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Partial purification and characterization of phytase from Aspergillus foetidus MTCC 11682

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Title Partial purification and characterization of phytase from Aspergillus foetidus MTCC 11682
 
Creator Ajith, Sreeja
Ghosh, Jyotirmoy AU
Shet, Divya
ShreeVidhya, S.
Punith, B. D.
Elangovan, A. V.
 
Subject Phytase
Aspergillus foetidus
Phy gene
 
Description Not Available
Phytase is a phosphatase enzyme widely used as feed additive to release inorganic phosphorus from plant phytate and enhance its uptake in monogastric animals. Although engineered fungal phytases are used most, a natural enzyme gives opportunity to understand novel properties, if any. In the current study, a novel fungal strain, Aspergillus foetidus MTCC 11682 was immobilized on poly urethane cubes and used for phytase production, purifcation and molecular characterization. Phytase produced by this method was partially purifed by ammonium sulphate precipitation and Sephacryl S-200HR gel fltration to 23.4-fold (compared to crude extract) with recovery of 13% protein.
Electrophoresis analysis revealed that phytase has molecular weight of 90.5 kDa on non-reducing and 129.6 kDa on reducing SDS-PAGE. The purifed phytase exhibited a wider pH and temperature stability. Analysis of the cloned sequence showed that the gene has 1176 bp that encodes for a peptide of 391 amino acids of the core catalytic region. It was also found that phytase from A. foetidus has a sequence identity of 99% with the phytase gene of other Aspergillus species at nucleotide level and 100% at protein level in A. niger, A. awamori, A. oryzae. In silico analysis of sequence identifed the presence of two consecutive and one non-consecutive intra chain disulfde bonds in the
phytase. This probably contributed to the diferential migration of phytase on reducing and non-reducing SDS-PAGE. There are predicted 11 O-glycosylation sites and 8 N-glycosylation sites, possibly contributed to an enhanced stability of enzyme produced by this organism. This study opened up a new horizon for exploring the novel properties of phytase for other applications.
Department of Biotechnology, GOI
 
Date 2019-11-15T05:49:39Z
2019-11-15T05:49:39Z
2019-04-01
 
Type Research Paper
 
Identifier Ajith S, Ghosh J, Shet D, Vidhya SS, Punith BD, Elangovan AV. 2019. Partial purification and characterization of phytase from Aspergillus foetidus MTCC 11682. AMB Express, 9:3.
2191-0855
http://krishi.icar.gov.in/jspui/handle/123456789/24731
 
Language English
 
Relation Not Available;
 
Publisher Springer