Galactinol synthase enzyme activity influences raffinose family oligosaccharides (RFO) accumulation in developing chickpea (Cicer arietinum L.) seeds

2016 ◽  
Vol 125 ◽  
pp. 88-98 ◽  
Author(s):  
Manu P. Gangola ◽  
Sarita Jaiswal ◽  
Udhaya Kannan ◽  
Pooran M. Gaur ◽  
Monica Båga ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cicer Arietinum ◽  
Raffinose Family Oligosaccharides ◽  
Galactinol Synthase ◽  
Cicer Arietinum L

Further Characterization of Chickpea Isoflavone 7-O-Glucoside- 6"-O-malonate: malonylesterase: Evidence for a Highly Specific, Membrane-Bound Enzyme in Roots of Cicer arietinum L.

1987 ◽  
Vol 42 (3) ◽  
pp. 251-257 ◽  
Author(s):  
Walter Hinderer ◽  
Johannes Köster ◽  
Wolfgang Barz
Keyword(s):  
Enzyme Activity ◽  
Cicer Arietinum ◽  
Biochanin A ◽  
Cicer Arietinum L ◽  
Apparent Homogeneity ◽  
Malonyl Coa ◽  
Highly Sensitive ◽  
Membrane Bound

The specific malonylesterase from chickpea (Cicer arietinum L.), hydrolyzing biochanin A 7-O- glucoside-6″-O-malonate (BGM), has been purified to apparent homogeneity and characterized recently (Hinderer et al., Arch. Biochem. Biophys. 248, 570-578 [1986]). Its substrate specificity as well as the high molecular mass of the native enzyme were further investigated. The 5-deoxy- isoflavone conjugate corresponding to BGM, the formononetin 7-O-glucoside-6,,-O-malonate (FGM), was shown to be a substrate of the malonylesterase essentially as BGM. By contrast, methyl-BGM, a diester of malonic acid was a poor substrate. The purified enzyme completely lacked thioesterase activity with malonyl-CoA as substrate. The inability of the malonylesterase to hydrolyze synthetic acetyl or propionyl esters was further demonstrated with a highly sensitive fluorometric assay using esters of 4-methylumbelliferone. The enzyme-catalyzed hydrolysis of BGM was stimulated in the presence of dissociated carboxylic acids like citrate which was most effective at 30 mM and pH 7.5-8.0. The purified malonylesterase as well as the enzyme activity in crude extracts were totally excluded in gelchromatography with Ultrogel AcA 22. The enrichment of the enzyme activity in microsomal fractions gave strong evidence that the malonylesterase is membrane-bound in vivo. Stimulation of the enzyme activity in vitro by detergents indicates the presence of lipid material in the enzyme and the activity profiles obtained after sedimentation analyses suggest that purifica­tion of a distinct membrane-protein complex had been achieved.

DIFERENCIACIÓN DE ACCESIONES DE GARBANZO MEDIANTE CARACTERES MORFOLÓGICOS Y MOLECULARES

2018 ◽  
Vol 41 (4) ◽  
pp. 469-476
Author(s):  
Ernestina Valadez-Moctezuma ◽  
Anselmo de J. Cabrera-Hidalgo
Keyword(s):  
Cicer Arietinum ◽  
Cicer Arietinum L

El garbanzo (Cicer arietinum L.) es una de las principales leguminosas de grano cultivadas en el mundo. México es de los diez principales productores a nivel mundial con una producción total de 171 mil toneladas de grano. Este cultivo presenta alto nivel de autogamia y de monotonía genética, lo que dificulta la diferenciación de genotipos élite. En este estudio preliminar se evaluó la variabilidad de 57 genotipos de diferentes áreas geográficas mediante caracteres morfológicos y marcadores moleculares tipo RAPD e ISSR. El análisis de correspondencia múltiple mostró que los mayores valores discriminantes fueron el color de la flor azul y semillas grandes y de forma redondeada, pero el agrupamiento respectivo no diferenció a las accesiones, incluyendo las especies silvestres; sin embargo, el análisis UPGMA logró una mejor separación. Los marcadores RAPD aun cuando generaron perfiles de ADN, no fueron informativos, mientras que los ISSR diferenciaron a las 57 accesiones de C. arietinum utilizadas y a la especie silvestre C. reticulatum, lo que los hace buenos candidatos para caracterizar este cultivo. Este estudio sirvió como base para desarrollar otro sistema de marcadores moleculares más eficiente en esta especie.

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