Regulation of xylanase in Aspergillus phoenicis: a physiological and molecular approach

Rizzatti, Ana Carolina Segato; Freitas, Fernanda Zanolli; Bertolini, Maria Célia; Peixoto-Nogueira, Simone C.; Terenzi, Héctor Francisco; Jorge, João Atı́lio; Polizeli, Maria de Lourdes Teixeira de Moraes

doi:10.1007/s10295-007-0290-9

Cited by 12 publications

(4 citation statements)

References 40 publications

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“…Xylanases production by A. phoenicis was shown positively affected by xylan, xylose and b -methylxyloside, similarly to the cases of other fungi belonging to the Aspergillus genus such as Aspergillus sydowii and A. tubingensis , as studied and discussed by Rizzatti et al [164]. This study also demonstrated that the levels of production of xylanase by A. phoenics , decreased when glucose was added to the inducers xylan or xylose, similarly to A. sydowii whose xylanase production is inhibited by glucose [165].…”

Section: Regulation Of Production Of Cellulases and Hemicellulases Inmentioning

confidence: 81%

Regulation of Cellulase and Hemicellulase Gene Expression in Fungi

Giacobbe²,

2013

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Research on regulation of cellulases and hemicellulases gene expression may be very useful for increasing the production of these enzymes in their native producers. Mechanisms of gene regulation of cellulase and hemicellulase expression in filamentous fungi have been studied, mainly in Aspergillus and Trichoderma. The production of these extracellular enzymes is an energy-consuming process, so the enzymes are produced only under conditions in which the fungus needs to use plant polymers as an energy and carbon source. Moreover, production of many of these enzymes is coordinately regulated, and induced in the presence of the substrate polymers. In addition to induction by mono- and oligo-saccharides, genes encoding hydrolytic enzymes involved in plant cell wall deconstruction in filamentous fungi can be repressed during growth in the presence of easily metabolizable carbon sources, such as glucose. Carbon catabolite repression is an important mechanism to repress the production of plant cell wall degrading enzymes during growth on preferred carbon sources. This manuscript reviews the recent advancements in elucidation of molecular mechanisms responsible for regulation of expression of cellulase and hemicellulase genes in fungi.

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Section: Regulation Of Production Of Cellulases and Hemicellulases Inmentioning

confidence: 81%

Regulation of Cellulase and Hemicellulase Gene Expression in Fungi

Giacobbe²,

2013

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“…Interestingly, Herrera-Herrera et al [ 50 ] showed that in Cellulomonas flavigena , an actinobacteria with special interest for its ability to degrade cellulose and hemicellulose, addition of exogenous cAMP in repressor culture medium decreased catabolite repression, while supplementation enhanced cellobiohydrolase production. Similarly, Rizzati et al [ 51 ] showed in Aspergillus phoenicis that repression of xylanase expression by glucose was partially reversed by addition of cAMP or dbcAMP.…”

Section: Discussionmentioning

confidence: 93%

Evidence of cAMP involvement in cellobiohydrolase expression and secretion by Trichoderma reesei in presence of the inducer sophorose

et al. 2015

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BackgroundThe signaling second messenger cyclic AMP (cAMP) regulates many aspects of cellular function in all organisms. Previous studies have suggested a role for cAMP in the regulation of gene expression of cellulolytic enzymes in Trichoderma reesei (anamorph of Hypocrea jecorina).MethodsThe effects of cAMP in T. reesei were analyzed through both activity and expression of cellulase, intracellular cAMP level measurement, western blotting, indirect immunofluorescence and confocal microscopy.ResultsTo elucidate the involvement of cAMP in the cellulase expression, we analyzed the growth of the mutant strain ∆acy1 and its parental strain QM9414 in the presence of the inducers cellulose, cellobiose, lactose, or sophorose, and the repressor glucose. Our results indicated that cAMP regulates the expression of cellulase in a carbon source-dependent manner. The expression cel7a, and cel6a genes was higher in the presence of sophorose than in the presence of cellulose, lactose, cellobiose, or glucose. Moreover, intracellular levels of cAMP were up to four times higher in the presence of sophorose compared to other carbon sources. Concomitantly, our immunofluorescence microscopy and western blot data suggest that in the presence of sophorose, cAMP may regulate secretion of cellulolytic enzymes in T. reesei.ConclusionsThese results allow us to better understand the role of cAMP and expand our knowledge on the signal transduction pathways involved in the regulation of cellulase expression in T. reesei. Finally, our data may help develop new strategies to improve the expression of cel7a and cel6a genes, and therefore, favor their application in several biotechnology fields.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-015-0536-z) contains supplementary material, which is available to authorized users.

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“…Aspergillus phoenicis, a thermotolerant fungus, has successfully been used in our laboratory to produce various enzymes with biotechnological applications [11,12]. This fungus was previously isolated from sugar cane bagasse and it has demonstrated high xylanase and b-xylosidase yields, as reported.…”

Section: Introductionmentioning

confidence: 95%

A novel glucoamylase activated by manganese and calcium produced in submerged fermentation by Aspergillus phoenicis

Benassi

Pasin

Facchini

et al. 2013

J. Basic Microbiol.

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This study investigates the production of glucoamylase from Aspergillus phoenicis in Machado Benassi (MB) medium using 1% maltose as carbon source. The maximum amylase activity was observed after four days of cultivation, on static conditions at 30 °C. Glucoamylase production was induced by maltose and inhibited by different glucose concentrations. The optimum of temperature and pH were 60-65 °C, and 4.5 or 5.0 to sodium acetate and Mcllvaine buffers, respectively. It was observed that the enzyme was totally stable at 30-65 °C for 1 h, and the pH range was 3.0-6.0. The enzyme was mainly activated by manganese (176%), and calcium (130%) ions. The products of starch hydrolysis were analyzed by thin layer chromatography and after 3 h, only glucose was detected, characterizing the amylolytic activity as a glucoamylase.

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Regulation of xylanase in Aspergillus phoenicis: a physiological and molecular approach

Cited by 12 publications

References 40 publications

Regulation of Cellulase and Hemicellulase Gene Expression in Fungi

Regulation of Cellulase and Hemicellulase Gene Expression in Fungi

Evidence of cAMP involvement in cellobiohydrolase expression and secretion by Trichoderma reesei in presence of the inducer sophorose

A novel glucoamylase activated by manganese and calcium produced in submerged fermentation by Aspergillus phoenicis

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