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AMB Express
Fig. 2 | AMB Express

Fig. 2

From: Improving the thermostability of Pseudoalteromonas Porphyrae κ-carrageenase by rational design and MD simulation

Fig. 2

The enzymatic properties and fluorescence spectrum analysis of κ-carrageenases. (a) SDS-PAGE analysis of wild-type κ-carrageenanase and its mutants. Band M represented the standard protein marker, and bands 1–16 represented WT, S76M, G96M, C97K, Q100M, T151S, L152R, T153L, E154R, N155L, S190R, T192R, G197M, E201P, T202M, E279D, respectively. (b) The relative activities of 15 mutant κ-carrageenases. The enzyme activity of WT was defined as 100%. (c) Thermostability of 5 mutant κ-carrageenases (T151S, T153L, E154R, S190R, and T192R) after treatment at 45–60 °C for 30 min. (d) Absolute values of ΔΔG for 5 mutants of T151S, T153L, E154R, S190R, and T192R. (e) The optimal temperature of S190R and WT. (f) Fluorescence spectral analysis of S190R and WT.

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