Mandelli F

References (2)

Title : Characterization and Low-Resolution Structure of an Extremely Thermostable Esterase of Potential Biotechnological Interest from Pyrococcus furiosus - Mandelli_2016_Mol.Biotechnol_58_757
Author(s) : Mandelli F , Goncalves TA , Gandin CA , Oliveira AC , Oliveira Neto M , Squina FM
Ref : Mol Biotechnol , 58 :757 , 2016
Abstract : Enzymes isolated from extremophiles often exhibit superior performance and potential industrial applications. There are several advantages performing biocatalysis at elevated temperatures, including enhanced reaction rates, increased substrate solubility and decreased risks of contamination. Furthermore, thermophilic enzymes usually exhibit high resistance against many organic solvents and detergents, and are also more resistant to proteolytic attack. In this study, we subcloned and characterized an esterase from the hyperthermophilic archaeon Pyrococcus furiosus (Pf_Est) that exhibits optimal activity around 80 degrees C using naphthol-derived substrates and p-nitrophenyl palmitate (pNPP). According to the circular dichroism spectra, the secondary structure of P. furiosus esterase, which is predominantly formed by a beta-sheet structure, is very stable, even after incubation at 120 degrees C. We performed SAXS to determine the low-resolution structure of Pf_Est, which is monomeric in solution at 80 degrees C and has a molecular weight of 28 kDa. The Km and V max values for this esterase acting on pNPP were 0.53 mmol/L and 6.5 x 10-3 U, respectively. Pf_Est was most active in the immiscible solvents and retained more than 50 % in miscible solvents. Moreover, Pf_Est possesses transesterification capacity, presenting better results when isobutanol was used as an acyl acceptor (2.69 +/- 0.14 x 10-2 mumol/min mg) and the highest hydrolytic activity toward olive oil among different types of oils testes in this study. Collectively, these biophysical and catalytic properties are of interest for several biotechnological applications that require harsh conditions, including high temperature and the presence of organic solvents.
ESTHER : Mandelli_2016_Mol.Biotechnol_58_757
PubMedSearch : Mandelli_2016_Mol.Biotechnol_58_757
PubMedID: 27665110
Gene_locus related to this paper: pyrfu-PF1108

Title : Biomass-to-bio-products application of feruloyl esterase from Aspergillus clavatus - Damasio_2013_Appl.Microbiol.Biotechnol_97_6759
Author(s) : Damasio AR , Braga CM , Brenelli LB , Citadini AP , Mandelli F , Cota J , de Almeida RF , Salvador VH , Paixao DA , Segato F , Mercadante AZ , de Oliveira Neto M , do Santos WD , Squina FM
Ref : Applied Microbiology & Biotechnology , 97 :6759 , 2013
Abstract : The structural polysaccharides contained in plant cell walls have been pointed to as a promising renewable alternative to petroleum and natural gas. Ferulic acid is a ubiquitous component of plant polysaccharides, which is found in either monomeric or dimeric forms and is covalently linked to arabinosyl residues. Ferulic acid has several commercial applications in food and pharmaceutical industries. The study herein introduces a novel feruloyl esterase from Aspergillus clavatus (AcFAE). Along with a comprehensive functional and biophysical characterization, the low-resolution structure of this enzyme was also determined by small-angle X-ray scattering. In addition, we described the production of phenolic compounds with antioxidant capacity from wheat arabinoxylan and sugarcane bagasse using AcFAE. The ability to specifically cleave ester linkages in hemicellulose is useful in several biotechnological applications, including improved accessibility to lignocellulosic enzymes for biofuel production.
ESTHER : Damasio_2013_Appl.Microbiol.Biotechnol_97_6759
PubMedSearch : Damasio_2013_Appl.Microbiol.Biotechnol_97_6759
PubMedID: 23229566