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Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science. KTH, Centres, Science for Life Laboratory, SciLifeLab. ACIB, Konrad Lorenz Str 20, A-3430 Tulln An Der Donau, Austria.
Univ Nat Resources & Life Sci BOKU, Inst Environm Biotechnol, Konrad Lorenz Str 20, A-3430 Tulln An Der Donau, Austria..
Univ Appl Sci, Dept Bioengn, Mauerbachstr 43, A-1140 Vienna, Austria..
ACIB, Konrad Lorenz Str 20, A-3430 Tulln An Der Donau, Austria.;Univ Nat Resources & Life Sci BOKU, Inst Environm Biotechnol, Konrad Lorenz Str 20, A-3430 Tulln An Der Donau, Austria..
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2019 (English)In: RSC Advances, ISSN 2046-2069, E-ISSN 2046-2069, Vol. 9, no 62, p. 36217-36226Article in journal (Refereed) Published
Abstract [en]

The recalcitrance of plastics like nylon and other polyamides contributes to environmental problems (e.g. microplastics in oceans) and restricts possibilities for recycling. The fact that hitherto discovered amidases (EC 3.5.1. and 3.5.2.) only show no, or low, activity on polyamides currently obstructs biotechnological-assisted depolymerization of man-made materials. In this work, we capitalized on enzyme engineering to enhance the promiscuous amidase activity of polyesterases. Through enzyme design we created a reallocated water network adapted for hydrogen bond formation to synthetic amide backbones for enhanced transition state stabilization in the polyester-hydrolyzing biocatalysts Humicola insolens cutinase and Thermobifida cellulosilytica cutinase 1. This novel concept enabled increased catalytic efficiency towards amide-containing soluble substrates. The afforded enhanced hydrolysis of the amide bond-containing insoluble substrate 3PA 6,6 by designed variants was aligned with improved transition state stabilization identified by molecular dynamics (MD) simulations. Furthermore, the presence of a favorable water-molecule network that interacted with synthetic amides in the variants resulted in a reduced activity on polyethylene terephthalate (PET). Our data demonstrate the potential of using enzyme engineering to improve the amidase activity for polyesterases to act on synthetic amide-containing polymers.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2019. Vol. 9, no 62, p. 36217-36226
Keywords [en]
Thermobifida-Cellulosilytica, Polyethylene Terephthalate, Surface Hydrolysis, Transition-State, Cutinase, Binding, Degradation, Polyethyleneterephthalate, Parameterization, Microplastics
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-265458DOI: 10.1039/c9ra07519dISI: 000497825500036Scopus ID: 2-s2.0-85075004406OAI: oai:DiVA.org:kth-265458DiVA, id: diva2:1377957
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QC 20200422

Available from: 2019-12-13 Created: 2019-12-13 Last updated: 2020-04-22Bibliographically approved

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Biundo, AntoninoSyrén, Per-Olof

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