Evaluation of solid and submerged fermentations for the production of cyclodextrin glycosyltransferase by Paenibacillus campinasensis H69-3 and characterization of crude enzyme

Cyclodextrin glycosyltransferase (CGTase) is an enzyme that produces cyclodextrins from starch by an intramolecular transglycosylation reaction. Cyclodextrins have been shown to have a number of applications in the food, cosmetic, pharmaceutical, and chemical industries. In the current study, the production of CGTase by Paenibacillus campinasensis strain H69-3 was examined in submerged and solid-state fermentations. P. campinasensis strain H69-3 was isolated from the soil, which grows at 45 C, and is a Gram-variable bacterium. Different substrate sources such as wheat bran, soybean bran, soybean extract, cassava solid residue, cassava starch, corn starch, and other combinations were used in the enzyme production. CGTase activity was highest in submerged fermentations with the greatest production observed at 48-72 h. The physical and chemical properties of CGTase were determined from the crude enzyme produced from submerged fermentations. The optimum temperature was found to be 70-75 degrees C, and the activity was stable at 55 degrees C for 1 h. The enzyme displayed two optimum pH values, 5.5 and 9.0 and was found to be stable between a pH of 4.5 and 11.0.

Microbial rennet produced by Mucor miehei in solid-state and submerged fermentation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Studies on productivity and characterization of polygalacturonase from Aspergillus giganteus submerged culture using citrus pectin and orange waste

Polygalacturonases are part of the group of enzymes involved in pectin degradation. The aim of this work was to investigate some of the factors affecting polygalacturonase production by an Aspergillus giganteus strain and to characterize this pectinolytic activity. Several carbon sources, both pure substances and natural substrates, were tested in standing cultures, and the best results were obtained with orange bagasse and purified citrus pectin. on citrus pectin as sole carbon source, the highest extracellular activity (9.5 U/ml and 40.6 U/mg protein) was obtained in 4.5-day-old cultures shaken at 120 rpm, pH 3.5 and 30 degrees C, while on orange bagasse, the highest extracellular activity (48.5 U/ml and 78.3 U/mg protein) was obtained in 3.5-day-old cultures shaken at 120 rpm, pH 6.0 and 30 degrees C. Optimal polygalacturonase activity was observed in assays conducted at pH 5.5-6.5 and 55-60 degrees C. The activity showed good thermal stability, with half-lives of 90 and 30 min when incubated at 55 and 60 degrees C, respectively. High stability was observed from pH 4.5 to 8.5; more than 90% of the activity remained after 24 h in this pH range.

Purification and characterization of the exopolygalacturonase produced by Aspergillus giganteus in submerged cultures

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Use of sugarcane bagasse and grass hydrolysates as carbon sources for xylanase production by Bacillus circulans D1 in submerged fermentation

The use of sugarcane bagasse and grass as low cost raw material for xylanase production by Bacillus circulans D1 in submerged fermentation was investigated. The microorganism was cultivated in a mineral medium containing hydrolysate of bagasse or grass as carbon source. High production of enzyme was obtained during growth in media with bagasse hydrolysates (8.4 U/mL) and in media with grass hydrolysates (7.5 U/mL). Xylanase production in media with hydrolysates was very close to that obtained in xylan containing media (7.0 U/ mL) and this fact confirm the feasibility of using this agro-industrial byproducts by B. circulans D1 as an alternative to save costs on the enzyme production process. (c) 2005 Elsevier Ltd. All rights reserved.

Localization and partial characterization of thermostable glucoamylase produced by newly isolated Thermomyces lanuginosus TO3 in submerged fermentation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Influence of Different Substrates on the Production of a Mutant Thermostable Glucoamylase in Submerged Fermentation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Pectinase production by a Brazilian thermophilic fungus Thermomucor indicae-seudaticae N31 in solid-state and submerged fermentation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Production and characterization of polygalacturonase from thermophilic Thermoascus aurantiacus on submerged fermentation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Optimization of xylanase production by Bacillus circulans D1 in submerged fermentation using response surface methodology

In this work, a 3(3) factorial design was performed with the aim of optimizing the culture conditions for xylanase production by an alkalophilic thermophilic strain of Bacillus circulans, using response surface methodology. The variables involved in this study were xylan concentration (X-1), pH (X-2) and cultivation time (X-3). The optimal response region was approached without using paths of steepest ascent. Statistical analysis of results showed that, in the range studied, only pH did not have a significant effect on xylanase production. A second-order model was proposed to represent the enzymic activity as a function of xylan concentration (X-1) and cultivation time (X-3). The optimum xylan concentration and cultivation time were 5 g/l and 48 h, respectively. Under these conditions, the model predicted a xylanase activity of 19.1 U/ml. (C) 2002 Elsevier B.V. Ltd. All rights reserved.

Production and partial characterization of serine and metallo peptidases secreted by Aspergillus fumigatus Fresenius in submerged and solid state fermentation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Phosphorus, nitrogen, and carbon contents of macrophytes in lakes lateral to a tropical river (Paranapanema River, São Paulo, Brazil)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Purification and characterization of polygalacturonase produced by thermophilic Thermoascus aurantiacus CBMAI-756 in submerged fermentation

An extracellular polygalacturonase was isolated from 5-day culture filtrates of Thermoascus aurantiacus CBMAI-756 and purified by gel filtration and ion-exchange chromatography. The enzyme was maximally active at pH 5.5 and 60-65 degrees C. The apparent K (m) with citrus pectin was 1.46 mg/ml and the V (max) was 2433.3 mu mol/min/mg. The apparent molecular weight of the enzyme was 30 kDa. The enzyme was 100% stable at 50 degrees C for 1 h and showed a half-life of 10 min at 60 degrees C. Polygalacturonase was stable at pH 5.0-5.5 and maintained 33% of initial activity at pH 9.0. Metal ions, such as Zn+2, Mn+2, and Hg+2, inhibited 50, 75 and 100% of enzyme activity. The purified polygalacturonase was shown to be an endo/exo-enzyme, releasing mono, di and tri-galacturonic acids within 10 min of hydrolysis.