Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?

Ferrario, Virgilio F.; Pellis, Alessandro; Cespugli, Marco; Guebitz, Georg M.; Gardossi, Lucia

doi:10.3390/catal6120205

Cited by 44 publications

(38 citation statements)

References 81 publications

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“…To date, cutinases and their homologues are potential tools towards polymer degradation, since they have been reported to hydrolyze a variety of polymeric substrates, such as poly(butylene succinate) (PBS), polycaprolactone (PCL), and PET. Such examples have been recapitulated previously [98]. Below, the most recent cutinase depolymerization paradigms are epitomized.…”

Section: Plastics Degradationmentioning

confidence: 94%

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

et al. 2018

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Cutinases are α/β hydrolases, and their role in nature is the degradation of cutin. Such enzymes are usually produced by phytopathogenic microorganisms in order to penetrate their hosts. The first focused studies on cutinases started around 50 years ago. Since then, numerous cutinases have been isolated and characterized, aiming at the elucidation of their structure–function relations. Our deeper understanding of cutinases determines the applications by which they could be utilized; from food processing and detergents, to ester synthesis and polymerizations. However, cutinases are mainly efficient in the degradation of polyesters, a natural function. Therefore, these enzymes have been successfully applied for the biodegradation of plastics, as well as for the delicate superficial hydrolysis of polymeric materials prior to their functionalization. Even though research on this family of enzymes essentially began five decades ago, they are still involved in many reports; novel enzymes are being discovered, and new fields of applications arise, leading to numerous related publications per year. Perhaps the future of cutinases lies in their evolved descendants, such as polyesterases, and particularly PETases. The present article reviews the biochemical and structural characteristics of cutinases and cutinase-like hydrolases, and their applications in the field of bioremediation and biocatalysis.

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Section: Plastics Degradationmentioning

confidence: 94%

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

et al. 2018

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“…For this study, it was prioritized a condition in which all enzymes could be active and stable, more than an ideal condition of PET availability, such as near to its glass transition temperature. As reviewed by Ferrario et al [10] from a large list of microbial sources, cutinases present molar mass of up to 40 kDa. As shown in Figs.…”

Section: Screening Of Enzymes For Pet Hydrolysismentioning

confidence: 99%

Screening of commercial enzymes for poly(ethylene terephthalate) (PET) hydrolysis and synergy studies on different substrate sources

Castro

Carniel²,

Nicomedes

et al. 2017

Journal of Industrial Microbiology and Biotechnology

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Poly(ethylene terephthalate) (PET) is one of the most consumed plastics in the world. The development of efficient technologies for its depolymerization for monomers reuse is highly encouraged, since current recycling rates are still very low. In this study, 16 commercial lipases and cutinases were evaluated for their abilities to catalyze the hydrolysis of two PET samples. Humicola insolens cutinase showed the best performance and was then used in reactions on other PET sources, solely or in combination with the efficient mono(hydroxyethyl terephthalate)-converting lipase from Candida antarctica. Synergy degrees of the final titers of up to 2.2 (i.e., more than double of the concentration when both enzymes were used, as compared to their use alone) were found, with increased terephthalic acid formation rates, reaching a maximum of 59,989 µmol/L (9.36 g/L). These findings open up new possibilities for the conversion of post-consumer PET packages into their minimal monomers, which can be used as drop in at existing industrial facilities.

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“…Thanks to its promiscuity and activity in the most disparate reaction conditions, the lipase B from Candida antarctica (CaLB) emerged in these studies as the most used and investigated biocatalysts for polymerization reactions. [9] More recently, the interest in biocatalysis for polyester (and polyamide) synthesis [10,11] has again led to the investigation of fungal cutinases as compared with the more commonly known CaLB as biocatalysts for polycondensation and ROP reactions, especially exploiting renewable resources that would contribute to the closure of the polymers carbon cycle. [12,13] The first reports of cutinase-catalyzed synthesis of polyesters were published by the Gross group, which reported how cutinase from Humicola insolens (HiC) in its immobilized form was able to catalyze ROP of various lactones (both in bulk and in toluene), [14,15] as well as catalyze the polycondensation of aliphatic polyesters starting from AA-BB building blocks and v-hydroxyacids.…”

Section: Introductionmentioning

confidence: 99%

His‐Tag Immobilization of Cutinase 1 From Thermobifida cellulosilytica for Solvent‐Free Synthesis of Polyesters

Pellis

Vastano

Quartinello

et al. 2017

Biotechnology Journal

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For many years, lipase B from Candida antarctica (CaLB) was the primary biocatalyst used for enzymatic esterification and polycondensation reactions. More recently, the need for novel biocatalysts with different selectivity has arisen in the biotechnology and biocatalysis fields. The present work describes how the catalytic potential of Thermobifida cellulosilytica cutinase 1 (Thc_Cut1) was exploited for polyester synthesis. In a first step, Thc_Cut1 was immobilized on three different carriers, namely Opal, Coral, and Amber, using a novel non-toxic His-tag method based on chelated Fe(III) ions (>99% protein bounded). In a second step, the biocatalyzed synthesis of an array of aliphatic polyesters was conducted. A selectivity chain study in a solvent-free reaction environment showed how, in contrast to CaLB, Thc_Cut1 presents a certain preference for C -C ester-diol combinations reaching monomer conversions up to 78% and M of 878 g mol when the Amber immobilized Thc_Cut1 was used. The synthetic potential of this cutinase was also tested in organic solvents, showing a marked activity decrease in polar media like that observed for CaLB. Finally, recyclability studies were performed, which showed an excellent stability of the immobilized Thc_Cut1 (retained activity >94%) over 24 h reaction cycles when a solvent-free workup was used. Concerning a practical application of the biocatalyst's preparation, the production of oligomers with M values below 10 kDa is usually desired for the production of nanoparticles and for the synthesis of functional pre-polymers for coating applications that can be crosslinked in a second reaction step.

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Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?

Cited by 44 publications

References 81 publications

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

Screening of commercial enzymes for poly(ethylene terephthalate) (PET) hydrolysis and synergy studies on different substrate sources

His‐Tag Immobilization of Cutinase 1 From Thermobifida cellulosilytica for Solvent‐Free Synthesis of Polyesters

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