ArticleJournal of Zhejiang University. Science. B2008
Expression, purification and characterization of a phyA(m)-phyCs fusion phytase.
Article in Journal of Zhejiang University. Science. B, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 22 citations in OpenAlex.
- Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153).Molecular biotechnology · 2018Article
- Purification and biochemical characterization of anBiotechnology reports (Amsterdam, Netherlands) · 2018Article
- Overexpression and biochemical characterization of a thermostable phytase from Bacillus subtilis US417 in Pichia pastoris.Molecular biotechnology · 2014Article
- Effects of neutral phytase on growth performance and phosphorus utilization in crucian carp (Carassius auratus).Journal of Zhejiang University. Science. BArticle
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phyA(m) gene encoding acid phytase and optimized neutral phytase phyCs gene were inserted into expression vector pPIC9K in correct orientation and transformed into Pichia pastoris in order to expand the pH profile of phytase and decrease the cost of production. The fusion phytase phyA(m)-phyCs gene was successfully overexpressed in P. pastoris as an active and extracellular phytase. The yield of total extracellular fusion phytase activity is (25.4+/-0.53) U/ml at the flask scale and (159.1+/-2.92) U/ml for high cell-density fermentation, respectively. Purified fusion phytase exhibits an optimal temperature at 55 degrees C and an optimal pH at 5.5~6.0 and its relative activity remains at a relatively high level of above 70% in the range of pH 2.0 to 7.0. About 51% to 63% of its original activity remains after incubation at 75 degrees C to 95 degrees C for 10 min. Due to heavy glycosylation, the expressed fusion phytase shows a broad and diffuse band in SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis). After deglycosylation by endoglycosidase H (EndoH(f)), the enzyme has an apparent molecular size of 95 kDa. The characterization of the fusion phytase was compared with those of phyCs and phyA(m).
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