| Autor: |
Hossain, Musaddique, Dodda, Subba Reddy, Kapoor, Bishwajit Singh, Aikat, Kaustav, Mukhopadhyay, Sudit S. |
| Jazyk: |
angličtina |
| Rok vydání: |
2020 |
| DOI: |
10.1101/2020.04.24.059154 |
| Popis: |
Efficient conversion of lignocellulosic biomass into fermentable sugar is a bottleneck for cheap production of bio-ethanol. Recently identified enzyme Lytic Polysaccharide Monooxygenase (LPMO) family has brought new hope because of its boosting capabilities of cellulose hydrolysis. Cellulase enzymes of Aspergillus origin are important for their thermo-stable nature. Here we have identified and characterized a new class of auxiliary (AA16) oxidative enzyme LPMO from the genome of a locally isolated thermophilic fungus Aspergillus fumigatus (NITDGPKA3). The biochemical, structural, and biomass conversion efficiency of Af LPMO16 have been explored. The Af LPMO16 is an intronless gene and encodes the protein of about 29kDa of molecular weight. Sequence-wise it is close to C1 type and structurally it is similar to AA11 family of LPMOs. The structure exclusively consists of loops and sheets. The gene was expressed under inducible promoter (AOX1) with C-terminal His tag in the Pichia pastoris . The protein was purified, and enzyme kinetics was studied with 2, 6-DMP. Polysaccharides hydrolysis activity was observed with Carboxymethyl cellulose (CMC) and Phosphoric acid swollen cellulose (PASC). Further, the lignocellulosic biomass conversion enhancement with Cellulase cocktail gives 2-fold enhancement in reducing sugar release suggests the importance of Af LPMO16 in the bio-ethanol industry. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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