Pregled bibliografske jedinice broj: 410748
GDS(L) lipases from streptomycetes
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. (poster, domaća recenzija, sažetak, znanstveni)
CROSBI ID: 410748 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
GDS(L) lipases from streptomycetes
Autori
Marić, Marija ; Bielen, Ana ; Abramić, Marija ; Vujaklija, Dušica
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Zbornik sažetaka znanstvenog simpozija 50 godina molekularne biologije u Hrvatskoj
/ Zahradka, Ksenija ; Plohl, Miroslav ; Ambriović-Ristov, Andreja - Zagreb : Institut Ruđer Bošković, 2008
ISBN
978-953-6690-78-7
Skup
Znanstveni simpozij "50 godina molekularne biologije u Hrvatskoj"
Mjesto i datum
Zagreb, Hrvatska, 20.11.2008. - 21.11.2008
Vrsta sudjelovanja
Poster
Vrsta recenzije
Domaća recenzija
Ključne riječi
GDS(L) lipases; streptomycetes
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Biologija, Biotehnologija
POVEZANOST RADA
Projekti:
058-0582261-2246 - Utjecaj mutagena i antimutagena na molekularne procese u stanici (Hrašćan, Reno, MZOS ) ( CroRIS)
098-0982913-2877 - Temeljna molekularno-biološka istraživanja streptomiceta (Vujaklija, Dušica, MZOS ) ( CroRIS)
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb,
Institut "Ruđer Bošković", Zagreb