Pregled bibliografske jedinice broj: 72542
Substrate specifity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus
Substrate specifity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus // Enzyme and Microbial Technology, 29 (2001), 548-553 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 72542 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Substrate specifity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus
Autori
Leščić, Ivana ; Vukelić, Bojana ; Majerić-Elenkov, Maja ; Saenger, Wolfram ; Abramić, Marija
Izvornik
Enzyme and Microbial Technology (0141-0229) 29
(2001);
548-553
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Streptomyces rimosus; Lipase; Lipid hydrolysis; Organic solvent effects; Conformational stability; Transesterification
Sažetak
Substrate specificity, regioselectivity and transesterification activity of purified extracellular lipase from Streptomyces rimosus were investigated. The enzyme showed pronounced lipolytic activity toward a number of triacylglycerols and oils of vegetable and animal origin.It hydrolyzed most efficiently medium chain lenght fatty acid glycerol esters (C8-C12). There was preference for the esters of C16 and C18 unsaturated fatty acids over C16 and C18 saturated fatty acid esters, as well as for triacylglycerol substrate with cis double bond (triolein)versus trans double bond (trielaidin). Streptomyces rimosus lipase hydrolyzed primary and secondary ester bonds in triacylglycerols (triolein and 2,3-dimercapto-1-propanol tributirate). The lipase catalyzed the hydrolysis of poly(oxyethylene) sorbitan monoesters (Tween 20-80) with rate comparable for that determined with triacylglycerols and oils. Several water-miscible solvents enhanced the lipase activity. 1,4-Dioxane activated the enzyme in a broad concentration range, up to 4-fold. Lipase was stable in solvent mixtures containing 50% (v/v) ethanol, 1,4-dioxane, acetonitrile or acetone. Tetrahydrofuran and N,N-dimethylformamide (both 50%) inactivated the enzyme with t1/2 of 5 min and t1/2 of 2 h, respectively. Transesterification of racemic 1-phenyl ethanol with vinyl acetate, catalyzed by extracellular lipase from Streptomyces rimosus in n-hexane, proceeded with partial R-enantioselectivity.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Marija Abramić
(autor)
Ivana Leščić Ašler
(autor)
Maja Majerić Elenkov
(autor)
Bojana Vukelić
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus