Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/1504
Title: Gene cloning and soluble expression of Aspergillus niger phytase in E-coli cytosol via chaperone co-expression
Authors: Ushasree, M V
Vidya, J
Pandey, A
Keywords: Chaperone
Glycosylation
Maltose-binding protein
Phytase
Issue Date: 2014
Publisher: Springer
Citation: Biotechnology Letters 36(1):85-91;Jan 2014
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.
URI: http://ir.niist.res.in:8080/jspui/handle/123456789/1504
ISSN: 0141-5492
Appears in Collections:2014

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