Enzyme-catalyzed simultaneous hydrolysis-glycolysis reactions reveals tunability on PET depolymerization products

Castro, Aline Machado de; Carniel, Adriano; Sirelli, Lys; Dias, Marcos L.; Menezes, Sônia Maria Cabral de; Chinelatto, Luiz S.; Honorato, Hercílio de Angeli

doi:10.1016/j.bej.2018.06.007

Cited by 21 publications

(10 citation statements)

References 19 publications

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“…Studies of polyester cleavage by polyester hydrolases, cutinases, and carboxylesterases reveal that increased terephthalate to adipate ratios in the substrate inhibit degradation by suppressing molecular chain flexibility [1,7,28]. Similar results were shown for PET oligomers, where addition of less mobile domains to the polymer blend significantly inhibits both hydrolytic as well as glycolytic degradation of the substrate [4].…”

Section: Glossarymentioning

confidence: 61%

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Inderthal

Tai

Harrison

2021

Trends in Biotechnology

119

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Section: Glossarymentioning

confidence: 61%

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Inderthal

Tai

Harrison

2021

Trends in Biotechnology

119

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“…107 Polymeric materials with high polymerization degrees (e.g., 100) have different physicochemical properties to those with low polymerization degrees (e.g., 10−50 carbon atoms), and the latter can be taken up by a cell for further metabolization. 108,109 Castero et al 110 attempted enzymecatalyzed simultaneous hydrolysis−glycolysis reactions using the HiC and depolymerized PET of a different number of average molecular masses (500, 600, and 3800) and showed that production levels were highest with oligomer 500. All materials have two amorphous phases, less and more mobile domain, in which higher molecular masses increase the former and decrease the latter domains.…”

Section: Applications Of Pet Hydrolasesmentioning

confidence: 99%

Current State and Perspectives Related to the Polyethylene Terephthalate Hydrolases Available for Biorecycling

Kawai

Kawabata

Oda

2020

ACS Sustainable Chem. Eng.

217

195

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Polyethylene terephthalate (PET) hydrolase is a challenging target as PET is a commonly used plastic that is extremely resistant to enzymatic attack. Since the discovery of a PET hydrolase from Thermobif ida f usca in 2005, novel PET hydrolases and their availability toward waste PET have been investigated. At present, at least four thermophilic cutinases are known as PET hydrolases that could be used for the management of amorphous PET waste, such as packaging materials. Heat-labile PETase from Ideonella sakaiensis and its homologues from mesophilic bacteria exist in the environment. However, PET can be efficiently hydrolyzed with thermophilic hydrolases. This Review focuses on the current state of PET hydrolases and the potential of their application. Contrary to an amorphous PET, the enzymatic hydrolysis of crystalline PET (particularly PET bottles) remains to be fully elucidated. It cannot be assured whether the biorecycling of general PET would be put into practice in the near future, but the plan is getting closer to the goal. PET hydrolases can be versatile polyesterases as they can hydrolyze not only PET but also other polyesters. Additionally, the thermostability of PET hydrolases is advantageous to their application in terms of reaction speed and durability.

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“…Therefore, cutinases must be thermally stable (at temperatures above 60 °C) for the hydrolysis of semi-crystalline PET [36,[52][53][54]. Such behavior is necessary because the mobility of the polymer chain increases above the glass transition temperature (T g ), which for PC-PET occurs at 78.5 °C [55]. Still, it may be lowered by approximately 10 °C in aqueous solutions [56,57].…”

Section: Effect Of Temperaturementioning

confidence: 99%

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

et al. 2021

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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.

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Enzyme-catalyzed simultaneous hydrolysis-glycolysis reactions reveals tunability on PET depolymerization products

Cited by 21 publications

References 19 publications

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Current State and Perspectives Related to the Polyethylene Terephthalate Hydrolases Available for Biorecycling

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

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