Purification and characterization of pectate lyase from banana (Musa acuminata) fruits

Payasi, Anurag; Misra, P. K.; Sanwal, G.G.

doi:10.1016/j.phytochem.2006.02.003

Cited by 20 publications

(21 citation statements)

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“…It was originally thought that Pel is strictly a microbial enzyme, but pel genes have now been detected in many plant species or sources (cf. Payasi et al 2006). Pel activity has been demonstrated in banana fruit (Maŕin-Rodriguez et al 2003;Payasi and Sanwal 2003).…”

Section: Distributionmentioning

confidence: 99%

“…The only available report on purification of Pel to homogeneity from plant sources is from banana fruits. The specific activity of the homogenous enzyme from banana is low compared to the enzyme from microbial sources, as the initial enzyme activity in fruit is very low compared to microbial sources (Payasi et al 2006). Properties…”

Section: Purification Of Pelmentioning

confidence: 99%

“…It is probably a tetramer with a MM of 38 kDa for the monomer. The MM of banana Pel, as determined by SDS-PAGE is 43 kDa (Payasi et al 2006). On the bases of complete cDNA sequence, the MM of the translated Pel protein from Zinia elegans is assumed to be 44 kDa (Domingo et al 1998).…”

Section: Molecular Massmentioning

confidence: 99%

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Microbial pectate lyases: characterization and enzymological properties

Payasi

Sanwal

2008

World J Microbiol Biotechnol

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Pectate lyase plays an important role in plant pathogenesis. The enzyme is widely distributed in diverse families of microorganisms. The current knowledge including biochemical studies on microbial pectate lyases, such as isozymes, structure, reaction mechanism, purification and properties like molecular mass, pI, optimum pH and temperature, substrate specificity, metal ion requirement, inhibitors and activators, and kinetic parameters of the enzyme are reviewed.

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Section: Distributionmentioning

confidence: 99%

Section: Purification Of Pelmentioning

confidence: 99%

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Microbial pectate lyases: characterization and enzymological properties

Payasi

Sanwal

2008

World J Microbiol Biotechnol

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“…Por otro lado, la enzima PL cataliza la rotura de enlaces glicosídicos entre residuos de ácido galacturónico desmetilados mediante un mecanismo de β-eliminación. Esta enzima suele ser abundante en bacterias fitopatógenas, pero en frutos sólo se ha cuantificado actividad PL en banana (Payasi et al, 2006). En el caso de la fresa, el silenciamiento del gen FaplC que codifica una pectato liasa específica de fruto, también redujo el reblandecimiento del fruto maduro (Jiménez-Bermúdez et al, 2002).…”

Section: Introductionunclassified

Caracterización de indicadores de la calidad del fruto en líneas de fresa transgénicas con genes silenciados que codifican para enzimas pectinolíticas

Julio-González

Matas

Mercado

2018

Rev. colomb. biotecnol.

