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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The pectinases from Sphenophorus levis: Potential for biotechnological applications

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Author(s):
Habrylo, Olivier [1] ; Evangelista, Danilo Elton [2] ; Castilho, Priscila Vasques [2] ; Pelloux, Jerome [1] ; Henrique-Silva, Flavio [2]
Total Authors: 5
Affiliation:
[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
Total Affiliations: 2
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 112, p. 499-508, JUN 2018.
Web of Science Citations: 1
Abstract

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)

FAPESP's process: 98/14138-2 - Center for Structural Molecular Biotechnology
Grantee:Glaucius Oliva
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC