LIPASE OF PSEUDOMONAS-CEPACIA FOR BIOTECHNOLOGICAL PURPOSES - PURIFICATION, CRYSTALLIZATION AND CHARACTERIZATION

 
see the original item page
in the repository's web site and access all digital files if the item*
share




1994 (EN)
LIPASE OF PSEUDOMONAS-CEPACIA FOR BIOTECHNOLOGICAL PURPOSES - PURIFICATION, CRYSTALLIZATION AND CHARACTERIZATION (EN)

FREITAG, R (EN)
SCHEPER, T (EN)
REIF, OW (EN)
LAUSCH, R (EN)
KOLISIS, FN (EN)
MENGE, U (EN)
BORNSCHEUER, U (EN)

N/A (EN)

Commercial lipase (triacylglycerol lipase, EC 3.1.1.3) of Pseudomonas cepacia (Amano) has been purified to homogeneity by a single chromatography on phenyl Sepharose. The eluted lipase crystallized spontaneously at 4 degrees C in the eluent, containing 58-69% 2-propanol. The yield of the lipase was 87-100% and the specific activity during the hydrolysis of triolein 5800 U/mg protein. This protein has a molecular weight of 34.1 kDa as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Its purity was determined by SDS-PAGE and capillary zone electrophoresis to be greater than or equal to 99%. Immobilization on Sepharose increased its stability in organic solvents. This lipase of P. cepacia differs from that of other Pseudomonas strains in respect to substrate specificity and during crystallization. It exhibits a high stability in organic solvents and supercritical carbon dioxide. (EN)

journalArticle

TRIACYLGLYCEROL LIPASE (EN)
GENE (EN)
CLONING (EN)
PROTEIN PURIFICATION (EN)
(P-CEPACIA) (EN)
PROTEINS (EN)
FLUORESCENS (EN)

Εθνικό Μετσόβιο Πολυτεχνείο (EL)
National Technical University of Athens (EN)

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (EN)

1994


ELSEVIER SCIENCE BV (EN)



*Institutions are responsible for keeping their URLs functional (digital file, item page in repository site)