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Synergistic action of thermophilic pectinases for pectin bioconversion into D-galacturonic acid

Flores-Fernández, Carol N; Cárdenas-Fernández, Max; Lye, Gary J; Ward, John M; (2022) Synergistic action of thermophilic pectinases for pectin bioconversion into D-galacturonic acid. Enzyme and Microbial Technology , 160 , Article 110071. 10.1016/j.enzmictec.2022.110071. Green open access

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Abstract

Large amounts of pectin-rich biomass are generated worldwide yearly, which can be hydrolysed by pectinases to obtain bio-based chemical building blocks such as D-galacturonic acid (GalA). The aim of this work was to investigate thermophilic pectinases and explore their synergistic application in the bioconversion of pectic substrates into GalA. Two exo-polygalacturonases (exo-PGs) from Thermotoga maritima (TMA01) and Bacillus licheniformis (BLI04) and two pectin methylesterases (PMEs) from Bacillus licheniformis (BLI09) and Streptomyces ambofaciens (SAM10) were cloned and expressed in Escherichia coli BL21 (DE3), purified and fully characterised. These pectinases exhibited optimum activity at temperatures above 50 °C and good stability at high temperature (40-90 °C) for up to 24 h. Exo-PGs preferred non-methylated substrates, suggesting that previous pectin demethylation by PMEs was necessary to achieve an efficient pectin monomerisation into GalA. Synergistic activity between PMEs and exo-PGs was tested using pectin from apple, citrus and sugar beet. GalA was obtained from apple and citrus pectin in a concentration of up to 2.5 mM after 4 h reaction at 50 °C, through the combined action of BLI09 PME with either TMA01 or BLI04 exo-PGs. Overall, this work contributes to expand the knowledge of pectinases from thermophiles and provides further insights into their application in the initial valorisation of sustainable pectin-rich biomass feedstocks.

Type: Article
Title: Synergistic action of thermophilic pectinases for pectin bioconversion into D-galacturonic acid
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1016/j.enzmictec.2022.110071
Publisher version: https://doi.org/10.1016/j.enzmictec.2022.110071
Language: English
Additional information: © 2022 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Keywords: D-galacturonic acid, Exo-polygalacturonases, Pectin biomass, Pectin methylesterases, Synergistic activity, Thermophilic enzymes
UCL classification: UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science > Dept of Biochemical Engineering
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL
URI: https://discovery.ucl.ac.uk/id/eprint/10151021
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