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Dive into the research topics where Blanca Vioque is active.

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Featured researches published by Blanca Vioque.


The Plant Cell | 2010

Mitochondrial β-Cyanoalanine Synthase Is Essential for Root Hair Formation in Arabidopsis thaliana

Irene García; José Castellano; Blanca Vioque; Roberto Solano; Cecilia Gotor; Luis C. Romero

The β-cyanoalanine synthase enzyme is responsible for detoxifying the cyanide generated during cellular metabolism, primarily in the synthesis of ethylene. This analysis of a null mutant of this enzyme indicates that cyanide can act in some developmental processes as a signaling molecule. Cyanide is stoichiometrically produced as a coproduct of the ethylene biosynthesis pathway and is detoxified by β-cyanoalanine synthase enzymes. The molecular and phenotypical analysis of T-DNA insertion mutants of the mitochondrial β-cyanoalanine synthase CYS-C1 suggests that discrete accumulation of cyanide is not toxic for the plant and does not alter mitochondrial respiration rates but does act as a strong inhibitor of root hair development. The cys-c1 null allele is defective in root hair formation and accumulates cyanide in root tissues. The root hair defect is phenocopied in wild-type plants by the exogenous addition of cyanide to the growth medium and is reversed by the addition of hydroxocobalamin or by genetic complementation with the CYS-C1 gene. Hydroxocobalamin not only recovers the root phenotype of the mutant but also the formation of reactive oxygen species at the initial step of root hair tip growth. Transcriptional profiling of the cys-c1 mutant reveals that cyanide accumulation acts as a repressive signal for several genes encoding enzymes involved in cell wall rebuilding and the formation of the root hair tip as well as genes involved in ethylene signaling and metabolism. Our results demonstrate that mitochondrial β-cyanoalanine synthase activity is essential to maintain a low level of cyanide for proper root hair development.


Phytochemistry | 1981

Role of IAA-oxidase in the formation of ethylene from 1-aminocyclopropane-1-carboxylic acid

Agustín Vioque; Miguel A. Albi; Blanca Vioque

Abstract The IAA-oxidase system of olive tree ( Olea europea ) in the presence of its substrate, IAA, and cofactors, DCP and Mn 2 , forms ethylene from 1-aminocyclopropane-l-carboxylic acid (ACC) bound as a Schiffs base to pyridoxal phosphate. Similarly, olive leaf discs upon incubation with ACC liberate considerable amounts of ethylene. The results suggest that this IAA-oxidase system may be the one active in the last step in the biosynthesis of ethylene from methionine.


Phytochemistry | 1993

Effect of methyl jasmonate on ethylene biosynthesis and stomatal closure in olive leaves

Luis C. Sanz; Juan Carlos Fernandez-Maculet; Eduardo Gómez; Blanca Vioque; José M. Olías

Abstract The influence of methyl jasmonate (MeJA) on ethylene production and 1-aminocyclopropane-1-carboxylic acid (ACC) and malonyl-ACC (MACC) contents in olive leaf discs and detached leaves was investigated. In leaf discs, both ACC content and ethylene-forming enzyme (EFE) activity were clearly stimulated by 45 μM MEJA. In detached leaves MeJA treatment increased ACC content with no clear increase in ethylene production. When detached leaves were incubated with MeJA (45 μM) and ACC (1 mM), the total endogenous ACC content was significantly lower than that of leaves incubated only with ACC (1 mM). These data could be explained on the basis that MeJA caused stomatal closure, and hence reduced ACC uptake.


Plant Growth Regulation | 2002

Characterisation of the ACC oxidase activity in transgenic auxin overproducing tomato during ripening

José Castellano; Blanca Vioque

As part of our studies on the role of auxin in regulating the ethylenebiosynthesis during fruit ripening, in this paper we describe the functionalproperties of the ACC oxidase activity extracted from transgenic tomato(Lycopersicum esculentum Mill. cv. Ailsa craig)overexpressing the tryptophan monooxygenase or iaaM protein fromAgrobacterium tumefaciens that increases the auxin levels.Maximal activity was recovered by extracting the enzyme at pH 8.0 from fruitspicked three days after the onset of the colour change. The enzyme exhibits ahalf-life of 85 min, two relative maxima at 30 and 38°C, an optimum pH of 7.9 and an apparent Km forACC of 118 μM. Our results also show the first evidence of anallosteric type kinetic of the ACC oxidase activity with respect to itscosubstrate ascorbate, with an apparent Km of 12.5mM,estimated as the concentration which gave 50% Vmax.


Carbohydrate Polymers | 2017

Physical and functional properties of pectin-fish gelatin films containing the olive phenols hydroxytyrosol and 3,4-dihydroxyphenylglycol

Alejandra Bermúdez-Oria; Guillermo Rodríguez-Gutiérrez; Blanca Vioque; Fátima Rubio-Senent; Juan Fernández-Bolaños

This study describes the development of a composite edible film based on pectin and fish skin protein capable of protecting food from microbial attack and oxidative degradation. The film was prepared with glycerol as plasticizer and the antioxidant and antimicrobial phenolic compounds hydroxytyrosol (HT) and 3,4-dihydroxyphenylglycol (DHPG), extracted from olive fruit, as active agents. The influence of the concentration of plasticizer and active HT/DHPG on the mechanical and functional properties of the films was investigated, with values of water vapor permeability (WVP) between 0.13-0.22gmm/hm2kPa and oxygen permeability (OP) between 9.91-40.76cm3μm/m2dkPa. The release behavior in water at different pH values was also evaluated. The antimicrobial capacity of the novel food coating was tested on strawberries, a fruit with high perishability. The bioactive edible film containing HT/DHPG preserved the strawberries against mold during storage with a significant delay in visible decay.


Physiologia Plantarum | 1994

Extraction and biochemical characterization of 1-aminocyclopropane-1-carboxylic acid oxidase from pear

Blanca Vioque; José Castellano


Journal of Agricultural and Food Chemistry | 1998

In Vivo and in Vitro 1-Aminocyclopropane-1-carboxylic Acid Oxidase Activity in Pear Fruit: Role of Ascorbate and Inactivation during Catalysis

Blanca Vioque; José Castellano


European Food Research and Technology | 2000

Biochemical features and inhibitors of the 1-aminocyclopropane-1-carboxylic acid oxidase isolated from pear fruit

José Castellano; Blanca Vioque


European Food Research and Technology | 1997

Changes in cell-wall-degrading enzyme activities in stored olives in relation to respiration and ethylene production Influence of exogenous ethylene

Juan Fernández-Bolaños; Antonia Heredia; Blanca Vioque; José Castellano; Rafael Guillén


Physiologia Plantarum | 1990

3-Hydroxypropyl amide formation from 1-aminocyclopropane-1-carboxylic acid by a cell-free ethylene-forming system from olive leaves.

Blanca Vioque; Juan Carlos Fernandez-Maculet

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José Castellano

Spanish National Research Council

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Miguel A. Albi

Spanish National Research Council

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Agustín Vioque

Spanish National Research Council

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Juan Fernández-Bolaños

Spanish National Research Council

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Alejandra Bermúdez-Oria

Spanish National Research Council

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Antonia Heredia

Spanish National Research Council

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Antonio López

Spanish National Research Council

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Cecilia Gotor

Spanish National Research Council

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Eduardo Gómez

Spanish National Research Council

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