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Production of Β-Glucosidase on Solid-State Fermentation by Lichtheimia Ramosa in Agroindustrial Residues

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Production of Β-Glucosidase on Solid-State Fermentation by Lichtheimia Ramosa in Agroindustrial Residues Electronic Journal of Biotechnology 18 (2015) 314–319 Contents lists available at ScienceDirect Electronic Journal of Biotechnology Production of β-glucosidase on solid-state fermentation by Lichtheimia ramosa in agroindustrial residues: Characterization and catalytic properties of the enzymatic extract Nayara Fernanda Lisboa Garcia a, Flávia Regina da Silva Santos a, Fabiano Avelino Gonçalves b, Marcelo Fossa da Paz a, Gustavo Graciano Fonseca b, Rodrigo Simões Ribeiro Leite a,⁎ a Laboratório de Enzimologia e Processos Fermentativos, Faculdade de Ciências Biológicas e Ambientais, Universidade Federal da Grande Dourados, Dourados, MS, Brazil b Laboratório de Bioengenharia, Faculdade de Engenharia, Universidade Federal da Grande Dourados, Dourados, MS, Brazil article info abstract Article history: Background: β-Glucosidases catalyze the hydrolysis of cellobiose and cellodextrins, releasing glucose as the main Received 18 February 2015 product. This enzyme is used in the food, pharmaceutical, and biofuel industries. The aim of this work is to Accepted 15 May 2015 improve the β-glucosidase production by the fungus Lichtheimia ramosa by solid-state fermentation (SSF) Available online 27 June 2015 using various agroindustrial residues and to evaluate the catalytic properties of this enzyme. Results: A high production of β-glucosidase, about 274 U/g of dry substrate (or 27.4 U/mL), was obtained by Keywords: cultivating the fungus on wheat bran with 65% of initial substrate moisture, at 96 h of incubation at 35°C. The Cellobiase enzymatic extract also exhibited carboxymethylcellulase (CMCase), xylanase, and β-xylosidase activities. The Cellulases and hemicellulases β – Industrial enzymes optimal activity of -glucosidase was observed at pH 5.5 and 65°C and was stable over a pH range of 3.5 10.5. Microbial enzymes The enzyme maintained its activity (about 98% residual activity) after 1 h at 55°C. The enzyme was subject to reversible competitive inhibition with glucose and showed high catalytic activity in solutions containing up to 10% of ethanol. Conclusions: β-Glucosidase characteristics associated with its ability to hydrolyze cellobiose, underscore the utility of this enzyme in diverse industrial processes. ©2015Pontificia Universidad Católica de Valparaíso. Production and hosting by Elsevier B.V. All rights reserved. 1. Introduction enzymatic hydrolysis of cellulose in order to obtain fermentable sugars and the production of functional foods derived from soy. The The pronounced scarcity of fossil fuels related to environmental enzyme is also used in the juice and beverage industry, where it can problems resulting from their processing and consumption has improve the aromatic quality of wine and other grape derivatives [3]. prompted the search for alternative sources of biofuels and renewable The obtainment of industrial enzymes in a sustainable and energy. This in turn, has generated significant interest in the use of economically viable manner requires the pursuit of renewable cellulases and other enzymes to convert vegetal biomass into raw materials and processes at low cost. The use of solid-state fermentable sugars [1]. fermentation (SSF) can reduce the environmental impact and Enzymatic hydrolysis of cellulose to glucose requires at least add value to the by-products of agroindustry [4]. The iterative three different enzymes including endo-glucanases (EC 3.2.1.4), improvement and advantages of SSF have been described in several that internally hydrolyze cellulose chains, reducing its degree of reports, which studied the influence of different cultivation polymerization; exo-glucanases (EC 3.2.1.91) that attack the parameters on the production of microbial enzymes [5,6].The non-reducing and reducing extremities of cellulose, releasing advantages of SSF include the simplicity of growth conditions, because cellobiose; and β-glucosidases (EC 3.2.1.21) that hydrolyze they are very similar to the environmental systems where many cellobiose and oligosaccharides, thereby releasing glucose [2]. microorganisms develop (especially filamentous fungi); the reduced The ability of β-glucosidase to utilize different glycosidic substrates energy consumption, and that complex equipment or sophisticated renders it suitable for several industrial processes, including the control systems are not required. The method also results in higher levels of productivity and low catabolite repression, and favors ⁎ Corresponding author. increased stability of the secreted enzymes [7]. E-mail address: [email protected] (R.S.R. Leite). In general, the industrial applicability of an enzyme is closely related Peer review under responsibility of Pontificia Universidad Católica de Valparaíso. to the cost of its production and physicochemical characteristics. The http://dx.doi.org/10.1016/j.ejbt.2015.05.007 0717-3458/© 2015 Pontificia Universidad Católica de Valparaíso. Production and hosting