Secretion of endoglucanases and β-glucosidases by Penicillium echinulatum 9A02S1 in presence of different carbon sources

Zampieri, Denise; Guerra, Letícia; Camassola, Marli; Dillon, Aldo José Pinheiro

doi:10.1016/j.indcrop.2013.08.045

Cited by 15 publications

(8 citation statements)

References 25 publications

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“…The cultures were grown during 6 days at 28 °C and 200 rpm. The dosage of total cellulases activity was made according to Ghose (1986) [ 153 ] with modifications proposed by Camassola and Dilon (2012) [ 154 ]. In summary, 50 μl of the crude supernatants were incubated with a strip of filter paper (1.0 × 0.6 cm) or carboxymethyl cellulose (1%) in 100 μl of sodium acetate buffer, 0.05 M, pH 5.0, during 120 min at 50 °C.…”

Section: Methodsmentioning

confidence: 99%

Ceratocystis cacaofunesta genome analysis reveals a large expansion of extracellular phosphatidylinositol-specific phospholipase-C genes (PI-PLC)

et al. 2018

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BackgroundThe Ceratocystis genus harbors a large number of phytopathogenic fungi that cause xylem parenchyma degradation and vascular destruction on a broad range of economically important plants. Ceratocystis cacaofunesta is a necrotrophic fungus responsible for lethal wilt disease in cacao. The aim of this work is to analyze the genome of C. cacaofunesta through a comparative approach with genomes of other Sordariomycetes in order to better understand the molecular basis of pathogenicity in the Ceratocystis genus.ResultsWe present an analysis of the C. cacaofunesta genome focusing on secreted proteins that might constitute pathogenicity factors. Comparative genome analyses among five Ceratocystidaceae species and 23 other Sordariomycetes fungi showed a strong reduction in gene content of the Ceratocystis genus. However, some gene families displayed a remarkable expansion, in particular, the Phosphatidylinositol specific phospholipases-C (PI-PLC) family. Also, evolutionary rate calculations suggest that the evolution process of this family was guided by positive selection. Interestingly, among the 82 PI-PLCs genes identified in the C. cacaofunesta genome, 70 genes encoding extracellular PI-PLCs are grouped in eight small scaffolds surrounded by transposon fragments and scars that could be involved in the rapid evolution of the PI-PLC family. Experimental secretome using LC–MS/MS validated 24% (86 proteins) of the total predicted secretome (342 proteins), including four PI-PLCs and other important pathogenicity factors.ConclusionAnalysis of the Ceratocystis cacaofunesta genome provides evidence that PI-PLCs may play a role in pathogenicity. Subsequent functional studies will be aimed at evaluating this hypothesis. The observed genetic arsenals, together with the analysis of the PI-PLC family shown in this work, reveal significant differences in the Ceratocystis genome compared to the classical vascular fungi, Verticillium and Fusarium. Altogether, our analyses provide new insights into the evolution and the molecular basis of plant pathogenicity.Electronic supplementary materialThe online version of this article (10.1186/s12864-018-4440-4) contains supplementary material, which is available to authorized users.

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Section: Methodsmentioning

confidence: 99%

Ceratocystis cacaofunesta genome analysis reveals a large expansion of extracellular phosphatidylinositol-specific phospholipase-C genes (PI-PLC)

et al. 2018

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“…Irshad et al (2012) reported the characterization of exo 1,4-β glucanase from Tricoderma viride MBL by culturing the organism in solid-state fermentation using orange peel waste as substrate [96]. Fusarium oxysporum , Bacillus subtilis , Penicillium echinulatum , Sclerotium rolfsii have also been reported to produce high levels of endo and exoglucanase when grown on biomass sources [93,97,98,99].…”

Section: Industrial Enzymesmentioning

confidence: 99%

A Review on Bioconversion of Agro-Industrial Wastes to Industrially Important Enzymes

Ravindran¹,

Hassan²,

Williams³

et al. 2018

Bioengineering

226

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Agro-industrial waste is highly nutritious in nature and facilitates microbial growth. Most agricultural wastes are lignocellulosic in nature; a large fraction of it is composed of carbohydrates. Agricultural residues can thus be used for the production of various value-added products, such as industrially important enzymes. Agro-industrial wastes, such as sugar cane bagasse, corn cob and rice bran, have been widely investigated via different fermentation strategies for the production of enzymes. Solid-state fermentation holds much potential compared with submerged fermentation methods for the utilization of agro-based wastes for enzyme production. This is because the physical–chemical nature of many lignocellulosic substrates naturally lends itself to solid phase culture, and thereby represents a means to reap the acknowledged potential of this fermentation method. Recent studies have shown that pretreatment technologies can greatly enhance enzyme yields by several fold. This article gives an overview of how agricultural waste can be productively harnessed as a raw material for fermentation. Furthermore, a detailed analysis of studies conducted in the production of different commercially important enzymes using lignocellulosic food waste has been provided.

