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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: Biochemical characteristics and molecular mechanism of an exo-type alginate lyase VxAly7D and its use for the preparation of unsaturated monosaccharides

Fig. 2

Purity analysis and biochemical characterization of recombinant VxAly7D. a Purified recombinant VxAly7D was resolved by 12.5% (w/v) SDS-PAGE. Lane M, Pageruler unstained protein ladder (Thermo Scientific, USA); Lane 1, Purified recombinant VxAly7D. b The optimum pH was determined by measuring the activity at 30 °C in 50 mM buffer (Na2HPO4–citric acid, Na2HPO4–NaH2PO4, Tris–HCl, and Gly‐NaOH) at different pH values. The maximum specific activity was 462.4 ± 0.64 U/mg. c pH stability. The residual activity was measured at 30 °C in PB (pH 7.3) after incubation at 4 °C for 12 h. The initial specific activity was 438.62 ± 1.22 U/mg. d Optimal temperature and temperature stability were determined by measuring its activity at 0–60 °C. The maximum specific activity when measuring the optimum temperature was 462.4 ± 0.64 U/mg. The initial specific activity when measuring the temperature stability was 441.15 ± 2.04 U/mg. e The temperature stability of recombinant VxAly7D was measured at 20 °C and 30 °C for 0–24 h. The initial specific activity was 441.15 ± 2.04 U/mg. f Effect of the NaCl concentration on enzymatic activity of recombinant VxAly7D. The maximum specific activity was 462.4 ± 0.64 U/mg. g, Substrate specificity towards sodium alginate (SA), polyM (PM) and polyG (PG). The maximum specific activity was 462.4 ± 0.64 U/mg

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