A comparative analysis of recombinant expression and solubility screening of two phytases in E. coli

Microbial phytases, especially from fungal and bacterial sources, have received much attention as food additives in human nutrition and as feed supplements for monogastric animals. An effective expression screening method for recombinant production of this enzyme on a small scale is industrially des...

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Bibliographic Details
Published in:Food technology and biotechnology 2011-07, Vol.49 (3), p.304-309
Main Authors: Vasudevan, Ushasree Mrudula, Salim, Sumayya Husaiba Beevi, Pandey, Ashok
Format: Article
Language:English
Subjects:
A. niger phytase
Analysis
Animals
Aspergillus
Bacteria
Cloning
Deoxyribonucleic acid
DNA
E coli
Enzymes
Escherichia coli
Feeds
Genetic aspects
Genetic engineering
Hogs
inducer concentration
Microbiology
Pets
Plasmids
Production processes
Proteins
recombinant appA
Temperature
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Summary:Microbial phytases, especially from fungal and bacterial sources, have received much attention as food additives in human nutrition and as feed supplements for monogastric animals. An effective expression screening method for recombinant production of this enzyme on a small scale is industrially desirable. An effort has been made in this work to clone and express phytase genes from Aspergillus sp. and Escherichia coli with the selected host, vector and inducer combination. Albeit the formation of insoluble inclusion bodies by fungal phytase, recombinant E. coli appA was effectively expressed in a cost-effective manner in the periplasm of BL21plysS using an inducer concentration of 0.01 mM in 4 h of growth. Enzyme was purified in three consecutive steps and functional studies were carried out. Key words: A. niger phytase, inducer concentration, recombinant appA
ISSN:1330-9862
1334-2606