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“…Also Aliyah et al (2017) observed a maximal β-glucosidase activity (91.67 and 85.01 U.mL -1 ) when A. niger was cultivate using sugarcane bagasse and corn cob for 6 days, respectively. However, Aspergillus and Penicillium species, are considered greater β-glucosidase producers (Zampieri et al 2013).…”

Section: Determination Of Physico-chemical Properties Of Enzymesmentioning

confidence: 99%

“…Hemicellulose is a branched heteropolymer of pentoses and/or hexoses and various types of uronic acids residues linked by -1,4 / -1,3 glucosidic bonds. The term hollocellulose comprises the cellulose and hemicelluloses of plant cell wall linked together (Gottschalk et al, 2010;Zampieri et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…The complete hydrolysis of cellulose is finalized through the action of -glucosidase (E.C. 3.2.1.21), which cleaves cellooligosaccharides and cellobiose to glucose (Zampieri et al, 2013;Singhania et al, 2013). Considering the hemicellulose fraction, endo-1,4-β-D-endoxylanases (EC 3.2.1.8) (Terrasan et al, 2010;Kirikyali and Connerton, 2014).…”

Section: Introductionmentioning

confidence: 99%

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Trichoderma atroviride 102C1: A promising mutant strain for the production of a -glucosidase, -xylosidase and -L-arabinofuranosidase activities using agroindustrial by-products

Silva¹,

Grigorevski-Lima²,

Bon³

et al. 2018

Afr. J. Biotechnol.

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Holocellulolytic accessory enzymes are very important in assisting hydrolysis of biomass. The use of these enzymes in the enzymatic hydrolysis of plant biomass is very important for obtaining building blocks in the concept of biorefinery. In previous studies, the mutant strain Trichoderma atroviride 102C1 was tested for production of endoglucanases, FPases and endoxylanases. This study aimed at evaluating the efficiency in holocellulolytic accessories enzymes production (-glucosidase, xylosidase and -L-arabinofuranosidase) by Trichoderma atroviride 102C1 using different lignocelluloses biomass as substrates. Accessory enzymes production was carried out in Erlenmeyer flasks containing Mandels salt medium, supplemented with different concentrations of sugarcane bagasse (SCB) and corn steep liquor (CSL), according to a Central Composite Rotational Design (CCRD). The fermentation system was incubated under agitation for 2 days / 28°C. For pH and temperature profile studies, a new CCRD was carried out. The best condition common to all enzymes, 55.4 U.mL-1 (β-glucosidase), 10.8 U.mL-1 (β-xylosidase) and 143.23 U.mL-1 (α-L-arabinofuranosidase), was observed when 2.5% (w/v) sugarcane bagasse (SCB) and 1.26% (w/v) of corn steep liquor (CSL) were used. All enzymes presented acidophilic characteristic in two different temperatures (44 and 55°C). The optimal profile characteristic for β-glucosidase and β-xylosidase activities were pH 5.0 and 3.0, respectively, both at 55°C, while for α-L-arabinofuranosidase it was pH 3.6 at 44°C. This study demonstrated the potential of T. atroviride 102C1 to produce three important holocellulolytic accessory enzymes in the presence of SCB and CSL, suggesting its use for enzymatic hydrolysis of lignocellulosic biomass.

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Secretion of endoglucanases and β-glucosidases by Penicillium echinulatum 9A02S1 in presence of different carbon sources

Cited by 15 publications

References 25 publications

Ceratocystis cacaofunesta genome analysis reveals a large expansion of extracellular phosphatidylinositol-specific phospholipase-C genes (PI-PLC)

Ceratocystis cacaofunesta genome analysis reveals a large expansion of extracellular phosphatidylinositol-specific phospholipase-C genes (PI-PLC)

A Review on Bioconversion of Agro-Industrial Wastes to Industrially Important Enzymes

Trichoderma atroviride 102C1: A promising mutant strain for the production of a -glucosidase, -xylosidase and -L-arabinofuranosidase activities using agroindustrial by-products

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