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Cereals --- Cereals --- Dietary fibres --- Dietary fibres --- Hydrolysis --- Hydrolysis --- Xylans --- Xylans --- Enzyme activity --- Enzyme activity --- Enzyme inhibitors --- Enzyme inhibitors --- Binding proteins --- Binding proteins
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The glycosidic aroma compounds are widely present in a variety of fruit. Their enzymic hydrolysis allows the liberation of additional flavour which can be usable. Glycosidic precursors occurring in strawberries were pointed out and characterized by extraction and identification of aglycone and sugar moieties. The qualitative and quantitative importance of these compounds compared with free volatiles was proved. Study of the evolution of glycosides during fruit development was carried out in order to clear up the role of conjugated flavours. The occurrence of glycosidase activities in strawberries and their impact on the liberation of this aroma potential were investigated. The use of the studied system was applied on strawberry based products in order to verify the usefulness of the new knowledge and to give evidence of the advantage of additional flavour liberation from glycosides in such products.
Fragaria --- Fragaria --- Flavour compounds --- Flavour compounds --- Glycosides --- Glycosides --- Enzyme activity --- Enzyme activity --- Glycosidases --- Glycosidases
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Triticum aestivum --- Triticum aestivum --- Starch --- Starch --- Xylans --- Xylans --- Enzyme inhibitors --- Enzyme inhibitors --- Isolation --- Insulation --- Purification --- Purification
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Amino acids --- Amino acids --- Enzymes --- Enzymes --- Enzyme activity --- Enzyme activity --- physiological functions --- physiological functions
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Surfactants --- Surfactants --- Hydrophobicity --- Hydrophobicity --- Adsorption --- Adsorption --- Esters --- Esters --- Biosynthesis --- Biosynthesis --- Enzyme activity --- Enzyme activity --- Structure moleculaire
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Enzyme Inhibitors --- Biochemistry --- Enzyme inhibitors --- Pharmaceutical chemistry --- Antienzymes --- Chimie pharmaceutique --- Periodicals. --- Périodiques --- Enzyme Inhibitors. --- Biochemistry. --- Enzyme inhibitors. --- Inhibitors, Enzyme --- Enzymes --- Sulfhydryl Reagents --- antagonists & inhibitors --- Periodicals --- Agriculture Sciences --- Health Sciences --- Food Science and Technology --- Physiology --- enzymology --- cell biology --- chemical biology --- microbiology --- physiology --- pharmacology --- Antagonists, Enzyme --- Enzyme antagonists --- Metabolic inhibitors --- Chemical inhibitors --- Antagonists --- Inhibitors --- Pharmaceutical chemistry. --- Chemistry, Medical and pharmaceutical --- Chemistry, Pharmaceutical --- Drug chemistry --- Drugs --- Medical chemistry --- Medicinal chemistry --- Pharmacochemistry --- Chemistry --- Pharmacology. Therapy --- farmacologie --- enzymen --- Enzyme Inhibitor --- Inhibitor, Enzyme
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Broiler chickens --- Broiler chickens --- Starch --- Starch --- Digestion --- Digestion --- Enzyme activity --- Enzyme activity --- Energy metabolism --- Energy metabolism --- Feed conversion efficiency --- Feed conversion efficiency
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Solanum tuberosum --- Solanum tuberosum --- storage --- storage --- Postharvest physiology --- Postharvest physiology --- Metabolites --- Metabolites --- Analytical methods --- Analytical methods --- Enzyme activity --- Enzyme activity --- Lipoxygenase. --- Lipoxygenase
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milk --- milk --- Fruit juices --- Fruit juices --- Escherichia coli --- Escherichia coli --- Bacteria --- Bacteria --- Pasteurization --- Pasteurization --- Pressure --- Pressure --- peptides --- peptides --- Antimicrobials --- Antimicrobials --- Enzyme activity --- Enzyme activity --- synergism --- synergism --- Lactoperoxidase
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The yeast P. anomala strain K protects post-harvest apples against Botrytis cinerea. Two genes encoding exo-beta-1, 3-glucanases, PaEXG1 and PaEXG2 have been isolated from strain K genome thanks to conserved regions in fungal exo-beta-1, 3-glucanases and to the sequencing of PaEXG2, an exo-beta-1, 3-glucanase from strain K culture fluids. PaEXG1 potentially encodes a 498 amino acids long protein, with a calculated molecular weight of 58 kDa, an estimated pI of 4.79 and 8 potential sites for N-linked glycosylation. PaEXG2 has a coding capacity for an acidic protein of 427 amino acids with a predicted molecular weight of 49 kDa, a calculated pI of 4.70 and one potential N-glycosylation site. Haploid uracil auxotrophic mutants derived from strain K showed an inferior biocontrol effect and colonization of apple wounded sites compared to the prototrophic strain. Antagonism and colonization were recovered after restoration of the prototrophy by transformation with the URA3 gene encoding orotidine monophosphate decarboxylase. PaEXG1 and PaEXG2 genes were separately disrupted by the insertion of the URA3 marker gene in their ORFs. Integrative transformation was shown to be mostly ectopic in strain K descendants (only 4 % of integration by homologous recombination). Disruption of PaEXG1 or PaEXG2 had no visible effect on in vitro growth with B. cinerea cell walls preparation as the sole carbon source or in apple wounds. PaEXG1 disruption had no effect on the in vitro or in situ extracellular exo-beta-1, 3-glucanases activity production while PaEXG2 disruption abolished all detectable activity in vitro and in vivo. Disruption of PaEXG1 or PaEXG2 did not affect the biocontrol towards B. cinerea on wounded apples, showing that the products of those genes are dispensable for protective activity (in singly disrupted mutants).
Apples --- Apples --- Botrytis cinerea --- Botrytis cinerea --- Enzyme activity --- Enzyme activity --- Biological control --- Biological control --- genetic code --- genetic code --- Pichia --- Pichia --- Molecular genetics --- Molecular genetics --- Disease resistance --- Disease resistance
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