Publications by authors named "Fernanda L Figueiredo"

Background: Fermentation of sugars derived from plant biomass feedstock is crucial for sustainability. Hence, utilizing customized enzymatic cocktails to obtain oligosaccharides instead of monomers is an alternative fermentation strategy to produce prebiotics, cosmetics, and biofuels. This study developed an engineered strain of Aspergillus niger producing a tailored cellulolytic cocktail capable of partially degrading sugarcane straw to yield cellooligosaccharides.

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Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that oxidize polysaccharides, leading to their cleavage. LPMOs are classified into eight CAZy families (AA9-11, AA13-17), with the functionality of AA16 being poorly characterized. This study presents biochemical and structural data for an AA16 LPMO (PnAA16) from the marine sponge symbiont Peniophora sp.

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is a filamentous fungus that was isolated from decaying sugarcane straw at a Brazilian ethanol biorefinery. This fungus shows potential as a source of plant cell wall-degrading enzymes (PCWDEs). In this study, we conducted a comprehensive multiomics investigation of to gain insights into its enzymatic capabilities and genetic makeup.

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Aspergillus fumigatus represents a public health problem due to the high mortality rate in immunosuppressed patients and the emergence of antifungal-resistant isolates. Protein acetylation is a crucial post-translational modification that controls gene expression and biological processes. The strategic manipulation of enzymes involved in protein acetylation has emerged as a promising therapeutic approach for addressing fungal infections.

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Protein acetylation is a crucial post-translational modification that controls gene expression and a variety of biological processes. Sirtuins, a prominent class of NAD -dependent lysine deacetylases, serve as key regulators of protein acetylation and gene expression in eukaryotes. In this study, six single knockout strains of fungal pathogen were constructed, in addition to a strain lacking all predicted sirtuins (SIRTKO).

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Lytic polysaccharide monooxygenases (LPMOs) are oxidative enzymes found in viruses, archaea, and bacteria as well as eukaryotes, such as fungi, algae and insects, actively contributing to the degradation of different polysaccharides. In Aspergillus nidulans, LPMOs from family AA9 (LPMO9s), along with an AA3 cellobiose dehydrogenase (CDH1), are cosecreted upon growth on crystalline cellulose and lignocellulosic substrates, indicating their role in the degradation of plant cell wall components. Functional analysis revealed that three target LPMO9s (LPMO9C, LPMO9F and LPMO9G) correspond to cellulose-active enzymes with distinct regioselectivity and activity on cellulose with different proportions of crystalline and amorphous regions.

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Background: Wood-decay basidiomycetes are effective for the degradation of highly lignified and recalcitrant plant substrates. The degradation of lignocellulosic materials by brown-rot strains is carried out by carbohydrate-active enzymes and non-enzymatic Fenton mechanism. Differences in the lignocellulose catabolism among closely related brown rots are not completely understood.

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Sugarcane straw (SS) is a widely available agricultural processing feedstock with the potential to produce 2nd generation bioethanol and bioproducts, in addition to the more conventional use for heat and/or electrical power generation. In this study, we investigated the operational parameters to maximize the production of xylo-oligosaccharides (XOS) using mild deacetylation, followed by hydrothermal pretreatment. From the laboratory to the pilot-scale, the optimized two-stage pretreatment promoted 81.

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Article Synopsis
  • The study focused on evaluating the effectiveness of endo-arabinanase (ABNase) from Bacillus licheniformis in breaking down sugarcane through enzyme immobilization and enhancement with a commercial enzyme cocktail.
  • Biochemical analysis revealed that ABNase's activity was significantly inhibited by certain metal ions (Cu²⁺, Zn²⁺, Fe³⁺), with optimal activity at a pH of 5.5-6.5 and temperature of 35-40 °C; enzyme stability increased dramatically when immobilized.
  • The findings indicate that recombinant ABNase enhances pectin hydrolysis, improving the efficiency of enzymatic cocktails in sugarcane biomass saccharification
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