Evidence of exponential growth of an anammox population in an anaerobic batch culture.
Twenty-five replicates of growth medium for anaerobic ammonium oxidation (anammox) containing (15)N-labeled ammonium and non-labeled nitrite were inoculated into an anammox enrichment culture at low density, and anaerobically incubated batchwise. In the headspace, (29)N(2) partial pressure linearly increased via anammox in 25 vials, confirming that anammox populations were viable in all subcultures. On prolonged incubation, exponential increases in (29)N(2) were not observed in all but 13 subcultures, suggesting that the anammox population may not proliferate unless all conditions for growth are satisfied. The estimated first-order rate coefficients in those 13 subcultures varied from 0.0029 to 0.0048 h(-1). (+info)
A novel recirculating flow-perfusion bioreactor for periosteal chondrogenesis.
Parametric optimization of feruloyl esterase production from Aspergillus terreus strain GA2 isolated from tropical agro-ecosystems cultivating sweet sorghum.
A fungal strain, Aspergillus terreus strain GA2, isolated from an agricultural field cultivating sweet sorghum, produced feruloyl esterase using maize bran. In order to obtain maximum yields of feruloyl esterase, the solid state fermentation (SSF) conditions for enzyme production were standardized. Effective feruloyl esterase production was observed with maize bran as substrate followed by wheat bran, coconut husk, and rice husk among the tested agro-waste crop residues. Optimum particle size of 0.71- 0.3 mm and moisture content of 80% favored enzyme production. Moreover, optimum feruloyl esterase production was observed at pH 6.0 and a temperature of 30 degrees C. Supplementation of potato starch (0.6%) as the carbon source and casein (1%) as the nitrogen source favored enzyme production. Furthermore, the culture produced the enzyme after 7 days of incubation when the C:N ratio was 5. Optimization of the SSF conditions revealed that maximum enzyme activity (1,162 U/gds) was observed after 7 days in a production medium of 80% moisture content and pH 6.0 containing 16 g maize bran [25% (w/v)] of particle size of 0.71-0.3 mm, 0.6% potato starch, 3.0% casein, and 64 ml of formulated basal salt solution. Overall, the enzyme production was enhanced by 3.2-fold as compared with un-optimized conditions. (+info)
Repeated-batch operation of immobilized beta-galactosidase inclusion bodies-containing Escherichia coli cell reactor for lactose hydrolysis.
In this study, we investigated the performance of an immobilized beta-galactosidase inclusion bodies-containing Escherichia coli cell reactor, where the cells were immobilized in alginate beads, which were then used in repeated-batch operations for the hydrolysis of o-nitrophenyl-beta-D-galactoside or lactose over the long-term. In particular, in the Tris buffer system, disintegration of the alginate beads was not observed during the operation, which was observed for the phosphate buffer system. The o-nitrophenyl-beta-D-galactoside hydrolysis was operated successfully up to about 80 h, and the runs were successfully repeated at least eight times. In addition, hydrolysis of lactose was successfully carried out up to 240 h. Using Western blotting analyses, it was verified that the beta-galactosidase inclusion bodies were sustained in the alginate beads during the repeated-batch operations. Consequently, we experimentally verified that beta-galactosidase inclusion bodies-containing Escherichia coli cells could be used in a repeated-batch reactor as a biocatalyst for the hydrolysis of o-nitrophenyl-beta-D-galactoside or lactose. It is probable that this approach can be applied to enzymatic synthesis reactions for other biotechnology applications, particularly reactions that require long-term and stable operation. (+info)