Pregled bibliografske jedinice broj: 902123
LPMO as a key player in the enzyme conversion of biomass
LPMO as a key player in the enzyme conversion of biomass // Journal of Biotechnology, European Biotechnology Congress 2017 / Dundar, Munis (ur.).
Dubrovnik, Hrvatska: Elsevier, 2017. str. S12-S12 (pozvano predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 902123 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
LPMO as a key player in the enzyme conversion of biomass
Autori
Andlar, Martina ; Kracher, Daniel ; Rezić, Tonči ; Ludwig, Roland
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Journal of Biotechnology, European Biotechnology Congress 2017
/ Dundar, Munis - : Elsevier, 2017, S12-S12
Skup
European Biotechnology Congress 2017
Mjesto i datum
Dubrovnik, Hrvatska, 25.05.2017. - 27.05.2017
Vrsta sudjelovanja
Pozvano predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
Lignocellulose, LPMO, copper reduction, substrate binding
Sažetak
Lignocellulose is a renewable resource that can be used for the sustainable production of platform chemicals or fuels. However, the recalcitrance of cellulose to hydrolytic depolymerization is a barrier to microbial and industrial utilization of lignocellulosic biomass. Cellulose is broken down to glucose by endo- and exo-acting glycosyl hydrolases which process the glucan chains in cellulose to soluble cellobiose moieties. In a process known as oxidative cellulose degradation, copper-dependent lytic polysaccharide monooxygenases (LPMO) cleave polymeric substrates, including crystalline cellulose, hemicelluloses and starch. It remains difficult to find how LPMOs orchestrate the complex reaction between copper reduction, co-substrate activation and substrate binding. To test the hypothesis that copper reduction increases binding of LPMO to cellulose, we studied the binding of oxidized and reduced LPMO to amorphous cellulose (PASC) and to microcrystalline cellulose (MC). Also, we aimed to quantify the substrate binding by measuring binding isotherms. The data demonstrate that copper reduction is a driver for substrate binding.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija, Interdisciplinarne biotehničke znanosti
POVEZANOST RADA
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb