U Cm (u + cm)

Distribution by Scientific Domains

Selected Abstracts

Mn-peroxidase production by Panus tigrinus CBS 577.79: response surface optimisation and bioreactor comparison

Daniele Quaratino
Abstract This study reports the statistical optimisation through response surface methodology of the growth medium for Panus tigrinus manganese-dependent peroxidase (MnP) production in shaken culture. Three crucial variables, including carbon source, malonic acid and Mn2+, were optimised in a nitrogen-limited medium. Sucrose was the best carbon source for MnP production. Mn2+ ions and malonic acid significantly stimulated MnP production at an optimal concentration of 53 mg dm,3 and 8.2 mmol dm,3, respectively, resulting in 0.83 U cm,3. Further experiments were performed in lab-scale stirred tank (STR) and bubble-column (BCR) reactors using the previously optimised liquid medium. BCR proved to be more adequate than STR in supporting MnP production, leading to 3700 U dm,3 after 144 h with a productivity of 25.7 U dm,3 h,1. On a comparative basis with other production data in lab-scale reactors, these results appear to be compatible with scale transfer. Copyright © 2006 Society of Chemical Industry [source]

Oxygen transfer effects in ,-lactamase fermentation by Bacillus licheniformis in a glucose-based defined medium

nar «al
Abstract The effects of oxygen transfer on the ,-lactamase production by Bacillus licheniformis were investigated in a glucose-based defined medium. The experiments were conducted in 3.0 dm3 batch bioreactor systems at three different air inlet (QO/VR = 0.2, 0.5 and 1.0 vvm) and agitation rates (N = 250, 500 and 750 min,1). During the fermentation, the concentrations of the cell, glucose, by-products, ie organic and amino acids, oxygen transfer coefficients (KLa), yield coefficients, specific rates and oxygen uptake rates (OUR) were determined, in addition to ,-lactamase activities. The highest ,-lactamase activity was obtained at QO/VR = 0.5 vvm and N = 500 min,1 and at QO/VR = 0.2 vvm and N = 500 min,1 conditions, as caA = 90 U cm,3. The highest cell concentration was obtained as CX = 0.67 kg m,3 at QO/VR = 0.5 vvm and N = 750 min,1 and at QO/VR = 0.2 vvm and N = 750 min,1 conditions. The values of KLa increased with increasing agitation and aeration rates and varied between 0.007 and 0.044 s,1, and the OUR varied between 0.4 and 1.6 mol m,3 s,1. With increasing QO/VR and/or N, the DamkŲhler number (ie the oxygen transfer limitation) decreased owing to the increase in mass transfer coefficients (KLa). The highest instantaneous yield of cell on substrate (YX/S) and yield of cell on oxygen (YX/O) values were respectively obtained at 0.5 vvm and 500 min,1 conditions at t = 2 h as YX/S = 0.72 kg kg,1 and YX/O = 1.49 kg kg,1. The highest instantaneous yield of substrate on oxygen (YS/O) was obtained at 0.5 vvm and 750 min,1 conditions at t = 20 h as YS/O = 8.07 kg kg,1. Copyright © 2005 Society of Chemical Industry [source]

Recovery of lipase by adsorption at the n -hexadecane,water interface

Hui-Min Wang
Abstract A novel separation process based on the hydrophobic adsorption at the n -hexadecane,water interface was developed for the recovery of Acinetobacter radioresistens lipase from a pre-treated fermentation broth. In a mixture containing water, lipase and n -hexadecane, a water-in-oil emulsion was formed when the n -hexadecane-to-water ratio (o/w ratio) was larger than 3, and a large amount of lipase was found to be adsorbed at the interface. Compared with the oil-in-water emulsion (occurring when o/w ratio < 3), the water-in-oil emulsion generated smaller droplets and larger interfacial area, and was more stable. The harvested emulsion phase could be centrifuged to give an aqueous, concentrated lipase solution. Adsorption of lipase at the interface could be described by the Langmuir isotherm. For lipase concentrations ranging from 8.4 to 87.2 U cm,3, a single-stage adsorption resulted in a six- to four-fold concentration and 16,45% activity recovery, where lipase concentration was the dominant factor. A method using data from a single-stage adsorption to predict multiple-stage operation was described, and the agreement between the experimental and the predicted results was good. To improve the enzyme recovery, a multiple-run adsorption process was proposed. The use of salts enhanced the hydrophobic interaction between lipase and n -hexadecane. Advantages of the proposed process include simple operation, low operational cost, environmentally friendly, no requirement for pre-concentration of the enzyme solution, and negligible enzyme denaturation. Copyright © 2003 Society of Chemical Industry [source]

Penicillin G splitting in a flow-through electro-membrane reactor with the membrane-bound enzyme

Pavel Hasal
Abstract Penicillin G (PenG) (0.05 mol dm,3 in phosphate buffer, pH = 8) was hydrolyzed in a continuous flow-through electro-membrane reactor (EMR) with the penicillin G acylase (PGA) (EC immobilized in 10% (w/v) polyacrylamide membrane with an area of 900 mm2, thickness of 1 mm and enzyme activity of 100 U cm,3 and 160 U cm,3, respectively. The PenG was continuously fed to the substrate compartment adjacent to one membrane surface. Reaction products were washed from the membrane by a phosphate buffer solution fed to the product compartment adjacent to the other membrane surface. The mean residence time of both streams was varied from 11.3 min to 45 min. An electric field perpendicular to the membrane surface was imposed on the reactor and the electric current density was varied from 0 to 822 A m,2. Substrate conversion was determined as a function of the mean residence time, of the applied electric current density and of the enzyme activity of the membrane. The conversion increased with increasing residence time. The applied electric current increased substrate conversion by 200% at short residence times and at low enzyme activity of the membrane. Oscillatory reaction regime was evoked by step change of the mean residence time of reactant streams in the reactor. Copyright © 2009 Curtin University of Technology and John Wiley & Sons, Ltd. [source]