Agronomic Evaluation and Chemical Characterization of Vahl. over 3 Consecutive Years Cultivated Under Harsh Climatic Conditions in Southeast Spain.

The cultivation of , Spanish sage, makes an important contribution to the economy of many rural areas in Southeastern Spain. This aromatic plant species is characterized by high intraspecific variability, which makes the selection process for the establishment of homogeneous crops difficult. Additionally, imminent climate change threatens to reduce its production, especially when cultivated in drylands.

Agronomic Evaluation and Chemical Characterization of Medik. under the Semiarid Conditions of the Spanish Southeast.

is one of the main rainfed crops of aromatic and medicinal plants produced in Spain. As a global concern, the agronomic productivity of this aromatic crop is also threatened by the consequences of imminent climate change. On this basis, the study of the agronomic production of two drought-tolerant ecotypes, after three years of cultivations practices, constitutes the main objective of the present study.

Biocidal Potential and Chemical Composition of Industrial Essential Oils from Hyssopus officinalis, Lavandula × intermedia var. Super, and Santolina chamaecyparissus.

This work presents the biocidal (insecticidal, ixodicidal, nematicidal, and phytotoxic) effects and chemical compositions of three essential oils obtained from the industrial steam distillation (IEOs) of hyssop (Hyssopus officinalis L.), lavandin (Lavandula × intermedia or L. × hybrida var.

A colorimetric method for determination of γ-glutamyl-S-ethenyl-cysteine in narbon vetch (Vicia narbonensis L.) seeds.

A new colorimetric method based on the bleaching of the iodoplatinate ion has been developed for fast and easy determination of γ-glutamyl-S-ethenyl-cysteine (GEC) in narbon vetch (Vicia narbonensis L.) seeds. The calibration curve showed a good correlation (r(2)=0.

Characterisation and foaming properties of hydrolysates derived from rapeseed isolate.

Two hydrolysis methods used to obtain rapeseed isolate derivates were compared: chemical hydrolysis performed under alkaline conditions and pepsic proteolysis performed under acidic conditions. The mean molecular weights obtained for the hydrolysates varied from 26 to 2.5 kDa, depending on the level of hydrolysis.

Emulsifying properties of acylated rapeseed (Brassica napus L.) peptides.

A peptide fraction having an average size of 5.6 amino acids has been purified from a rapeseed hydrolyzate, acylated using C(10)-C(14) acyl chlorides, and the surface tension values at the air-water interface and emulsifying properties studied. As compared with standard surface-active proteins, such as bovine serum albumin (BSA), and with detergents such as sodium dodecyl sulfate (SDS), acylated peptides exhibited particular surface characteristics.

Alcalase rapeseed inhibitors: purification and partial characterization.

Extensive rapeseed protein hydrolysate obtained sequentially with Alcalase and Flavourzyme showed inhibitory activity towards Alcalase. Inhibitory activity decreased as the hydrolytic process progressed probably by heat denaturation and/or partial protease degradation. Alcalase rapeseed inhibitors were purified by gel filtration and subsequent ion exchange chromatography.

Production of extensive chickpea (Cicer arietinum L.) protein hydrolysates with reduced antigenic activity.

Chickpea protein isolate was used as starting material for the production of hypoallergenic protein hydrolysates. Western blotting of the protein isolate showed that IgE in sensitized patient sera strongly bound to the basic polypeptidic chains and recognized the acidic ones of 11S globulin. During the hydrolysis process by the individual and/or sequential action of endo- and exoproteases, a high reduction of antigenic activity was observed.

Interaction of chickpea (Cicer arietinum L.) legumin with oxidized linoleic acid.

Chickpea legumin has been purified and incubated under oxidizing conditions with linoleic acid to investigate the influence of this acid on the structure and nutritional quality of the protein. At the end of the incubation time, >30% of the linoleic acid was oxidized. The oxidized linoleic acid was highly detrimental to legumin, and the electrophoretic pattern of the protein was completely changed after the incubation period.

Purification and partial characterization of chickpea 2S albumin.

A chickpea 2S albumin has been purified by solubilization in 60% methanol and ion-exchange chromatography. Under denaturing conditions it is composed of two peptides of 10 and 12 kDa. Native molecular mass determined by gel filtration chromatography is 20 kDa.