Alkaline phosphatase (APase) was found to be inducible in Anabaena sp. strain CA Growth was less than control in presence of most amino acids except glycine and serine, but most amino acids enhanced APase activity. Highest APase activity was recorded in tyrosine supplemented culture followed by hydroxyproline, cystein, valine and glutamic acid. Threonine supplemented material showed lowest APase level (1.8 nmol/mg protein/min). Lactose, glucose, sodium pyruvate and succinate stimulated growth but not APase activity. APase activity was high in the presence of sucrose, mellibiose, mannitol, arabinose, maltose and sorbose, even though the growth in these supplements was less than in control. Organic phosphate sources supported good growth of the organism. Best growth occurred in presence of inorganic phosphate, adenosine diphosphate, fructose 1,6-diphosphate or ribulose 1,5-diphosphate, followed by other phosphorus sources tested. APase activity in presence of any of the organic phosphate sources was 3 to 5 fold low as compared to phosphate limited culture. Also, there was no APase activity in cultures grown on inorganic phosphate. These data indicate that most amino acids and a few carbohydrates (sucrose, mellibiose, arabinose and sorbose) are suitable for APase production. Lactose, glucose, pyruvate or succinate may be used as a carbon source during photoheterotrophic growth of the cyanobacterium. Glycine and serine are preferred nitrogen sources for its growth. Phosphate repressible APase activity has been found in Anabaena sp. strain CA.
DOI 인용 스타일