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Production of D-myo-inositol(1,2,4,5,6)pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase BABT
Greiner,Ralf; Sajidan,.
The glucose-1-phosphatase encoding gene (agp) of Pantoea agglomerans was sequenced and heterologously expressed in Escherichia coli. The enzyme showed very high homology to periplasmatic glucose-1-phosphatases of other members of the Enterobacteriaceae family. It was isolated from transformed Escherichia coli cells in a single step in high yields (32.3 ± 1.2 mg per litre of culture) by Ni-NT agarose affinity chromatography to >95% purity as calculated from specific activity determinations. The purified glucose-1-phosphatase was entrapped in alginate beads with an entrapment efficiency of >80%. Temperature stability was enhanced as a consequence of entrapment, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Entrapment; Glucose-1-phosphatase; Myo-inositol pentakisphosphate Pantoea agglomerans; Phytase.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132008000200002
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