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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

The pectinases from Sphenophorus levis: Potential for biotechnological applications

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Autor(es):
Habrylo, Olivier [1] ; Evangelista, Danilo Elton [2] ; Castilho, Priscila Vasques [2] ; Pelloux, Jerome [1] ; Henrique-Silva, Flavio [2]
Número total de Autores: 5
Afiliação do(s) autor(es):
[1] Univ Picardie, BIOPI Biol Plantes & Innovat SFR Condorcet FR CNR, EA3900, 33 Rue St Leu, F-80039 Amiens - France
[2] Univ Fed Sao Carlos, Dept Genet & Evolut, Lab Mol Biol, Rd Washington Luis Km 235, BR-13565905 Sao Carlos, SP - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: International Journal of Biological Macromolecules; v. 112, p. 499-508, JUN 2018.
Citações Web of Science: 1
Resumo

Pectinases represent about one fifth of the enzyme worldwide market due their wide range of biotechnological applications. Current commercial pectinases are exclusively obtained from microbial sources, but here we report a pectin methylesterase (Sl-PME) and an endo-polygalacturonase (Sl-EPG) bioprospected from the sugarcane weevil, Sphenophorus levis, which revealed good potential for industrial applications. Sl-PME and Sl-EPG were overexpressed in Pichia pastoris, purified and enzymatically characterized. Sl-EPG presents optimal activity at pH 4-5 and 50 degrees C, showing that it can be used for juice extraction and clarification. On the other hand, Sl-PME presents optimal activity at pH 6-8 and 40 degrees C, and thus, suitable for both acidic and alkaline processing, such as coffee and tea fermentation. Sl-EPG shows V-max = 3.23 mM/min, K-M = 2.4 g/L and k(cat) = 418.6 s(-1). While Sl-PME shows V-max = 0.14 mM/min, K-M = 4.1 g/L and k(cat) = 1.7 s(-1). A PG inhibitor (PGIP2) weakly interfered in the Sl-EPG activity and Sl-PME was not affected by a usual PME inhibitor. Moreover, these enzymes manifested synergistic action towards methylesterified pectin. Here, we propose these enzymes as novel alternative tools for the current commercial pectinases. (C) 2018 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 98/14138-2 - Center for Structural Molecular Biotechnology
Beneficiário:Glaucius Oliva
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs