Which properties of cutinases are important for applications?

Nyyssölä, Antti

doi:10.1007/s00253-015-6596-z

Cited by 54 publications

(49 citation statements)

References 81 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We reasoned that an MOF with this unusual hierarchical pore structure would be especially suitable for the encapsulation of Fusarium solani pisi cutinase (PDB: 1CEX), an esterase that has shown promise as a biocatalyst in the preparation of aliphatic esters. [30][31][32][33] The sizes of the larger channels of NU-1000 match that of cutinase, an ellipsoid-shaped protein featuring a small-axis length of $3.0 nm. 34 These features, in addition to the high chemical (at pH 1-11) 35 and thermal stability (at >450 C) 29 of NU-1000, make this MOF a promising candidate material for use as a solid support in biocatalysis.…”

Section: The Bigger Picturementioning

confidence: 98%

Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks

Modica

Howarth

et al. 2016

Chem

317

254

View full text Add to dashboard Cite

Metal-organic frameworks (MOFs) are porous, crystalline materials comprised of metal nodes and organic linkers. Here, a Zr-based MOF named NU-1000 is used to encapsulate and protect an enzyme. The encapsulation and subsequent protection of enzymes in solid supports is important for the potential industrialization of enzymes as chemical catalysts. NU-1000 is shown to be capable of stabilizing the enzyme under harsh conditions, and in addition, the encapsulated enzyme is shown to maintain full functionality.

show abstract

Section: The Bigger Picturementioning

confidence: 98%

Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks

Modica

Howarth

et al. 2016

Chem

317

254

View full text Add to dashboard Cite

show abstract

“…Cutinases (EC: 3.1.1.74) are members of the alpha/beta hydrolase family of lipases (Kolattukudy, ; Longhi & Cambillau, ). The enzyme is able to hydrolyze fatty acids esters and emulsified triacylglycerol as efficiently as lipases, and therefore, it is considered an intermediate between esterases and lipases (https://www.ebi.ac.uk/enzymeportal/ec/3.1.1.74) (Nyyssölä, ). The enzyme plays an active role in (a) carbon acquisition for saprophytic growth, (b) adhesion of fungal structures to the host surface, and (c) the early stages of fungal penetration (Auyong et al, ).…”

Section: Introductionmentioning

confidence: 99%

Diversity, structure, and synteny of the cutinase gene ofColletotrichumspecies

Villafana

Rampersad

2020

Ecology and Evolution

View full text Add to dashboard Cite

Colletotrichum species complexes are among the top 10 economically important fungal plant pathogens worldwide because they can infect climacteric and nonclimacteric fruit at the pre and/or postharvest stages. C. truncatum is the major pathogen responsible for anthracnose of green and red bell pepper fruit worldwide. C. brevisporum was recently reported to be a minor pathogen of red bell pepper fruit in Trinidad, but has recently been reported as pathogenic to other host species in other countries. The ability of these phytopathogens to produce and secrete cutinase is required for dismantling the cuticle of the host plant and, therefore, crucial to the necrotrophic phase of their infection strategy. In vitro bioassays using different lipid substrates confirmed the ability of C. truncatum and C. brevisporum isolates from green and red bell peppers to secrete cutinase. The diversity, structure and organization and synteny of the cutinase gene were determined among different Colletotrichum species. Cluster analysis indicated a low level of nucleotide variation among C. truncatum sequences. Nucleotide sequences of C. brevisporum were more related to C. truncatum cutinase nucleotide sequences than to C. gloeosporioides. Cluster patterns coincided with haplotype and there was evidence of significant positive selection with no recombination signatures. The structure of the cutinase gene included two exons with one intervening intron and, therefore, one splice variant. Although amino acid sequences were highly conserved among C. truncatum isolates, diversity “hot spots” were revealed when the 66‐amino acid coding region of 200 fungal species was compared. Twenty cutinase orthologues were detected among different fungal species, whose common ancestor is Pezizomycotina and it is purported that these orthologues arose through a single gene duplication event prior to speciation. The cutinase domain was retained both in structure and arrangement among 34 different Colletotrichum species. The order of aligned genomic blocks between species and the arrangement of flanking protein domains were also conserved and shared for those domains immediately located at the N‐ and C‐terminus of the cutinase domain. Among these were an RNA recognition motif, translation elongation factor, signal peptide, pentatricopeptide repeat, and Hsp70 family of chaperone proteins, all of which support the expression of the cutinase gene. The findings of this study are important to understanding the evolution of the cutinase gene in C. truncatum as a key component of the biotrophic–necrotrophic switch which may be useful in developing gene‐targeting strategies to decrease the pathogenic potential of Colletotrichum species.

