Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.8 (phytase)
 1,997 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phytase enzymes can increase the nutritional value of food and feed by liberating inorganic phosphate from phytate, the major storage form of phosphorus in plants. The phytase (phyC) from Bacillus subtilis VTT E-68013 was expressed in Lactobacillus plantarum strain 755 using Lact. amylovorus alpha-amylase secretion signals. In an overnight cultivation in MRS medium containing cellobiose for induction of the alpha-amylase promoter, catalytically active phytase was secreted as a predominant extracellular protein. However, Western blot analysis revealed unprocessed and processed phytase in the cell fraction. Pulse chase experiments showed that the recombinant phytase was secreted at a slower rate in comparison to the native proteins of Lact. plantarum 755.
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PMID:Expression of Bacillus subtilis phytase in Lactobacillus plantarum 755. 1079 56

A phytase gene (appA) from Escherichia coli was cloned into Streptomyces lividans and expressed as an extracellular protein which was then compared with the same enzyme expressed in Pichia pastoris. The phytase expressed in S. lividans was not glycosylated and had a molecular mass of 45 kDa. Compared with the glycosylated phytase expressed in P. pastoris, this non-glycosylated phytase was 25-50% less active (p < 0.05) at pH 2 to 3.5 or at 45 and 55 degrees C, but 50% more active (p < 0.05) at 75 degrees C. The thermo-tolerance of the non-glycosylated phytase was 26 and 48% higher (p < 0.05) than that of the glycosylated phytase at 45 and 55 degrees C, but was 80 and 94% lower (p < 0.05) at 65 degrees and 75 degrees C, respectively.
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PMID:Comparison of extracellular Escherichia coli AppA phytases expressed in Streptomyces lividans and Pichia pastoris. 1288 15