Cutinase: From molecular level to bioprocess development

Carvalho, Cristina; Aires-Barros, M. Raquel; Cabral, Joaquim M. S.

doi:10.1002/(sici)1097-0290(1999)66:1<17::aid-bit2>3.0.co;2-f

Cited by 216 publications

(145 citation statements)

References 93 publications

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“…The enzymatic hydrolysis by CcCUT1 and Optimyze 525 of the samples subjected to microscopic analysis (residue 6 and 7, Figure 1) was also analyzed by determining the fatty acids released (monomer-oligomer mix 2, Figure 1). The Free Fatty Acids Kit (Roche) used is limited to fatty acids with carbon chain lengths between C 8 and C 18 and does not therefore necessarily represent the total amount of suberin monomers released. The method can nevertheless be used for estimating the amounts of oligomers and monomers released.…”

Section: Resultsmentioning

confidence: 99%

“…CcCUT1 is able to hydrolyze both apple cutin and birch outer bark suberin (17). Due to their broad substrate specificities cutinases have been proposed for various applications for processing diverse raw materials (18). With this perspective, these enzymes are potential tools in the food industry as they may be applied to improve the exploitation of several plant materials and for recovering valuable polyfunctional monomers from polyesters such as suberins and cutins.…”

Section: Introductionmentioning

confidence: 99%

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Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Järvinen¹,

Silvestre²,

Holopainen³

et al. 2009

J. Agric. Food Chem.

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Chemical and enzymatic depolymerizations of suberin isolated from potato peel (Solanum tuberosum var. Nikola) were performed under various conditions. Enzymatic hydrolysis with cutinase CcCut1 and chemical methanolysis with NaOMe of suberin yielded monomeric fragments, which were identified as TMS derivatives with GC-MS and GC-FID. The solid, hydrolysis-resistant residues were analyzed with solid state 13 C CPMAS NMR, FT-IR, and microscopic methods. Methanolysis released more CHCl 3 -soluble material than the cutinase treatment when determined gravimetrically. Interestingly, cutinase-catalyzed hydrolysis produced higher proportions of aliphatic monomers than hydrolysis with the NaOMe procedure when analyzed by GC in the form of TMS derivatives. Monomers released by the two methods were mainly R,ω-dioic acids and ω-hydroxy acids, but the ratios of the detected monomers were different, at 40.0 and 32.7% for methanolysis and 64.6 and 8.2% for cutinase, respectively. Thus, cutinase CcCut1 showed higher activity toward ester bonds of R,ω-dioic acids than toward the bonds of ω-hydroxy acids. The most abundant monomeric compounds were octadec-9-ene-1,18-dioic acid and 18-hydroxyoctadec-9-enoic acid, which accounted for ca. 37 and 28% of all monomers, respectively. The results of the analyses of the chemical and enzymatic hydrolysis products were supported by the spectroscopic analyses with FT-IR and CPMAS 13 C NMR together with the analysis of the microstructures of the hydrolysis residues by light and confocal microscopy.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Järvinen¹,

Silvestre²,

Holopainen³

et al. 2009

J. Agric. Food Chem.

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“…[13][14][15][16][17] O uso de micelas reversas, principalmente AOT, é a estratégia mais freqüentemente empregada na literatura, devido ao maior ganho de atividade obtido. 16 Micelas reversas são sistemas compostos por molé-culas anfifílicas que se auto-organizam de forma que seus grupamentos polares se orientam para a face interna e a parte apolar se encontra na face externa.…”

Section: Características Das Cutinasesunclassified

“…A presença do hexanol e o reduzido conteúdo de água promovem a estabilização da estrutura da enzima no interior das micelas aumentando sua termoestabilidade. 14,15 O emprego de enzimas encapsuladas em micelas reversas fornece uma área de interface muito grande, tornando possível a solubilização de substratos hidrofílicos e hidrofóbicos e freqüentemente aumentando a atividade catalítica. A separação dos produtos de reação bem como a recuperação da enzima são facilitados e constituem uma importante área de pesquisa relacionada ao uso de micelas.…”

