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Single-step purification and immobilization of MBP–phytase fusion on starch agar beads: Application in dephytination of soy milk

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dc.contributor.author Ushasree, M V
dc.contributor.author Gunasekaran, P
dc.contributor.author Pandey, A
dc.date.accessioned 2013-05-24T05:59:08Z
dc.date.available 2013-05-24T05:59:08Z
dc.date.issued 2012-07
dc.identifier.citation Applied Biochemistry & Biotechnology 167(5):981-990;2012 en_US
dc.identifier.uri http://hdl.handle.net/123456789/372
dc.description.abstract Periplasmic phytase, appA from E. coli has been noticed as a superior feed and food additive owing to its high specific activity, acidic pH optimum and resistance to gastric proteases.E. coli phytase was expressed as a fusion protein with maltose-binding protein, affinity-purified to homogeneity and, subsequently, immobilized in one step using a cost-effective matrix prepared from starch agar bead. Immobilized enzyme revealed an activity optimum at pH 6, while that of free enzyme was observed at pH 4. Both the immobilized and free enzyme showed a temperature optimum at 60 °C. Cleavage of 87 kDa fusion protein using factor Xa released 45 kDa appA. Hydrolysis of soy milk using immobilized enzyme led to 10% increase in release of inorganic phosphate at 50 °C relative to free fusion protein. This study suggests the usability of MBP as an immobilizing linker to other food enzymes for economical use in industry en_US
dc.language.iso en en_US
dc.publisher Springer en_US
dc.subject Starch agar beads en_US
dc.subject Soy milk en_US
dc.subject Dephytination en_US
dc.subject E. coli phytase en_US
dc.title Single-step purification and immobilization of MBP–phytase fusion on starch agar beads: Application in dephytination of soy milk en_US
dc.type Article en_US


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