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Caracterización de indicadores de la calidad del fruto en líneas de fresa transgénicas con genes silenciados que codifican para enzimas pectinolíticas Characterization of quality traits in transgenic strawberry fruits with genes encoding pectinolytic enzymes down-regulated DOI: 10.15446/rev.colomb.biote.v20n1.73673 RESUMENSe han evaluado algunos indicadores de calidad del fruto en líneas transgénicas de fresa con los genes de poligalacturonasa FaPG1 (líneas PG) o pectato liasa FaplC (líneas APEL) silenciados. Se analizaron dos líneas independientes por genotipo transgéni-co. No se observaron diferencias en el contenido de sólidos solubles entre las líneas transgénicas y el control. De igual forma, la acidez total y el pH fueron similares en las líneas PG29, APEL21 y el control; sin embargo, la acidez de los frutos de las líneas PG62 y APEL39 fue superior al control. Los parámetros de color L*, a* y b* fueron similares en todos los genotipos; sin embargo, el contenido en antocianos fue menor en la línea APEL21. Los valores más altos de firmeza de fruto, estimada mediante un ensayo de extrusión, se observaron en las dos líneas transgénicas PG y en la línea APEL39. En cuanto a las pérdidas por goteo (drip loss), la línea APEL39 presentó un valor mayor que el control, pero la línea APEL21 registró valores menores. El contenido de compuestos fenólicos se analizó en la línea PG29, no encontrándose diferencias estadísticas con respecto al control. Finalmente, la capacidad del fruto para captar radicales libres fue ligeramente menor en la línea PG29 que en el control. Los resultados indican que el silenciamiento de los genes de pectinasas incrementa significativamente la firmeza de la fresa sin modificar sustancialmente pará-metros de calidad del fruto maduro como color, acidez, sólidos solubles o contenido en antocianos.Palabras clave: maduración de frutos, pared celular, pectinas, postcosecha, transformación genética. ABSTRACTSome quality traits of transgenic strawberry fruits with low levels of expression of the pectinase genes FaPG1 (PG lines) or FaplC gene (APEL lines) were evaluated. Two independent lines per transgenic genotype were analyzed. Soluble solids were similar in control and transgenic lines. Similarly, pH and titratable acidity was similar in lines PG29, APEL21 and control; however, lines PG62 and APEL39 showed acidity values higher than the control. The color parameters L*, a* and b* were similar in control and transgenic fruits; however, line APEL21 displayed a lower value of anthocyanin content. The highest values of fruit firmness, measured with an extrusion test, were observed in both PG transgenic lines and in the APEL39 line. Regarding the drip loss, APEL39 line showed a higher value than the control, but the APEL21 line displayed lower values. The content of phenolic compounds was analyzed in line PG29, not observing significant differences with the control. Finally, the antiradical activity of the fruit was slightly lower in the line PG29 than in the control. The results obtained indicate that...

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“…This strain produces some lyases during the growth, and degrades cellouronate by cleaving glycoside bonds through b-elimination, resulting in the formation of depolymerized products having double bonds between C4 and C5 at the non-reducing termini. Also in the case of natural polyuronates such as alginate (Rehm 1998;Yoon et al 2000;Hashimoto et al 2000;Suzuki et al 2006;Ochiai et al 2006), pectin (Pissavin et al 1998;Shevchik et al 1999a, b;Benten et al 2000;Kluskens et al 2005;Klug-Santner et al 2006;Payasi et al 2006), xanthan (Hashimoto et al 1998(Hashimoto et al , 2001 and hyaluronan (Ponnuraj and Jedrzejas 2000;Oettl et al 2003), lyases predominantly take part in their enzymatic degradation. In a previous paper (Konno et al 2006), cellouronate lyase-I (CUL-I) was purified from the cell-free extracts of Brevundimonas sp.…”

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confidence: 99%

Purification and characterization of exo-type cellouronate lyase

et al. 2007

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A bacterial strain, Brevundimonas sp. SH203, has an ability to degrade cellouronate, b-(1?4)-linked polyglucuronic acid sodium salt, which is artificially prepared from regenerated cellulose by TEMPO (2,2,6,6-tetramethylpiperidine-1-oxyl radical)-mediated oxidation. In a previous paper, an endo-type cellouronate lyase (CUL-I) has been isolated from the strain. In this paper, we purified another cellouronate lyase, CUL-II, from cell-free extracts of Brevundimonas sp. SH203. CUL-II was a monomeric protein with a molecular mass of 56 kDa by size exclusion chromatography and 62 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and most active at pH 7.5. CUL-II formed monomers in a small quantity from cellouronate without forming any intermediate oligomers, whereas it degraded C4 0 -C5 0 unsaturated cellouronate dimer more easily. Thus, CUL-II behaves as an exo-type lyase in degradation of cellouronate. When CUL-I and CUL-II were simultaneously treated to cellouronate, it was degraded to monomers more efficiently than treatment with one enzyme alone, CUL-I or CUL-II. Hence, cellouronate is synergistically degraded to monomers by Brevundimonas sp. SH203 by endo-and exo-type lyases, CUL-I and CUL-II, respectively.

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Purification and characterization of pectate lyase from banana (Musa acuminata) fruits

Cited by 20 publications

References 41 publications

Microbial pectate lyases: characterization and enzymological properties

Microbial pectate lyases: characterization and enzymological properties

Caracterización de indicadores de la calidad del fruto en líneas de fresa transgénicas con genes silenciados que codifican para enzimas pectinolíticas

Purification and characterization of exo-type cellouronate lyase

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