Purification and properties of extracellular lipase from Streptomyces rimosus (CROSBI ID 85544)
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Podaci o odgovornosti
Abramić, Marija ; Leščić, Ivana ; Korica, Tamara ; Vitale, Ljubinka ; Saenger, Wolfram ; Pigac, Jasenka
engleski
Purification and properties of extracellular lipase from Streptomyces rimosus
An extracellular lipase of Streptomyces rimosus R6-554W was isolated from culture filtrate by column chromatography using diethylaminoethyl-cellulose, carboxymethyl-cellulose, hydroxylapatite, Mono S (fast protein liquid chromatography), and Sephadex G-75. It was shown to be a monomeric, basic protein (Mr=27500, pI=8.45), active toward triolein and p-nitrophenyl esters, with preferrence for those with medium size (C8-C12) acyl chain length. Interfacial activation was observed with p-nitophenyl butyrate as substrate. The lipase was most active at 50-60°C and in alkaline conditions around pH 9-10, with p-nitrophenyl palmitate as substrate. It showed high stability at a broad pH range of 4-10 and was fairly thermostable. Dithiothreitol moderately inactivated the enzyme. Phenylmethylsulfonyl fluoride partly inhibited lipase only when added during the hydrolytic reaction.
Streptomyces rimosus; bacterial; extracellular; lipase
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