Section: Compostos De Aromaunclassified

Cutinases fúngicas: propriedades e aplicações industriais

et al. 2008

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Recebido em 18/12/07; aceito em 20/6/08; publicado na web em 10/11/08 FUNGAL CUTINASES: PROPERTIES AND INDUSTRIAL APPLICATIONS -REVIEW.Cutinases (EC 3.1.1.74) are also known as cutin hidrolases. 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. They are also active in different reaction media, allowing their applications 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 review describes the characteristics, potential applications and new perspectives for these enzymes.Keywords: cutinase; industrial applications; biochemical characteristics. introduçÃoCutinases são enzimas que catalisam a hidrólise de um biopoliéster insolúvel, a cutina, componente estrutural da cutícula das plantas.1 Este poliéster é composto do seguintes ácidos graxos: ω-hidróxi ácidos graxos, ácido diidroxidróxi palmítico, e ácidos 18-hidróxi-9,10,-epóxi C 18 saturados e Δ12 insaturados, e ácidos 9,10,18-triidróxi C 18 saturados e Δ12 monoinsaturados. A composição da cutina é dependente da espécie, porém, em geral, em plantas de crescimento rápido predominam os ácidos de 16 carbonos, particularmente diidroxipalmitato, enquanto em plantas de crescimento lento uma mistura de ácidos de 16 e 18 carbonos é encontrada. A cutinase libera hidroliticamente todos os tipos de monômeros a partir do polímero. 2Além da hidrólise, assim como as lipases, as cutinases também são capazes de catalisar reações reversas, como esterificação, transesterificação (interesterificação, alcoólise e acidólise) e aminólise, sendo que a atividade de água do meio reacional é um dos fatores determinantes para cada classe de reação. 3,4 Segundo Brenda 5 a cutinase é classificada como EC 3.1.1.3 com nome recomendado de triacilglicerol lipase, e nome sistemático de triacilglicerolacil-hidrolase. Também é classificada, pela mesma fonte, como 3.1.l.74 com nome recomendado de cutinase e nome sistemático de cutina hidrolase, ou seja, uma esterase que hidrolisa a cutina, podendo agir e ser classificada também como lipase.As cutinases apresentam diversas características interessantes para aplicações em uma ampla gama de produtos, variando de detergentes a alimentos.6 Conseqüentemente, tem sido desenvolvida intensa pesquisa abordando suas estruturas, funções, purificação e aplicações, visando o desenvolvimento de novos processos empregando este grupo de enzimas. 1O presente artigo descreve as características e potenciais aplicações das cutinases fúngicas em processos industriais. Características das cutinasesCutinases são dos menores membros da família serina hidrolase, que apresenta a tríade catalítica clássica composta por serina, histidina e um grupo carboxil. A sub-família das cutinases consiste em ...

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“…Some enzymes are excreted actively through the plasma membrane [2,3]. Enzymes in the liquid are thought to erode the cuticle [4][5][6][7]. Cutinase and esterase activities in the matrix surrounding uredospores have been demonstrated to contribute to spore adhesion to the leaf cuticle [8].…”

Section: Introductionmentioning

confidence: 99%

G protein and MAPK signaling pathways control the ability of <i>Cochliobolus heterostrophus</i> to exploit different carbon sources

Degani

2014

ABC

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Phytopathogenic fungi are heterotrophic organisms that excrete a complex array of enzymes for digestion of plant host tissues. Regulation and coordination of extracellular enzyme production, according to growth conditions and fungus nutritional needs, may be controlled by conserved eukaryotic signaling elements such as G-protein subunits and mitogen-activated protein kinase (MAPK). These pathways are known to mediate a complex set of responses in fungi involved in development, reproduction and pathogenicity. Here, we used a series of mutants, deficient in G-protein α (cga1) or/and β subunits or in MAPK, to test their contribution to the ability of Cochliobolus heterostrophus to utilize different carbon sources. In saprophytic culture, the G-protein α subunit mutant strains had WT levels of cellulase, pectinase and protease degradation activities, but it grew significantly slower on minimal medium containing maltose. This weakened ability implies an essential role of the CGA1 signaling in some poor nutritional environments. Remarkably, the MAPK null mutant failed to achieve the WT (and cga1) growth rate on cellulose as a sole carbon and did not grow at all for the first seven days of culture. An enzymatic activity test revealed that this strain significantly reduced cellulose extracellular degradation activity when grew on this medium. Deficiency in the MAPK encoding gene also led to reduced ability to grow on pectin, protein sources and maltose as a sole carbon. The evidence presented indicates a significant and nutrient-specific role of the G-protein and MAPK pathways in mediating growth of this fungus in different environments.

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Cutinase: From molecular level to bioprocess development

Cited by 216 publications

References 93 publications

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Cutinases fúngicas: propriedades e aplicações industriais

G protein and MAPK signaling pathways control the ability of <i>Cochliobolus heterostrophus</i> to exploit different carbon sources

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Cutinase: From molecular level to bioprocess development

Cited by 216 publications

References 93 publications

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Cutinases fúngicas: propriedades e aplicações industriais

G protein and MAPK signaling pathways control the ability of &lt;i&gt;Cochliobolus heterostrophus&lt;/i&gt; to exploit different carbon sources

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G protein and MAPK signaling pathways control the ability of <i>Cochliobolus heterostrophus</i> to exploit different carbon sources