Optimization of xylanase production by Streptomyces sp. P12-137 using response surface methodology and central composite design

Response surface methodology and central composite design were used to optimize a biosynthesis medium for the production of xylanases by Streptomyces sp. P12-137 in submerged fermentation culture at pH 5.0, with wheat bran as substrate. The three variables involved in this research were the wheat bran, potassium nitrate and xylose concentrations. Statistical analysis of the results showed that, in the range studied, xylose and potassium nitrate concentrations had a significant effect on xylanase production. The optimized biosynthesis medium contained (in %, w/v): wheat bran 1.0, KNO3 1.0, xylose 0.5. This medium resulted in a 3-fold increased level of the xylanase (27.77 UA/ml) production compared to the initial level (8.30 UA/ml) after 120 h of fermentation, whereas the value predicted by the quadratic model was 26.45 UA/ml

Evaluation of cell disruption for partial isolation of intracellular pyruvate decarboxylase enzyme by silver nanoparticles method

Candida tropicalis TISTR 5350 was used in the comparison of seven concentration levels of silver nanoparticles (0, 5, 10, 15, 20, 25, and 30 μg ml–1) for cell disruption methods. The optimized cell disruption strategy was selected based on the optimal protein yield and biological activity. The maximum volumetric and specific pyruvate decarboxylase (PDC, EC 4.1.1.1) activities (0.53±0.05 U ml–1 and 0.17±0.02 U mg–1 protein, respectively) were observed at 15 μg ml–1 silver nanoparticles. The silver nanoparticle concentration level of 15 μg ml–1 was investigated further by comparing the reaction mixtures at different time intervals of 0, 1, 2, 3, 4, 5, and 6 min. The result showed that the highest specific PDC activity of 0.39±0.01 U mg–1 protein was obtained from mixing for 3 min. This was not significantly different (P≤0.05) from other mixing time intervals

Xylanase and β-xylosidase production by Aspergillus ochraceus: new perspectives for the application of wheat straw autohydrolysis liquor

The xylanase biosynthesis is induced by its substrate—xylan. The high xylan content in some wastes such as wheat residues (wheat bran and wheat straw) makes them accessible and cheap sources of inducers to be mainly applied in great volumes of fermentation, such as those of industrial bioreactors. Thus, in this work, the main proposal was incorporated in the nutrient medium wheat straw particles decomposed to soluble compounds (liquor) through treatment of lignocellulosic materials in autohydrolysis process, as a strategy to increase and undervalue xylanase production by Aspergillus ochraceus. The wheat straw autohydrolysis liquor produced in several conditions was used as a sole carbon source or with wheat bran. The best conditions for xylanase and β-xylosidase production were observed when A. ochraceus was cultivated with 1% wheat bran added of 10% wheat straw liquor (produced after 15 min of hydrothermal treatment) as carbon source. This substrate was more favorable when compared with xylan, wheat bran, and wheat straw autohydrolysis liquor used separately. The application of this substrate mixture in a stirred tank bioreactor indicated the possibility of scaling up the process to commercial production.This work was supported by Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP/Brazil), Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq/Brazil), National System for Research on Biodiversity (SISBIOTA-Brazil, CNPq 563260/2010-6/FAPESP no. 2010/52322-3), and Fundacao para a Ciencia e a Tecnologia (FCT/Portugal)

PRODUCTION AND CHARACTERIZATION OF THERMOPHILIC CARBOXYMETHYL CELLULASE SYNTHESIZED BY Bacillus sp. GROWING ON SUGARCANE BAGASSE IN SUBMERGED FERMENTATION

Abstract The production and characterization of cellulase from thermophilic strain Bacillus sp. C1AC5507 was studied. For enzyme production, sugarcane bagasse was used as carbon source. The produced carboxymethyl cellulase (CMCase) had a molecular weight around 55 kDa and its activity varied between 0.14 and 0.37 IU mL-1 in conditions predicted by Response Surface Methodology. The optimum temperature and pH for the CMCase production were 70 °C and 7.0, respectively. The enzyme activity was inhibited mostly by Cu+2 and activated mostly by Co+2, Mn2+, Ca+2 and Fe+3. Our findings provide a contribution to the use of natural wastes such as sugarcane bagasse as substrate for growth and production of thermophilic CMCase. Further optimization to increase the production of cellulase enables the use in industrial applications