dc.contributor.author | Ushasree, M V | |
dc.contributor.author | Vidya, J | |
dc.contributor.author | Pandey, A | |
dc.date.accessioned | 2014-06-10T11:23:44Z | |
dc.date.available | 2014-06-10T11:23:44Z | |
dc.date.issued | 2014 | |
dc.identifier.citation | Biotechnology Letters 36(1):85-91;Jan 2014 | en_US |
dc.identifier.issn | 0141-5492 | |
dc.identifier.uri | http://ir.niist.res.in:8080/jspui/handle/123456789/1504 | |
dc.description.abstract | A 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.iso | en | en_US |
dc.publisher | Springer | en_US |
dc.subject | Chaperone | en_US |
dc.subject | Glycosylation | en_US |
dc.subject | Maltose-binding protein | en_US |
dc.subject | Phytase | en_US |
dc.title | Gene cloning and soluble expression of Aspergillus niger phytase in E-coli cytosol via chaperone co-expression | en_US |
dc.type | Article | en_US |