Extended Data Fig. 3: Comparison of reactions with HotPETase and LCCICCG over a range of temperatures. | Nature Catalysis

Extended Data Fig. 3: Comparison of reactions with HotPETase and LCCICCG over a range of temperatures.

From: Directed evolution of an efficient and thermostable PET depolymerase

Extended Data Fig. 3

48 h time-courses of cryPET reactions, showing the mean total concentration of released MHET and TPA, with HotPETase (yellows-pinks) and LCCICCG (greens) over time, at a range of temperatures, using 0.4% cryPET substrate loading (4 g L−1) and 0.29 mg g−1 enzyme loading (0.04 μM). LCCICCG was assayed in its reported optimal operating buffer: pH 8, 100 mM K-Pi; IsPETase and its derivatives were assayed under the library screening buffer conditions: pH 9.2, 50 mM Gly-OH buffer, 4% BugBuster. Reactions were carried out in triplicate, with error bars representing the s.d. of the replicate measurements.

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