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Novel efficient enzymatic synthesis of the key-reaction intermediate of PET depolymerization, mono(2-hydroxyethyl terephthalate) - MHET.
Eugenio, Erika de Queiros; Campisano, Ivone Sampaio Pereira; Dias, Ayres Guimarães; Castro, Aline Machado de; Coelho, Maria Alice Zarur; Langone, Marta Antunes Pereira.
Afiliação
  • Eugenio EQ; Chemical School, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil; Faculty of Technology, Rio de Janeiro State University (UERJ), Rio de Janeiro, Brazil.
  • Campisano ISP; Chemical School, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
  • Dias AG; Chemistry Institute, Rio de Janeiro State University (UERJ), Rio de Janeiro, Brazil.
  • Castro AM; Biotechnology Division, Research, and Development Center, Petrobras, Rio de Janeiro, Brazil.
  • Coelho MAZ; Chemical School, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
  • Langone MAP; Chemistry Institute, Rio de Janeiro State University (UERJ), Rio de Janeiro, Brazil; Federal Institute of Education, Science, and Technology of Rio de Janeiro (IFRJ), Rio de Janeiro, Brazil. Electronic address: marta.langone@gmail.com.
J Biotechnol ; 358: 102-110, 2022 Nov 10.
Article em En | MEDLINE | ID: mdl-36063976
Poly(ethylene terephthalate) (PET) is one of the main synthetic plastics produced worldwide. The extensive use of this polymer causes several problems due to its low degradability. In this scenario, biocatalysts dawn as an alternative to enhance PET recycling. The enzymatic hydrolysis of PET results in a mixture of terephthalic acid (TPA), ethylene glycol (EG), mono-(2-hydroxyethyl) terephthalate (MHET) and bis-(2-hydroxyethyl) terephthalate (BHET) as main products. This work developed a new methodology to quantify the hydrolytic activity of biocatalysts, using BHET as a model substrate. The protocol can be used in screening enzymes for PET depolymerization reactions, amongst other applications. The very good fitting (R2 = 0.993) between experimental data and the mathematical model confirmed the feasibility of the Michaelis-Menten equation to analyze the effect of BHET concentration (8-200 mmol L-1) on initial hydrolysis rate catalyzed by Humicola insolens cutinase (HiC). In addition to evaluating the effects of enzyme and substrate concentration on the enzymatic hydrolysis of BHET, a novel and straightforward method for MHET synthesis was developed using an enzyme load of 0.025 gprotein gBHET-1 and BHET concentration of 60 mmol L-1 at 40 °C. MHET was synthesized with high selectivity (97 %) and yield (82 %). The synthesized MHET properties were studied using differential scanning calorimetry (DSC), thermogravimetry (TGA), and proton nuclear magnetic resonance (1H NMR), observing the high purity of the final product (86.7 %). As MHET is not available commercially, this synthesis using substrate and enzyme from open suppliers adds new perspectives to monitoring PET hydrolysis reactions.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Prótons / Polietilenotereftalatos Idioma: En Revista: J Biotechnol Assunto da revista: BIOTECNOLOGIA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Prótons / Polietilenotereftalatos Idioma: En Revista: J Biotechnol Assunto da revista: BIOTECNOLOGIA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda