Decomposition of the PET Film by MHETase Using Exo-PETase Function
Citations Over TimeTop 10% of 2020 papers
Abstract
Monohydroxyethyl terephthalate (MHET) hydrolase (MHETase) is an enzyme known to be involved in the final degradation step of poly(ethylene terephthalate) (PET) by hydrolyzing MHET into terephthalic acid and ethylene glycol in Ideonella sakaiensis. Here, we report the extracellular production of MHETase in an active form with a proper folding. Based on the structural observations and biochemical experiments, we reveal that MHETase also functions as exo-PETase by hydrolyzing the synthesized PET pentamer. We further present that MHETase has a hydrolysis activity against the termini-generated PET film, demonstrating the exo-PETase function of the enzyme. We also develop a MHETaseR411K/S416A/F424I variant with a higher BHET activity, and the variant exhibits an enhanced degradation activity against the PET film. Based on these results, we propose that MHETase plays several roles in the biodegradation of PET using the BHETase and exo-PETase activities as well as the MHET hydrolysis function.
Related Papers
- → p-Xylene Oxidation to Terephthalic Acid: New Trends(2023)36 cited
- → Optimization of hydroxyl radical formation using TiO2 as photocatalyst by response surface methodology(2008)64 cited
- Elementary Studies on Biotransformation of p- Xylene into Terephthalic Acid(2006)
- TREATMENT TECHNOLOGY OF WASTEWATER CONTAINING TERPHTHALIC ACID(2002)
- → BP‐Amoco Mid‐Century Process for Terephthalic Acid Production (Case Study)(2023)2 cited