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• W2079758934 abstract "Bacterial strains were isolated from the pig colon to screen for phytase and acid phosphatase activities. Among 93 colonies, Colony 88 had the highest activities for both enzymes and was identified as anEscherichia colistrain. Using primers derived from theE. colipH 2.5 acid phosphataseappAsequence (Dassaet al.(1990),J. Bacteriol.172, 5497–5500), we cloned a 1482 bp DNA fragment from the isolate. In spite of 95% homology between the sequenced gene and theappA,7 amino acids were different in their deduced polypeptides. To characterize the properties and functions of the encoded protein, we expressed the coding region of the isolated DNA fragment andappAinPichia pastoris,respectively, as r-appA2 and r-appA. The recombinant protein r-appA2, like r-appA and the r-phyA phytase expressed inAspergillus niger, was able to hydrolyze phosphorus from sodium phytate andp-nitrophenyl phosphate. However, there were distinct differences in their pH profiles,KmandVmaxfor the substrates, specific activities of the purified enzymes, and abilities to release phytate phosphorus in soybean meal. In conclusion, the DNA fragment isolated fromE. coliin pig colon seems to encode for a new acid phosphatase/phytase and is designated asE. coli appA2." @default.
• W2079758934 created "2016-06-24" @default.
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• W2079758934 date "1999-04-01" @default.
• W2079758934 modified "2023-10-10" @default.
• W2079758934 title "Cloning, Sequencing, and Expression of anEscherichia coliAcid Phosphatase/Phytase Gene (appA2) Isolated from Pig Colon" @default.
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• W2079758934 doi "https://doi.org/10.1006/bbrc.1999.0361" @default.
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