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Fig. 7 | AMB Express

Fig. 7

From: Extracellular production of a thermostable Cellvibrio endolytic β-agarase in Escherichia coli for agarose liquefaction

Fig. 7

Time-kinetic analysis of GH16B β-agarase-catalyzed hydrolysates of agarose, NAOS, and AOS using thin layer chromatography. ac Each substrate (0.4%[w/v] agarose, 1.0%[w/v] NAOS, or 1.0%[w/v] AOS) was treated with the purified enzyme (0.8 µg/mL) in 50 mM Mcllvaine buffer (pH 7.0) at 50 °C for the indicated time. Standard NAOS (STD NAOS) and AOS were prepared as described in “Materials and methods” section. Equivalent amounts of each sample were spotted on TLC plates and developed with n-butanol-ethanol-H2O (3:2:2[v/v]). Oligosaccharides were visualized as described in “Materials and methods” section. Representative results are shown; two additional experiments yielded similar results

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