The Escherichia coli phytase gene appA was highly expressed in the methylotrophic yeast Pichia pastoris under the control of the AOX1 promoter. Replacement of culture medium with fresh medium in order to remove repressing glycerol and metabolic wastes prior to methanol induction significantly improved phytase expression. The phytase activity level was enhanced from 118 to 204 U/ml at the flask ...

This experiment was conducted to investigate the effect of phytase superdoses alone or in combination with citric acid (CA) in canola meal-based diets severely limited in available phosphorus (Pa) on growth performance, plasma phosphorus (P), and tibia ash (TA) in broilers from 22 to 42 d of age. Two hundreds and eighty 21-d-old male broilers were used in 28 pens of 10 birds per each. The exper...

Phytase expressed and anchored on the cell surface of Pichia pastoris avoids the expensive and time-consuming steps of protein purification and separation. Furthermore, yeast cells with anchored phytase can be used as a whole-cell biocatalyst. In this study, the phytase gene of Citrobacter amalonaticus was fused with the Pichia pastoris glycosylphosphatidylinositol (GPI)-anchored glycoprotein h...

Abstract Aims An essential task of agricultural systems is to improve internal phosphorus (P) recycling. Cover crops and tillage reduction can increase sustainability, but it not known whether stimulation the soil microbial community availability organic P pools. Methods In a field experiment in southwest Germany, effects winter cover crop mixture (vs. bare fallow) no-till non-inversion tillage...

The Bacillus subtilis strain VTT E-68013 was chosen for purification and characterization of its excreted phytase. Purified enzyme had maximal phytase activity at pH 7 and 55 degrees C. Isolated enzyme required calcium for its activity and/or stability and was readily inhibited by EDTA. The enzyme proved to be highly specific since, of the substrates tested, only phytate, ADP, and ATP were hydr...

In this study, an extracellular phytase produced by Aspergillus niger 7A-1, was biochemically characterized for possible industrial application. The enzyme was purified from a crude extract obtained by solid-state fermentation (SSF) of triticale waste. The extract was obtained by microfiltration, ultrafiltration (300, 100 and 30 kDa) and DEAE-Sepharose column chromatography. The molecular weigh...

A phytase (EC 3.1.3.8) with a high affinity for phytic acid was found in Aspergillus niger SK-57 and purified to homogeneity in four steps by using ion-exchange chromatography (two types), gel filtration, and chromatofocusing. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme gave a single stained band at a molecular mass of approximately 60 kDa. The Michaelis con...

Goal, Scope and Background. Ronozyme® P5000 CT is an industrially produced enzyme product (phytase) which is able to degrade naturally occurring phytate in animal feed and release the phytate's content of phosphorus for pig's growth. Ronozyme P5000 CT (hereafter called Ronozyme Phytase) can be used as an alternative to inorganic phosphorus supplementation to feed and the study addresses the env...

Phytase-producing Klebsiella and Shigella sp. were isolated from environmental samples based on their ability to degrade phytate and the enzymes were purified and characterized. The enzymes from both sources were intracellular monomeric proteins with the molecular mass of about 40kDa. The enzymes were active in the pH range of 2.0 to 7.5 with pH optima at 5.5. The optimum in vitro temperatures ...

Among sixty one yeast isolates from various samples, twelve were capable of producing phytase. Out of twelve, 5 isolates showed maximum phytase activity. CB3 isolate was selected for further study. CB3 isolate was genetically characterized as Candida parapsilosis. The crude extract was optimized for maximum enzyme activity. The enzyme was stable between the pH 2 to 7 but the optimal pH was foun...