Kinetic Modeling of the Post-consumer Poly(Ethylene Terephthalate) Hydrolysis Catalyzed by Cutinase from Humicola insolens

• Published in: Journal of polymers and the environment Vol. 30; no. 4; pp. 1627 - 1637
• Main Authors: Eugenio, Erika de Queiros, Campisano, Ivone Sampaio Pereira, de Castro, Aline Machado, Coelho, Maria Alice Zarur, Langone, Marta Antunes Pereira
• Format: Journal Article
• Language: English
• Published: New York Springer US 01-04-2022; Springer Nature B.V
• Subjects: Acids; Activation energy; Biocatalysts; Catalysis; Chemistry; Chemistry and Materials Science; Circular economy; Cutinase; Employment; Enthalpy; Entropy; Entropy of activation; Environmental Chemistry; Environmental Engineering/Biotechnology; Enzymes; Ethylene; Fungi; Humicola insolens; Hydrolysis; Industrial Chemistry/Chemical Engineering; Materials Science; Mathematical models; Original Paper; Parameters; Polyethylene terephthalate; Polymer Sciences; Polymers; Terephthalic acid; Heterogeneous biocatalysis; Kinetic parameters; cutinase; PET biodegradation
• ISSN: 1566-2543; 1572-8919
• DOI: 10.1007/s10924-021-02301-4

The search for a straightforward technology for post-consumer poly(ethylene terephthalate) (PC-PET) degradation is essential to develop a circular economy. In this context, PET hydrolases such as cutinases can be used as bioplatforms for this purpose.
Humicola insolens
cutinase (HiC) is a promising biocatalyst for PC-PET hydrolysis. Therefore, this work evaluated a kinetic model, and it was observed that the HiC seems not to be inhibited by any of the main PET hydrolysis products such as terephthalic acid (TPA), mono-(2-hydroxyethyl) terephthalate (MHET), and bis-(2-hydroxyethyl) terephthalate (BHET). The excellent fitting of the experimental data to a kinetic model based on enzyme-limiting conditions validates its employment for describing the enzymatic PC-PET hydrolysis using two-particle size ranges (0.075–0.250, and 0.250–0.600 mm) and temperatures (40, 50, 55, 60, 70, and 80 °C). The Arrhenius law provided a reliable parameter (activation energy of 98.9 ± 2.6 kJ mol
−1
) for enzymatic hydrolysis, which compares well with reported values for chemical PET hydrolysis. The thermodynamic parameters of PC-PET hydrolysis corresponded to activation enthalpy of 96.1 ± 3.6 kJ mol
−1
and activation entropy of 78.9 ± 9.5 J mol
−1
 K
−1
. Thus, the observed rate enhancement with temperature was attributed to the enthalpic contribution, and this understanding is helpful to the comprehension of enzymatic behavior in hydrolysis reaction.