Isolation and characterization of a cutinase from Fusarium roseum culmorum and its immunological comparison with cutinases from F. solani pisi

Soliday, Charles L.; Kolattukudy, P. E.

doi:10.1016/0003-9861(76)90172-7

Cited by 53 publications

(24 citation statements)

References 15 publications

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“…Thus, it appears that the nonlinear increase in the rate of release of 14C from cutin by increasing protein concentrations might be caused by some physicochemical feature of the assay with the insoluble polymer. However, similar assays with cutinase from fungal sources did not show any unusual concentration dependence (22,25).…”

Section: Effect Of Enzyme Concentration and Time On Hydrolysis Ofmentioning

confidence: 71%

“…Using cytochemical techniques and artificial substrates, esterases have been shown to be released by pollen (12,20,26). One or more of these esterases previously observed might have been cutinase, as it is known that fungal cutinases also hydrolyze a variety of esters (22,25). The so-called poral esterase (1) …”

Section: Effect Of Enzyme Concentration and Time On Hydrolysis Ofmentioning

confidence: 98%

“…Since the assay involves only the release of 14C into the medium, all bond cleavages catalyzed by the enzyme might not be measured with such an assay. The enzyme preparation also catalyzed hydrolysis of certain model substrates, which are known to be substrates for purified fungal cutinases (22,23,25). With these model substrates, namely p-nitrophenyl esters of fatty acids, the rate of hydrolysis increased in a linear fashion with increasing protein concentrations in the range which did not give linear response with the assays using labeled cutin (Fig.…”

Section: Effect Of Enzyme Concentration and Time On Hydrolysis Ofmentioning

confidence: 99%

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Production of a Novel Extracellular Cutinase by the Pollen and the Chemical Composition and Ultrastructure of the Stigma Cuticle of Nasturtium (Tropaeolum majus)

1977

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Germinating nasturtium polen (Tropaeolum majus) is shown to excrete an enzyme(s) which hydrolyzes all types of monomers from biosyntheticafly labeled cutin andp-nitrophenyl esters, which are model substrates for fungal cutases. The poUen cutinase showed an optimum pH near 6.5 and was inhibited by thiol-directed reagents such as phydroxymercurnbenzoate and N-ethyl maleimide but not by diisopropylfluoropbosphate, an "active serine"-directed reagent indicating that the polen enzyme is an "-SH cutinase" unlike the fungal enzyme which is a serine cutinase. Excretion of the pollen cutinse into the extracelular fluid was complete within 4 to 6 bourn at 30 C. Since actinomycin D and cyclohexinide showed little effect on the level of cutinase excreted, it appears that cutinase is an enzyme synthesized prior to germination. Release of cutinase into the medium did not require germination. Electron microscopy revealed the presence of a continuous cutin layer on mature stigma with extensive folds, which are proposed to play a role similar to that played by the celular papifine found in the stigma of other plants. Chemical analysis of stigma cutin by depolymerization and combined gas-liquid chromatogrphy and mass spectrometry showed that this cutin consists of mainly the C,6 family of acids. The major (70%) components were dihydroxy C,6 acids which consisted of 10,16-(64%), 9,16-(16%), 8,16-(12%), and 7,16-(8%) dihydroxy palmitic acid. Deuterium-labeling studies sbowed the presence of 16-oxo-9-hydroxy C,6 acid and 16-oxo-10-hydroxy C,6 add in this cutin. The biochemical and ultratctrl studies indicate that the poUen tube may gain entry into stigma using cutinase excreted by the pollen.tal evidence for the presence of cutinase in germinating pollen consisted of the demonstration that addition of cutin preparation to germinating pollen caused a slight increase in titratable acidity (7,18). With this increase as a measure of cutinase, it was found that the presence of cutinase in germinating pollen was a characteristic of plants which have ' cutinized" stigma. Since fungal extracts also catalyzed release of titratable acids in the presence of cutin, including a cutin preparation from stigma surface, it was suggested that cutinase of germinating pollen was "identical with" cutinase detected in molds (7). Cutinase from neither molds nor pollen had been isolated or characterized and, therefore, it was not possible to compare the enzymes from the two sources. Recently, fungal cutinases, isolated in homogeneous form, have been characterized (22, 23. 25). The products released from cutin by the germinating pollen were also not characterized and therefore it was difficult to determine whether the pollen enzyme released all types of monomers of cutin or only the peripheral fatty acids.In this paper we demonstrate, with the use of radioactive cutin, that germinating pollen from nasturtium excrete an enzyme(s) which releases all types of monomers from apple cutin. Results which suggest that the appearance of this cutinase activity...

