Pregled bibliografske jedinice broj: 906564
Substrate binding of a copper-dependent fungal lytic polysaccharide monooxigenase
Substrate binding of a copper-dependent fungal lytic polysaccharide monooxigenase // European Summit of Industrial Biotechnology 2017
Graz, Austrija, 2017. str. 167-167 (poster, međunarodna recenzija, sažetak, znanstveni)
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Naslov
Substrate binding of a copper-dependent fungal lytic polysaccharide monooxigenase
Autori
Andlar, Martina ; Kracher, Daniel ; Rezić, Tonči ; Šantek, Božidar ; Ludwig, Roland
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
European Summit of Industrial Biotechnology 2017
/ - , 2017, 167-167
Skup
European Summit of Industrial Biotechnology 2017
Mjesto i datum
Graz, Austrija, 14.11.2017. - 16.11.2017
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
substrate binding ; copper reduction ; LPMO
Sažetak
The depolymerisation of complex biomass such as lignocellulose by organisms depends on a network of enzymatic and chemical reactions. Fungi that can grow on lignocellulosic materials are equipped with a complex enzymatic degradation system, including a broad variety of hydrolases and oxidoreductases. In 2010, a new class of enzymes was discovered, which carry out oxidative cleavage of polysaccharides. These enzymes, today known as lytic polysaccharide monooxygenases (LPMOs, CAZy family AA9) are copper-dependent oxidoreductases that can hydroxylate the C1 or C4 positions of glucose and thereby cleave the glycosidic bonds in cellulose. These “cellulase activity boosters” provide hydrolytic enzymes access to crystalline cellulose by introducing chain breaks. LPMOs, despite their importance in biotechnology, are difficult to investigate because of their complex heterogeneous reaction mechanism. An open question is how LPMOs orchestrate the complex reaction between copper reduction, co-substrate activation and substrate binding. It is generally accepted that the first reaction step of LPMO is the reduction of the active-site copper by small molecule reductants or by other enzymes (CDH, GDH). In this work, we address the substrate binding of oxidized and reduced LPMO-02916 from Neurospora crassa to phosphoric acid swollen cellulose (PASC) and microcrystalline cellulose (MC) to investigate the role of the copper centre for substrate binding.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija, Interdisciplinarne biotehničke znanosti
POVEZANOST RADA
Projekti:
HRZZ-IP-2013-11-9158 - Održiva proizvodnja bioetanola i biokemikalija iz otpadnih poljoprivrednih lignoceluloznih sirovina (SPECH-LRM) (Šantek, Božidar, HRZZ - 2013-11) ( CroRIS)
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb