Extended Data Fig. 6: Comparison HotPETase activity under standard and optimised reaction conditions. | Nature Catalysis

Extended Data Fig. 6: Comparison HotPETase activity under standard and optimised reaction conditions.

From: Directed evolution of an efficient and thermostable PET depolymerase

Extended Data Fig. 6

24 h time-courses of reactions conducted at 60 °C with HotPETase, showing the mean percentage of cryPET depolymerized (0.4% cryPET substrate loading (4 g L−1)), calculated using the concentration of MHET and TPA produced. Standard conditions were: 0.29 mg g−1 enzyme loading (0.04 μM), library screening buffer: pH 9.2, 50 mM Gly-OH, 4% BugBuster (dashed line). Optimised reaction conditions were: 3.62 mg g−1 enzyme loading (0.5 μM), pH 9.7, 50 mM Gly-OH, 4% BugBuster (solid line). Reactions were carried out in triplicate; error bars represent the s.d. of the replicate measurements.

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