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dc.contributor.authorUshasree, M V-
dc.contributor.authorVidya, J-
dc.contributor.authorPandey, A-
dc.date.accessioned2014-06-10T11:23:44Z-
dc.date.available2014-06-10T11:23:44Z-
dc.date.issued2014-
dc.identifier.citationBiotechnology Letters 36(1):85-91;Jan 2014en_US
dc.identifier.issn0141-5492-
dc.identifier.urihttp://ir.niist.res.in:8080/jspui/handle/123456789/1504-
dc.description.abstractA phytase gene from Aspergillus niger was isolated and two Escherichia coli expression systems, based on T7 RNA polymerase promoter and tac promoter, were used for its recombinant expression. Co-expression of molecular chaperone, GroES/EL, aided functional cytosolic expression of the phytase in E. coli BL21 (DE3). Untagged and maltose-binding protein-tagged recombinant phytase showed an activity band of similar to 49 and 92 kDa, respectively, on a zymogram. Heterologously-expressed phytase was fractionated from endogenous E. coli phytase by (NH4)(2)SO4 precipitation. The enzyme had optimum activity at 50 A degrees C and pH 6.5.en_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.subjectChaperoneen_US
dc.subjectGlycosylationen_US
dc.subjectMaltose-binding proteinen_US
dc.subjectPhytaseen_US
dc.titleGene cloning and soluble expression of Aspergillus niger phytase in E-coli cytosol via chaperone co-expressionen_US
dc.typeArticleen_US
Appears in Collections:2014

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