Literature DB >> 25981992

Which properties of cutinases are important for applications?

Antti Nyyssölä1.   

Abstract

Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to α/β hydrolases. They are serine esterases with the classical Ser-His-Asp triad similar to several lipases and serine proteases. In nature, cutinases catalyse the hydrolysis of the polyesters of the cuticle and the suberin layers, which protect plant surfaces. Cutinase production is typical for plant pathogenic fungi, but also, bacterial cutinases and cutinases from plant pollen have been discovered. Cutinases are promiscuous esterases catalysing reactions with a wide range of different substrates, such as short-chain soluble esters, water-insoluble medium and long-chain triacylglycerols, polyesters and waxes. In the current work, an overview is given on suggested applications of cutinases in the textile industry, in laundry detergents, in processing of biomass and food, in biocatalysis and in detoxification of environmental pollutants. The applications are discussed from the point of view of cutinase properties-which properties of cutinases are already advantageous and which would be desired. In addition, improvements that have been made on cutinase performance by protein and reaction engineering are reviewed.

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Year:  2015        PMID: 25981992     DOI: 10.1007/s00253-015-6596-z

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  7 in total

1.  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

2.  Production of cutinase from Fusarium falciforme and its application for hydrophilicity improvement of polyethylene terephthalate fabric.

Authors:  Taweeporn Sooksai; Wichanee Bankeeree; Usa Sangwatanaroj; Pongtharin Lotrakul; Hunsa Punnapayak; Sehanat Prasongsuk
Journal:  3 Biotech       Date:  2019-10-09       Impact factor: 2.406

3.  Structure-function analysis of two closely related cutinases from Thermobifida cellulosilytica.

Authors:  Jenny Arnling Bååth; Vera Novy; Leonor V Carneiro; Georg M Guebitz; Lisbeth Olsson; Peter Westh; Doris Ribitsch
Journal:  Biotechnol Bioeng       Date:  2021-11-17       Impact factor: 4.395

Review 4.  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

5.  Extracellular secretion of a cutinase with polyester-degrading potential by E. coli using a novel signal peptide from Amycolatopsis mediterranei.

Authors:  Yeqi Tan; Gary T Henehan; Gemma K Kinsella; Barry J Ryan
Journal:  World J Microbiol Biotechnol       Date:  2022-02-23       Impact factor: 3.312

6.  Production of secretory cutinase by recombinant Saccharomyces cerevisiae protoplasts.

Authors:  Hideki Aoyagi; Yoichi Katakura; Akio Iwasaki
Journal:  Springerplus       Date:  2016-02-24

7.  Spatially confined lignin nanospheres for biocatalytic ester synthesis in aqueous media.

Authors:  Mika Henrikki Sipponen; Muhammad Farooq; Jari Koivisto; Alessandro Pellis; Jani Seitsonen; Monika Österberg
Journal:  Nat Commun       Date:  2018-06-12       Impact factor: 14.919

  7 in total

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