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Fig. 1 | BMC Biotechnology

Fig. 1

From: Characterization of the 4,6-α-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies

Fig. 1

Bargraphs of the relative activities of soluble, refolded and different ncIB GTFB enzymes. The refolded GTFB enzymes were obtained from various refolding buffers, and the non-classical inclusion bodies (ncIBs) GTFB were expressed at different temperatures (a). All enzyme concentrations used were 100 μg/ml. The enzyme activity was defined as the release of glucose from maltoheptaose at 37 °C and pH 4.7. The hydrolysis activity of soluble GTFB was set at 100 % (0.17 U). The total hydrolysis and transferase activities of soluble, refolded and ncIB GTFB enzymes obtained from one liter E. coli culture expressing GTFB are shown in bargraphs (b) and (c). In (b) 100 % activity corresponds to 13.4 U hydrolysis activity and in (c) the 100 % value corresponds to a transferase activity of 4.3 U in 1 l culture

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