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Fernanda Dell Antonio Facchini

Researcher at University of São Paulo

Publications -  16
Citations -  321

Fernanda Dell Antonio Facchini is an academic researcher from University of São Paulo. The author has contributed to research in topics: Lipase & Immobilized enzyme. The author has an hindex of 11, co-authored 16 publications receiving 281 citations.

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Production of fibrolytic enzymes by Aspergillus japonicus C03 using agro-industrial residues with potential application as additives in animal feed

TL;DR: Solid-state fermentation obtained from different and low-cost carbon sources was evaluated to endocellulases and endoxylanases production by Aspergillus japonicus C03 and xylanase was greatly stable in goat rumen fluid for 4 h during in vivo and in vitro experiments.
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Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.

TL;DR: The alkaline protease produced through solid-state fermentation (SSF), was immobilized on beads of calcium alginate, allowing comparative analyses of free and immobilized proteases to be carried out and it was observed that both optimum temperature and thermal stability of the immobilized enzyme were higher than for the free enzyme.
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Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: Determination of thermal and organic solvent stabilities for applications in the oleochemical industry

TL;DR: The adsorption of lipases in low ionic strength and highly hydrophobic supports is shown to be a simple and rapid tool for the immobilization of H. pseudokoningii lipase, and derivatives with excellent thermal stabilities strongly increase the chances of this biocatalyst for industrial application.
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A novel glucoamylase activated by manganese and calcium produced in submerged fermentation by Aspergillus phoenicis.

TL;DR: This study investigates the production of glucoamylase from Aspergillus phoenicis in Machado Benassi medium using 1% maltose as carbon source and finds that the enzyme was totally stable at 30–65 °C for 1 h, and the pH range was 3.0–6.0.
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A New Lipase Isolated from Oleaginous Seeds from Pachira aquatica (Bombacaceae)

TL;DR: A new lipase from seeds of Pachira aquatica was purified to homogeneity by SDS-PAGE obtaining an enzyme with a molecular weight of approximately 55 kDa that showed preference for esters of long-chain fatty acids, but demonstrated significant activity against a wide range of substrates.