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Section: Effect Of Enzyme Concentration and Time On Hydrolysis Ofmentioning

confidence: 71%

Section: Effect Of Enzyme Concentration and Time On Hydrolysis Ofmentioning

confidence: 98%

Section: Effect Of Enzyme Concentration and Time On Hydrolysis Ofmentioning

confidence: 99%

See 1 more Smart Citation

Production of a Novel Extracellular Cutinase by the Pollen and the Chemical Composition and Ultrastructure of the Stigma Cuticle of Nasturtium (Tropaeolum majus)

1977

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“…The use of these and other techniques have revealed fungal cutinases of about 22 kDa (Castro-Ochoa et al, 2010;Degani, 2015). Soliday & Kolattukudy (1976) reported that Fusarium roseum culmorum produced cutinases and non-specific esterases that hydrolyzed cutin and p-NPB in a similar way to those cutinases from F. oxysporum, which molecular weight was 24.3 kDa. In this paper, we were able to observe by zymography, esterase activity bands between 72 and 104 in the four different media, with a molecular weight of approximately 50 kDa..…”

Section: Discussionmentioning

confidence: 99%

Reducción de astringencia del pseudofruto de marañón (Anacardium occidentale L.) como alternativa para consumo humano

et al. 2016

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Cutinase is a very versatile enzyme due to the wide range of substrates that it can use. It has application in several biotechnological areas, acting as biocatalysts in the food industry, in detergents as well as in biodegradation of polymers and other toxic substances. In this research, glucose consumption, protein content, biomass and cutinase production by Fusarium culmorum were evaluated. Cutinolitic activity was observed using gel zymography. This fungus was grown on culture media containing glucose and different concentrations of apple cutin (0, 1, 3 and 10 g/L) in solid-state fermentation. F. culmorum showed the highest production of biomass, protein and cutinase in medium supplemented with 10 g of cutin/L. Glucose uptake was inversely proportional to the cutin concentration. Medium lacking cutin showed the fastest glucose consumption. Heavily stained bands were observed in the gel with increasing concentrations of cutin after 72 h, showing a molecular weight of 50 kDa. These results shown that apple cutin induced cutinase production and was also used as carbon source. It was also observed that glucose did not act as a repressor of cutinase production. Keywords: cutinase, Fusarium culmorum, solid-state fermentation. RESUMENLa versatilidad de la cutinasa es debida a los diversos sustratos que puede emplear. Estas enzimas tienen aplicación en distintas áreas biotecnológicas, lo que las convierte en atractivos biocatalizadores para la industria alimentaria, de detergentes, así como en la degradación de polímeros y sustancias tóxicas. En este trabajo se evaluó el consumo de glucosa, contenido de proteína, la producción de biomasa y cutinasas por el hongo Fusarium culmorum crecido en medios conteniendo glucosa y diferentes concentraciones de cutina de manzana (0, 1, 3 y 10 g/L) en fermentación sólida. La actividad cutinolítica fue observada empleando zimografia. F. culmorum mostró la mayor producción de biomasa, proteína y cutinasas en el medio adicionado con 10 g de cutina/L. El consumo de glucosa fue inversamente proporcional a la concentración de cutina. La glucosa se consumió más rápido en el medio sin adición de cutina. El aumento en la concentración de cutina de manzana incremento la intensidad en la banda mostrada en el zimograma a partir de las 72 h, cuyo peso molecular fue de 50 kDa. Estos resultados muestran que la cutina de manzana indujo la producción de cutinasa y que fue usada como fuente de carbono. La glucosa no actúa como un represor de la producción de cutinasas.Palabras clave: cutinasa, fermentación sólida, Fusarium culmorum.

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“…Previous workers have isolated extracellular esterases from many organisms with the ability to depolymerize cutin (9,28,32,46,50,53) and have shown that for some, the cutin esterase is necessary for pathogen penetration of the intact cuticle (30,31,35). Penetration of the protective suberin layer covering underground tubers by S. scabies may also involve the production and secretion of suberin-degrading enzymes.…”

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confidence: 99%

Cloning, sequencing, and regulation of expression of an extracellular esterase gene from the plant pathogen Streptomyces scabies

1990

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The gene that encodes the extraceliular esterase produced by Streptomyces scabies has been cloned and sequenced. The gene was identified by hybridization to a synthetic oligonucleotide that corresponds to the amino-terminal amino acid sequence determined for the secreted form of the esterase. Nucleotide sequence analysis predicted a 345-amino-acid open reading frame, a putative ribosome-binding site, and 39 amino acids at the amino terminus of the sequence that is not found in the secreted protein. This 39-amino-acid sequence has many of the characteristics common to known signal peptides. End mapping the esterase transcript revealed a single 5' end of the mRNA located 51 nucleotides upstream from the start point for translation. Northern (RNA) hybridization analysis of the esterase message by using the cloned esterase gene as a probe indicated that the esterase mRNA is about 1,440 nucleotides in length and was detected only when the cells were grown in the presence of zinc. These results suggest that the level of esterase mRNA detected in the cells is regulated by zinc.

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Isolation and characterization of a cutinase from Fusarium roseum culmorum and its immunological comparison with cutinases from F. solani pisi

Cited by 53 publications

References 15 publications

Production of a Novel Extracellular Cutinase by the Pollen and the Chemical Composition and Ultrastructure of the Stigma Cuticle of Nasturtium (Tropaeolum majus)

Production of a Novel Extracellular Cutinase by the Pollen and the Chemical Composition and Ultrastructure of the Stigma Cuticle of Nasturtium (Tropaeolum majus)

Reducción de astringencia del pseudofruto de marañón (Anacardium occidentale L.) como alternativa para consumo humano

Cloning, sequencing, and regulation of expression of an extracellular esterase gene from the plant pathogen Streptomyces scabies

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