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GDS(L) lipases from streptomycetes (CROSBI ID 551419)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija

Marić, Marija ; Bielen, Ana ; Abramić, Marija ; Vujaklija, Dušica GDS(L) lipases from streptomycetes // Zbornik sažetaka znanstvenog simpozija 50 godina molekularne biologije u Hrvatskoj / Zahradka, Ksenija ; Plohl, Miroslav ; Ambriović-Ristov, Andreja (ur.). Zagreb: Institut Ruđer Bošković, 2008. str. 41-x

Podaci o odgovornosti

Marić, Marija ; Bielen, Ana ; Abramić, Marija ; Vujaklija, Dušica

engleski

GDS(L) lipases from streptomycetes

GDS(L) esterases/lipases investigated so far have very interesting biochemical and structural properties, but are still insufficiently studied. Furthermore, only a small number of streptomycete GDS(L) enzymes has been characterized so far. Three highly homologous GDS(L) lipases from genus Streptomyces were cloned: lipase from S. rimosus (Q93MW7, SrL) and two lipases from S. coelicolor (SCO1725, Sc1 and SCO7513, Sc2). Genes were PCR amplified and ligated into E. coli vector, resequenced, and subsequently ligated into the Streptomyces expression plasmid pANT849. Heterologous, lipase deficient host Streptomyces lividans was used enzyme production. We will present here the results of biochemical characterization of SrL and Sc1. Both enzymes are predominantly α -helical proteins, as shown by CD spectroscopy. They have high working temperature (55°C), stability over a broad range of pH and temperature, and can hydrolyze numerous classes of substrates (p-nitrophenyl alkanoates, α - and ß-naphthyl alkanoates, oils, triacylglycerols, and Tween detergents). The most pronounced difference between SrL and Sc1 is in acyl chain length specificity, as SrL shows maximal activity toward substrates with chain lengths C8-C10, and Sc1 shows preference for substrates with longer acyl-chain lengths (C14). Further, enzymes are stable and show activation in several tested organic solvents. These results implicate high biotechnological potential of the studied enzymes.

GDS(L) lipases; streptomycetes

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Podaci o prilogu

41-x.

2008.

objavljeno

Podaci o matičnoj publikaciji

Zbornik sažetaka znanstvenog simpozija 50 godina molekularne biologije u Hrvatskoj

Zahradka, Ksenija ; Plohl, Miroslav ; Ambriović-Ristov, Andreja

Zagreb: Institut Ruđer Bošković

978-953-6690-78-7

Podaci o skupu

Znanstveni simpozij 50 godina molekularne biologije u Hrvatskoj

poster

20.11.2008-21.11.2008

Zagreb, Hrvatska

Povezanost rada

Biotehnologija, Biologija