Literature DB >> 19203649

Cutinases: properties and industrial applications.

Tatiana Fontes Pio1, Gabriela Alves Macedo.   

Abstract

Cutinases, also known as cutin hydrolases (EC 3.1.1.74) are enzymes first discovered from phytopathogenic fungi that grow on cutin as the sole carbon source. Cutin is a complex biopolymer composed of epoxy and hydroxy fatty acids, and forms the structural component of higher plants cuticle. These enzymes share catalytic properties of lipases and esterases, presenting a unique feature of being active regardless the presence of an oil-water interface, making them interesting as biocatalysts in several industrial processes involving hydrolysis, esterification, and trans-esterification reactions. Cutinases present high stability in organic solvents and ionic liquids, both free and microencapsulated in reverse micelles. These characteristics allow the enzyme application in different areas such as food industry, cosmetics, fine chemicals, pesticide and insecticide degradation, treatment and laundry of fiber textiles, and polymer chemistry. The present chapter describes the characteristics, potential applications, and new perspectives for these enzymes.

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Year:  2009        PMID: 19203649     DOI: 10.1016/S0065-2164(08)00804-6

Source DB:  PubMed          Journal:  Adv Appl Microbiol        ISSN: 0065-2164            Impact factor:   5.086


  8 in total

1.  Enhanced cutinase-catalyzed hydrolysis of polyethylene terephthalate by covalent fusion to hydrophobins.

Authors:  Doris Ribitsch; Enrique Herrero Acero; Agnieszka Przylucka; Sabine Zitzenbacher; Annemarie Marold; Caroline Gamerith; Rupert Tscheließnig; Alois Jungbauer; Harald Rennhofer; Helga Lichtenegger; Heinz Amenitsch; Klaus Bonazza; Christian P Kubicek; Irina S Druzhinina; Georg M Guebitz
Journal:  Appl Environ Microbiol       Date:  2015-03-20       Impact factor: 4.792

2.  A Novel Actinobacterial Cutinase Containing a Noncatalytic Polymer-Binding Domain.

Authors:  Kofi Abokitse; Stephan Grosse; Hannes Leisch; Christopher R Corbeil; Florence Perrin-Sarazin; Peter C K Lau
Journal:  Appl Environ Microbiol       Date:  2021-10-27       Impact factor: 5.005

3.  Characterization of CpdC, a large-ring lactone-hydrolyzing enzyme from Pseudomonas sp. strain HI-70, and its use as a fusion tag facilitating overproduction of proteins in Escherichia coli.

Authors:  Yali Xu; Stephan Grosse; Hiroaki Iwaki; Yoshie Hasegawa; Peter C K Lau
Journal:  Appl Environ Microbiol       Date:  2013-09-13       Impact factor: 4.792

4.  Two novel class II hydrophobins from Trichoderma spp. stimulate enzymatic hydrolysis of poly(ethylene terephthalate) when expressed as fusion proteins.

Authors:  Liliana Espino-Rammer; Doris Ribitsch; Agnieszka Przylucka; Annemarie Marold; Katrin J Greimel; Enrique Herrero Acero; Georg M Guebitz; Christian P Kubicek; Irina S Druzhinina
Journal:  Appl Environ Microbiol       Date:  2013-05-03       Impact factor: 4.792

5.  Cloning, Expression and Characterization of a Thermostable Esterase HydS14 from Actinomadura sp. Strain S14 in Pichia pastoris.

Authors:  Pichapak Sriyapai; Fusako Kawai; Somjai Siripoke; Kosum Chansiri; Thayat Sriyapai
Journal:  Int J Mol Sci       Date:  2015-06-12       Impact factor: 5.923

6.  Genome-wide transcriptional profiling of Botrytis cinerea genes targeting plant cell walls during infections of different hosts.

Authors:  Barbara Blanco-Ulate; Abraham Morales-Cruz; Katherine C H Amrine; John M Labavitch; Ann L T Powell; Dario Cantu
Journal:  Front Plant Sci       Date:  2014-09-03       Impact factor: 5.753

Review 7.  Microbial enzymes: industrial progress in 21st century.

Authors:  Rajendra Singh; Manoj Kumar; Anshumali Mittal; Praveen Kumar Mehta
Journal:  3 Biotech       Date:  2016-08-19       Impact factor: 2.406

Review 8.  Current Knowledge on Polyethylene Terephthalate Degradation by Genetically Modified Microorganisms.

Authors:  Aneta K Urbanek; Katarzyna E Kosiorowska; Aleksandra M Mirończuk
Journal:  Front Bioeng Biotechnol       Date:  2021-11-30
  8 in total

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