show abstract

“…Cutinolytic esterase (i.e., cutinase) is known as cutin hydrolase (EC 3.1.1.74) and it is an enzyme that catalyzes not only the cleavage of ester bonds in cutin but also in diverse soluble and insoluble esters, insoluble triglycerides, phthalates, plastics and others (Kim et al, 2003;Chen et al, 2013;Nyyssölä, 2015;Ferrario et al, 2016;Ferrer-Parra et al, 2018). Cutinase is an extracellular enzyme produced by several phytopathogenic fungi that grow in cutin as sole carbon source.…”

Section: Introductionmentioning

confidence: 99%

“…Cutin is a high molecular weight and insoluble biopolymer composed of epoxy and interesterified hydroxy fatty acids that forms the structural component of higher plants cuticle, and that function as a structural support (Pio & Macedo, 2009;Fich et al, 2016). Cutinase shares properties of lipase and esterase in its catalytic action, since it is a serine esterase with the classical Ser-His-Asp triad similar to several lipases and serine proteases (Nyyssölä, 2015). This enzyme presents a unique feature of being active regardless the presence of an oil-water interface, making it attractive as a biocatalyst for several promising industrial applications like inter-and intra-transesterification reactions (Pio & Macedo, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…These properties of cutinase are being used for several applications in agriculture, in the textile industry, in household detergents, in pharmaceuticals, in processing food and dairy, in biocatalysis, in detoxification of environmental pollutants etc. (Nyyssölä, 2015). Therefore, cutinase is an important industrial catalyst that replaces older technologies with environmentally friendly processes (Chen et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Production of cutinolytic esterase by Fusarium culmorum grown at different apple cutin concentrations in submerged fermentation

et al. 2019

View full text Add to dashboard Cite

Cutinolytic esterase (i.e., cutinase) is an enzyme that catalyzes the cleavage of ester bonds in cutin and also in diverse soluble and insoluble esters. It has application in several biotechnological areas, acting as biocatalysts in the food industry, in detergents, in biodegradation of polymers and other toxic substances, being important in biorremediation. In this research, specific growth rate, protein content, cutinolytic activity by biochemical tests and polyacrylamide gel electrophoresis, and growth and enzymatic kinetic parameters were determined for F. culmorum grown at different apple cutin concentrations (0.2, 2 and 20 g/L) in submerged fermentation. It was observed that biomass, protein content and enzymatic activity enhanced as cutin concentration increased in the media. A cutinase activity band of around 65 KDa was observed in zymograms of different cutin concentration. An additional cutinase activity band of around 90 KDa was also observed in zymograms of F. culmorum grown in 20 g of apple cutin/L. These studies showed that F. culmorum used apple cutin as the sole carbon source, which acted as a cutinase inducer. The highest-yielding parameters of cutinase were observed in 2 g of apple cutin/L. This research showed promising results in the cutinase induction for F. culmorum using a low concentration of apple cutin.

show abstract

Which properties of cutinases are important for applications?

Cited by 54 publications

References 81 publications

Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks

Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks

Diversity, structure, and synteny of the cutinase gene ofColletotrichumspecies

Production of cutinolytic esterase by Fusarium culmorum grown at different apple cutin concentrations in submerged fermentation

Contact Info

Product

Resources

About