Study of Acid Phosphatase in Solubilization of Inorganic Phosphates by Piriformospora indica.

Phosphorus is an essential plant macronutrient present in the soil. Only a small portion of phosphorus in soil is taken up by plants and the rest of it becomes unavailable to plants as it is immobilized. Phosphate solubilizing microorganisms play a vital role in converting the insoluble form of phosphates to the soluble form. The present paper reports the solubilization of tricalcium phosphate, rock phosphate, single super phosphate, zinc phosphate and aluminum phosphate by Piriformospora indica with the production of organic acids as well as acid phosphatase. The amount of phosphate released (4.73 mg ml-1) and titratable acidity (0.12%) was found to be the highest in the case of single super phosphate as compared to other phosphate sources. High performance liquid chromatography (HPLC) revealed the presence of oxalic acid, lactic acid, citric acid and succinic acid in the media. Highest phosphatase activity was observed with the cell membrane extract of the organism in the presence of zinc phosphate.

Production and characterization of protease enzyme from Acinetobacter pittii using peanut meal as substrate.

A significantly high protease enzyme yield of 617 U/ml was achieved with Acinetobacter pittii as the microorganism and peanut oil meal as the substrate. Peanut oil meal, which consists of proteins (40-60%) and carbohydrates (22-30%), serves as a sufficient source of nitrogen and carbon necessary for microbial growth and production of enzymes. Moreover, peanut meal offers the advantages of being affordable and available in large quantities, making the meal suitable for cost-effective enzyme production. In the present study, two bacterial strains and one fungal strain were selected to produce proteases utilizing peanut oil meal as the substrate. The experimental conditions during the enzyme production, including pH and temperature, were optimized. In addition, the substrate was enriched with various carbon and nitrogen sources. The microbial strains were streaked on nutritional agar (for bacteria) and potato dextrose agar (for fungus). Following an incubation period, the plates were stored at 4°C for further studies. The molecular weight of partially purified proteases of Acinetobacter pittii was found to be ≅ 95.5 kDa. Potassium nitrate was the most ideal nitrogen source (up to 411% increase in activity) and fructose was the best carbon source (425% increase). These enzymes exhibited excellent temperature tolerance and were capable of functioning over a wide pH range. Furthermore, the obtained proteases demonstrated ability to coagulate milk effectively, indicating their potential for various food-related applications.