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

The polymer and plastic sectors are under the urge of mitigating their environmental impact. The need for novel and more benign catalysts for polyester synthesis or targeted functionalization led, in recent years, to an increasing interest towards cutinases due to their natural ability to hydrolyze...

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Published in:Catalysts
Main Authors: FERRARIO, VALERIO, CESPUGLI, MARCO, GARDOSSI, Lucia, Pellis, Alessandro, Guebitz, Georg
Other Authors: Ferrario, Valerio, Cespugli, Marco, Gardossi, Lucia
Format: Article in Journal/Newspaper
Language:English
Published: 2016
Subjects:
Online Access:http://hdl.handle.net/11368/2889748
https://doi.org/10.3390/catal6120205
http://www.mdpi.com/2073-4344/6/12/205
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spelling ftunitriestiris:oai:arts.units.it:11368/2889748 2023-05-15T13:55:40+02:00 Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener? FERRARIO, VALERIO CESPUGLI, MARCO GARDOSSI, Lucia Pellis, Alessandro Guebitz, Georg Ferrario, Valerio Pellis, Alessandro Cespugli, Marco Guebitz, Georg Gardossi, Lucia 2016 ELETTRONICO http://hdl.handle.net/11368/2889748 https://doi.org/10.3390/catal6120205 http://www.mdpi.com/2073-4344/6/12/205 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000392482900025 volume:6 issue:12 firstpage:205 lastpage:219 numberofpages:15 journal:CATALYSTS http://hdl.handle.net/11368/2889748 doi:10.3390/catal6120205 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85008178726 http://www.mdpi.com/2073-4344/6/12/205 info:eu-repo/semantics/openAccess cutinase enzymatic polyesters synthesi green polymer synthesi enzymatic polymer hydrolysis info:eu-repo/semantics/article 2016 ftunitriestiris https://doi.org/10.3390/catal6120205 2023-04-09T06:13:50Z The polymer and plastic sectors are under the urge of mitigating their environmental impact. The need for novel and more benign catalysts for polyester synthesis or targeted functionalization led, in recent years, to an increasing interest towards cutinases due to their natural ability to hydrolyze ester bonds in cutin, a natural polymer. In this review, the most recent advances in the synthesis and hydrolysis of various classes of polyesters and polyamides are discussed with a critical focus on the actual perspectives of applying enzymatic technologies for practical industrial purposes. More specifically, cutinase enzymes are compared to lipases and, in particular, to lipase B from Candida antarctica, the biocatalyst most widely employed in polymer chemistry so far. Computational and bioinformatics studies suggest that the natural role of cutinases in attacking natural polymers confer some essential features for processing also synthetic polyesters and polyamides. Article in Journal/Newspaper Antarc* Antarctica Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) Catalysts 6 12 205
institution Open Polar
collection Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste)
op_collection_id ftunitriestiris
language English
topic cutinase
enzymatic polyesters synthesi
green polymer synthesi
enzymatic polymer hydrolysis
spellingShingle cutinase
enzymatic polyesters synthesi
green polymer synthesi
enzymatic polymer hydrolysis
FERRARIO, VALERIO
CESPUGLI, MARCO
GARDOSSI, Lucia
Pellis, Alessandro
Guebitz, Georg
Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?
topic_facet cutinase
enzymatic polyesters synthesi
green polymer synthesi
enzymatic polymer hydrolysis
description The polymer and plastic sectors are under the urge of mitigating their environmental impact. The need for novel and more benign catalysts for polyester synthesis or targeted functionalization led, in recent years, to an increasing interest towards cutinases due to their natural ability to hydrolyze ester bonds in cutin, a natural polymer. In this review, the most recent advances in the synthesis and hydrolysis of various classes of polyesters and polyamides are discussed with a critical focus on the actual perspectives of applying enzymatic technologies for practical industrial purposes. More specifically, cutinase enzymes are compared to lipases and, in particular, to lipase B from Candida antarctica, the biocatalyst most widely employed in polymer chemistry so far. Computational and bioinformatics studies suggest that the natural role of cutinases in attacking natural polymers confer some essential features for processing also synthetic polyesters and polyamides.
author2 Ferrario, Valerio
Pellis, Alessandro
Cespugli, Marco
Guebitz, Georg
Gardossi, Lucia
format Article in Journal/Newspaper
author FERRARIO, VALERIO
CESPUGLI, MARCO
GARDOSSI, Lucia
Pellis, Alessandro
Guebitz, Georg
author_facet FERRARIO, VALERIO
CESPUGLI, MARCO
GARDOSSI, Lucia
Pellis, Alessandro
Guebitz, Georg
author_sort FERRARIO, VALERIO
title Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?
title_short Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?
title_full Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?
title_fullStr Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?
title_full_unstemmed Nature Inspired Solutions for Polymers: Will Cutinase Enzymes Make Polyesters and Polyamides Greener?
title_sort nature inspired solutions for polymers: will cutinase enzymes make polyesters and polyamides greener?
publishDate 2016
url http://hdl.handle.net/11368/2889748
https://doi.org/10.3390/catal6120205
http://www.mdpi.com/2073-4344/6/12/205
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation info:eu-repo/semantics/altIdentifier/wos/WOS:000392482900025
volume:6
issue:12
firstpage:205
lastpage:219
numberofpages:15
journal:CATALYSTS
http://hdl.handle.net/11368/2889748
doi:10.3390/catal6120205
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85008178726
http://www.mdpi.com/2073-4344/6/12/205
op_rights info:eu-repo/semantics/openAccess
op_doi https://doi.org/10.3390/catal6120205
container_title Catalysts
container_volume 6
container_issue 12
container_start_page 205
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