Which properties of cutinases are important for applications?

Research output: Contribution to journalArticleScientificpeer-review

14 Citations (Scopus)

Abstract

Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to a/ß 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.
Original languageEnglish
Pages (from-to)4931-4942
JournalApplied Microbiology and Biotechnology
Volume99
Issue number12
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Fingerprint

Polyesters
cutinase
Biocatalysis
Textile Industry
Protein Engineering
Environmental Pollutants
Food Handling
Waxes
Serine Proteases
Hydrolases
Esterases
Pollen
Lipase
Detergents
Biomass
Esters
Triglycerides
Hydrolysis
Fungi
Water

Keywords

  • cutin
  • suberin
  • cutinase
  • esterase
  • applications

Cite this

@article{4c1506f104634b9b8a5cb2744cae056b,
title = "Which properties of cutinases are important for applications?",
abstract = "Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to a/{\ss} 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.",
keywords = "cutin, suberin, cutinase, esterase, applications",
author = "Antti Nyyss{\"o}l{\"a}",
year = "2015",
doi = "10.1007/s00253-015-6596-z",
language = "English",
volume = "99",
pages = "4931--4942",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "Springer",
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}

Which properties of cutinases are important for applications? / Nyyssölä, Antti.

In: Applied Microbiology and Biotechnology, Vol. 99, No. 12, 2015, p. 4931-4942.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Which properties of cutinases are important for applications?

AU - Nyyssölä, Antti

PY - 2015

Y1 - 2015

N2 - Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to a/ß 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.

AB - Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to a/ß 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.

KW - cutin

KW - suberin

KW - cutinase

KW - esterase

KW - applications

U2 - 10.1007/s00253-015-6596-z

DO - 10.1007/s00253-015-6596-z

M3 - Article

VL - 99

SP - 4931

EP - 4942

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 12

ER -