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Fig. 5 | AMB Express

Fig. 5

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

Fig. 5

Biochemical characteristics of GH16B β-agarase. a, b The optimal temperature and pH of the enzymatic activity were determined using 0.4%[w/v] agarose and 0.8 µg/mL of the purified enzyme. Each value is expressed as the mean ± SEM (n = 3; three replicates per independent experiment). c, d Temperature and pH stabilities of the purified enzyme were measured following incubation for the indicated time at various temperatures and incubation for 4 h at various pH values. Data are expressed as the mean ± SEM (n = 3; three replicates per independent experiment). e Lineweaver‒Burk plot was used to determine Km and Vmax values of the purified enzyme based on indicated concentrations of the substrate (agarose) and enzyme. Representative results are shown; two additional experiments yielded similar results

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