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Substrate specifity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus


Leščić, Ivana; Vukelić, Bojana; Majerić-Elenkov, Maja; Saenger, Wolfram; Abramić, Marija
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)


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


Projekt / tema
00980608
00980701
00980705

Ustanove
Institut "Ruđer Bošković", Zagreb

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