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Plant hydrophobicity

Saponins are a diverse group of surface-active heteroglycosides occurring mainly in plants. Hydrophobic aglycones of saponins, which are called sapogenols (formerly sapogenins) are compounds... [Pg.781]

Mammals, fungi, and higher plants produce a family of proteolytic enzymes known as aspartic proteases. These enzymes are active at acidic (or sometimes neutral) pH, and each possesses two aspartic acid residues at the active site. Aspartic proteases carry out a variety of functions (Table 16.3), including digestion pepsin and ehymosin), lysosomal protein degradation eathepsin D and E), and regulation of blood pressure renin is an aspartic protease involved in the production of an otensin, a hormone that stimulates smooth muscle contraction and reduces excretion of salts and fluid). The aspartic proteases display a variety of substrate specificities, but normally they are most active in the cleavage of peptide bonds between two hydrophobic amino acid residues. The preferred substrates of pepsin, for example, contain aromatic residues on both sides of the peptide bond to be cleaved. [Pg.519]

After uptake, lipophilic pollutants tend to move into hydrophobic domains within animals or plants (membranes, lipoproteins, depot fat, etc.), unless they are biotransformed into more polar and water soluble with compounds having low Metabolism of lipophilic compounds proceeds in two stages ... [Pg.24]

Pollution Control Pervaporation is used to reduce the organic loading of a waste stream, thus effecting product recovery and a reduction in waste-treatment costs. An illustration is a waste stream containing II percent (wt) n-propanol. The residue is stripped to 0.5 percent and 96 percent of the alcohol is recovered in the permeate as a 45 percent solution. This application uses a hydrophobic, rubbery membrane. The residue is sent to a conventional waste-treatment plant. [Pg.65]

Upon formation of a metal chelate or complex, the next rate-limiting step in delivering iron to the cell is the diffusion of iron complexes through the. soil in response to diffusion gradients. In the vicinity of plant roots, metal chelates and complexes may also move by bulk flow in the transpiration stream as water moves from the soil into the plant. However, depending on their charge characteristics and hydrophobicity, metal chelators and complexes can become adsorbed to clay and organic matter, which may then decrease their mobility and bioavail-... [Pg.229]

Oily crops such as soybeans and canola (oilseed rape) cannot be extracted with aqueous buffers, because the extraction solvent cannot permeate the hydrophobic plant tissue matrix. In these cases, homogenization in acetonitrile-hexane is recommended. This solvent mixture is able to extract sulfonylureas from these samples with a minimum of co-extracted oil. After extraction, the sulfonylureas partition into the acetonitrile phase while most of the oil stays in the hexane phase. Further cleanup is accomplished using a silica SPE cartridge and normal-phase conditions. [Pg.406]

Buprofezin and its metabolites, p-OH-buprofezin and BF12, are hydrophobic under neutral conditions. Having the organic base part in their chemical structure, these compounds form water-soluble salts under strongly acidic conditions. The change in solubilities of these compounds influences the cleanup procedure. Four different residue analytical methods have been developed to measure buprofezin and its metabolites in plants (rice, citrus and tomato cucumber, pepper, tomato, squash and eggplant), soil and water ... [Pg.1271]

Factors that affect the accessibility of chemicals to plant roots include hydrophobicity, polarity, sorption properties and solubility. In order to apply phytoremediation techniques to soils polluted by organic contaminants, the contaminant must come into contact with the plant roots and be dissolved... [Pg.548]


See other pages where Plant hydrophobicity is mentioned: [Pg.2789]    [Pg.441]    [Pg.308]    [Pg.255]    [Pg.401]    [Pg.350]    [Pg.2055]    [Pg.239]    [Pg.241]    [Pg.452]    [Pg.228]    [Pg.170]    [Pg.399]    [Pg.23]    [Pg.97]    [Pg.110]    [Pg.116]    [Pg.27]    [Pg.34]    [Pg.76]    [Pg.133]    [Pg.44]    [Pg.46]    [Pg.405]    [Pg.405]    [Pg.755]    [Pg.191]    [Pg.3]    [Pg.220]    [Pg.549]    [Pg.550]    [Pg.552]    [Pg.552]    [Pg.556]    [Pg.341]    [Pg.61]    [Pg.116]    [Pg.117]    [Pg.368]    [Pg.64]    [Pg.70]    [Pg.184]    [Pg.185]   
See also in sourсe #XX -- [ Pg.30 ]




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