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title Botryosphaeriales fungi produce extracellular enzymes with biotechnological potential
authors Esteves, A.C.; Saraiva, M.; Correia, A.; Alves, A.
author full name Esteves, Ana Cristina; Saraiva, Marcia; Correia, Antonio; Alves, Artur
title Botryosphaeriales fungi produce extracellular enzymes with biotechnological potential
nationality internacional
source Canadian Journal of Microbiology
language English
document type Article
author keywords cell-wall-degrading enzymes; proteases; lipases; cellulases; thermostable enzymes
keywords plus SOLID-STATE FERMENTATION; MACROPHOMINA-PHASEOLINA; THERMOPHILIC FUNGI; SECRETOME ANALYSIS; RHODINA MAMB-05; PECTIC ENZYMES; LACCASE; ENDOPHYTES; LIPASE; BIOREFINERIES
abstract Phytopathogenic fungi are known for producing an arsenal of extracellular enzymes whose involvement in the infection mechanism has been suggested. However, these enzymes are largely unknown and their biotechnological potential also remains poorly understood. In this study, the production and thermostability of extracellular enzymes produced by phytopathogenic Botryosphaeriaceae was investigated. Hydrolytic and oxidative activities were detected and quantified at different temperatures. Most strains (70%; 37/53) were able to produce simultaneously cellulases, laccases, xylanases, pectinases, pectin lyases, amylases, lipases, and proteases. Surprisingly for mesophilic filamentous fungi, several enzymes proved to be thermostable: cellulases from Neofusicoccum mediterraneum CAA 001 and from Dothiorella prunicola CBS 124723, lipases from Diplodia pinea (CAA 015 and CBS 109726), and proteases from Melanops tulasnei CBS 116806 were more active at 70 degrees C than at any of the other temperatures tested. In addition, lipases produced by Diplodia pinea were found to be significantly more active than any other known lipase from Botryosphaeriales. The thermal activity profile and the wide array of activities secreted by these fungi make them optimal producers of biotechnologically relevant enzymes that may be applied in the food and the health industries (proteases), the pulp-and-paper and biofuel industries (cellulases), or even in the detergent industry (lipases, proteases, amylases, and cellulases).
author address [Esteves, Ana Cristina] Univ Aveiro, Dept Biol, P-3810193 Aveiro, Portugal; Univ Aveiro, Ctr Environm & Marine Studies, P-3810193 Aveiro, Portugal
reprint address Esteves, AC (reprint author), Univ Aveiro, Dept Biol, P-3810193 Aveiro, Portugal.
e-mail address acesteves@ua.pt
researcherid number Alves, Artur/C-3645-2008
orcid number Alves, Artur/0000-0003-0117-2958
funding agency and grant number FEDER (Fundo Europeu de Desenvolvimento Regional) through the COMPETE Program; FCT (Fundacao para a Ciencia e a Tecnologia) within the research project PROMETHEUS [PTDC/AGR-CFL/113831/2009, FCOMP-01-0124-FEDER-014096]; Pest [PEst-C/MAR/LA0017/2013]; FCT [BPD/38008/2007]
funding text This study was partially supported by FEDER (Fundo Europeu de Desenvolvimento Regional) funding through the COMPETE Program and by national funding through FCT (Fundacao para a Ciencia e a Tecnologia) within the research project PROMETHEUS (PTDC/AGR-CFL/113831/2009 and FCOMP-01-0124-FEDER-014096) and Pest (PEst-C/MAR/LA0017/2013). FCT also financed the postdoctoral fellowship of Ana Cristina Esteves (BPD/38008/2007).
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cited reference count 55
publisher CANADIAN SCIENCE PUBLISHING, NRC RESEARCH PRESS
publisher city OTTAWA
publisher address 65 AURIGA DR, SUITE 203, OTTAWA, ON K2E 7W6, CANADA
issn 0008-4166
iso source abbreviation CAN J MICROBIOL
publication date Can. J. Microbiol.
year published 2014
volume 60
issue 5
beginning page 332
ending page 342
digital object identifier (doi) 10.1139/cjm-2014-0134
page count 11
web of science category Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology; Immunology; Microbiology
subject category Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology; Immunology; Microbiology
unique article identifier AH2RX
link http://dx.doi.org/10.1139/cjm-2014-0134