by Elsevier B.V. All rights reserved. N.F.L. Garcia et al. / Electronic Journal of Biotechnology 18 (2015) 314–319 315 production costs can be reduced by screening hyper producer 2.6. Characterization of β-glucosidase produced by the fungus L. ramosa strains, associated with the cultivation process optimized in low-cost mediums [3]. Previous work conducted by our Research Group 2.6.1. Effect of pH revealed high β-glucosidase production by the fungus Lichtheimia The optimum pH for β-glucosidase activity was determined by ramosa by SSF using several lignocellulosic materials [6,8]. This study measuring the activity at 50°C at different pH values (3.0–8.0), with aimed to optimize the β-glucosidase production by this fungus by SSF. increments of 0.5, using 0.1 M citrate–phosphate buffer solution. The The β-glucosidase produced was biochemically characterized and the pH stability was determined incubating the enzyme for 24 h at 25°C at catalytic properties of the enzymatic extract were evaluated. different pH values, appropriately diluted with buffer solutions: 0.1 M citrate–phosphate (pH 3.0–8.0), 0.1 M Tris–HCl (pH 8.0–8.5), and 0.1 M glycine NaOH (pH 8.5–10.5), with increments of 0.5, adopting 2. Material and methods as 100% the highest value of residual activity obtained after the samples treatment. The residual activity was determined under 2.1. Microorganism optimal conditions of pH and temperature. The filamentous fungus L. ramosa was isolated from sugarcane bagasse provided by São Fernando Açúcar e Álcool Ltda., Dourados, 2.6.2. Effect of temperature β MS, Brazil [8]. The microorganism was maintained on Sabouraud The optimum temperature for -glucosidase activity was obtained Dextrose Agar medium; after growth at 28°C for 48 h, the strain was by determining the enzymatic activity over a temperature range of – stored at 4°C. 30°C 75°C, with increments of 5°C, at the respective optimum pH. Thermostability was determined by incubating the enzyme for 1 h at different temperatures (30°C–70°C), with increments of 5°C, adopting 2.2. Inoculum as 100% the highest value of residual activity obtained after the samples treatment. The residual activities were measured under The organism was cultivated in inclined 250 mL Erlenmeyer flasks optimal conditions of pH and temperature. containing 40 mL of Sabouraud Dextrose Agar and maintained for 48°C h at 28°C. A fungal suspension was obtained by adding 25 mL of 2.6.3. Effect of glucose and ethanol on β-glucosidase activity nutrient solution and gently scraping the surface of the culture. The The enzymatic activity was quantified with the addition of glucose or nutrient solution was composed of 0.1% ammonium sulfate, 0.1% ethanol at different concentrations in the reaction mixture (0–200 mM magnesium sulfate heptahydrate, and 0.1% ammonium nitrate (w/v) glucose or 0–30% of ethanol). The activities were measured under [9]. As inoculum, 5 mL of this suspension was transferred to each optimal conditions of pH and temperature. 250 mL Erlenmeyer flask containing lignocellulosic material as substrates. 2.7. Catalytic potential of the enzymatic extract 2.3. Solid-state fermentation (SSF) The CMCase and xylanase activities were quantified using 3% carboxymethylcellulose (Sigma C5678) and 1% xylan (Sigma The enzyme was produced by cultivating the fungus in 250 mL Birch-Wood), respectively. The reducing sugar released was quantified Erlenmeyer flasks containing 5 g of substrate (wheat bran, soy bran, by the DNS method [11].Theβ-xylosidase activity was measured with corn cob, corn straw, rice peel, or sugarcane bagasse), previously the synthetic substrate p-nitrophenyl-β-D-xylopyranoside (4 mM, washed and dried at 60°C for 24 h. The optimal substrate for enzyme Sigma), following the methodology described in Section 2.5. The production was used in subsequent steps to evaluate the effects of potential to hydrolyze cellobiose was evaluated with a glucose-oxidase varying the pH of cultivation medium, moisture content, temperature, kit (Glucose-PP Analisa). Specifically, 100 μL of the enzymatic extract and time of cultivation. The parameter selected in each step was used was added to 0.9 mL of 50 mM sodium acetate buffer containing 0.5% for further cultivation, in an iterative strategy designed to optimize cellobiose (Fluka). One unit of enzymatic activity was defined as the the fermentation process for β-glucosidase production. All material amount of enzyme capable of producing 1 μmol of product per min of was previously autoclaved for 20 min at 121°C, and the experiments reaction. were performed in duplicate. 3. Results and discussion 2.4. Enzyme extraction 3.1. Production of β-glucosidase by solid-state fermentation The extraction of the enzyme from the fermented substrate was 3.1.1. Selection of substrates for β-glucosidase production carried out by adding 50 mL of distilled water, and constantly shaking Among the tested substrates, the cultivation of the fungus L. ramosa at 100 rpm for 1 h. The sample was filtered and centrifuged at in wheat bran provided higher β-glucosidase production (162.2 U/g 3000 × g for 5 min. The supernatant was considered the enzymatic or 16.22 U/mL) (Table 1).
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