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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)

Fig. 1

Heterologous expression and functional validation of the putative inulin hydrolysis encoding genes from B. amyloliquefaciens in Escherichia coli. a Restriction analysis of recombinant plasmid pET28a-sacC. Lanes 1 and 2: pET28a-sacC digested with BamHI or XhoI; lane 3: pET28a-sacC digested with BamHI and XhoI; and lane M: DL15,000 marker. Inulinase activity was determined by DNS method. Lane C: the control crude extract and lanes 4, 5, and 6: inulinase activity detected at 30, 45, and 55 °C, respectively. b Restriction analysis of recombinant plasmid pET28a-CscA. Lanes 1 and 2: pET28a-CscA digested with BamHI or XhoI; lane 3, pET28a-CscA digested with BamHI and XhoI; and lane M: DL15,000 marker. Inulinase activity was determined by DNS method. Lane C: the control crude extract and lane 4, 5, and 6, inulinase activity detected at 30, 45, and 55 °C, respectively

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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