, transports, enzymes. Molecular biology; Hot Temperature; Hydrogen-Ion Concentration; Isoenzyme; Isoenzymes - chemistry; Isoenzymes - isolation & purification; Kinetics; Lipase; Lipase - chemistry; Lipase - isolation & purification; Microbiology; Molecular Sequence Data; Molecular Weight; Mycology; Solvents; Substrate Specificity; Temperature; Triolein - metabolism; Candida cylindracea; Bes; THF; Enzyme purification; Con A; Isoenzyme; Mes; Lipase; Candida rugosa; Enzyme characterization; Fungi; Purification; Enzymatic activity; Enzyme; Substrate specificity; Triacylglycerol lipase; Fungi Imperfecti; Physicochemical properties; Aminoacid sequence; Thallophyta
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(93)90134-T

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.