An olive beta-glucosidase was purified to apparent homogeneity from mature fruits ( Olea europaea cv. Picual) by selective extraction and successive anion exchange and hydrophobic interaction chromatographic procedures. The enzyme was shown to be a homodimer made up of two identical subunits of 65.4 kDa. Optimum activity was recorded at pH 5.5 and 45 degrees C. The enzyme was active on the main olive phenolic glycosides, with maximum activity toward oleuropein (100%), followed by ligstroside (65%) and demethyloleuropein (21%). The enzyme showed very low activity with apigenin and luteolin glucosides and was not active on verbascoside and rutin. Kinetic values show that olive beta-glucosidase is 200-fold more active against oleuropein than against the synthetic substrate p-nitrophenyl-beta-d-glucopyranoside (pNPG). According to its catalytic properties, the implication of the purified olive beta-glucosidase on the synthesis of virgin olive oil phenolics is discussed.
Islands harbour evolutionary and ecologically unique biota, which are currently disproportionately threatened by a multitude of anthropogenic factors, including habitat loss, 2568 Biodivers Conserv (2018) 27:2567-2586 1 3 invasive species and climate change. Native forests on oceanic islands are important refugia for endemic species, many of which are rare and highly threatened. Long-term monitoring schemes for those biota and ecosystems are urgently needed: (i) to provide quantitative baselines for detecting changes within island ecosystems, (ii) to evaluate the effectiveness of conservation and management actions, and (iii) to identify general ecological patterns and processes using multiple island systems as repeated 'natural experiments'. In this contribution, we call for a Global Island Monitoring Scheme (GIMS) for monitoring the remaining native island forests, using bryophytes, vascular plants, selected groups of arthropods and vertebrates as model taxa. As a basis for the GIMS, we also present new, optimized monitoring protocols for bryophytes and arthropods that were developed based on former standardized inventory protocols. Effective inventorying and monitoring of native island forests will require: (i) permanent plots covering diverse ecological gradients (e.g. elevation, age of terrain, anthropogenic disturbance); (ii) a multiple-taxa approach that is based on standardized and replicable protocols; (iii) a common set of indicator taxa and community properties that are indicative of native island forests' welfare, building on, and harmonized with existing sampling and monitoring efforts; (iv) capacity building and training of local researchers, collaboration and continuous dialogue with local stakeholders; and (v) long-term commitment by funding agencies to maintain a global network of native island forest monitoring plots.
The effect of high-oxygen atmospheres on strawberry flavor was studied. Strawberry fruits (Fragariax ananassa Duch. cv. Camarosa) were stored at 8 degrees C in four different atmospheres: air, 5% O(2)/20% CO(2), 80% O(2)/20% CO(2), and 90% O(2)/10% CO(2). Changes in several quality parameters were evaluated. Atmospheres combining high O(2) and high CO(2) were the most effective in preventing fungal growth and enhancing strawberry firmness. Other quality parameters such as color, titrable acidity, sugars and organic acids distribution, off-flavor development, and aroma were only mildly affected by superatmospheric O(2) levels. After one week of storage, unexpected high contents of off-flavor related compounds were found in the 80% O(2)/20% CO(2) and 90% O(2)/10% CO(2) atmospheres. Evidence of an altered ester biosynthesis was also found in fruits stored under these high-O(2) atmospheres. Data obtained suggest that stress induced by high CO(2) and stress induced by high O(2) have an additive effect on strawberry flavor alteration.
Hydroperoxide lyase (HPOOH lyase) was extracted from tomato leaves (Lycopersicon esculentum Mill.) and purified to apparent homogeneity by fractionated precipitation with polyethylene glycol 6000, ion exchange chromatography, and ultrafiltration. The enzyme is a trimer of 73 000 Da units with a molecular mass of 216 000 (determined by native-PAGE and gel filtration); its pI is around 4.9. Enzyme activity measurments realized with 9-and 13-hydroperoxides of linoleic acid (9-La OOH and 13-La OOH, respectively), R-linolenic acid (9-Ln OOH and 13-Ln OOH, respectively), and γ-linolenic acid (9-γLn OOH and 13-γ-Ln OOH, respectively) revealed a great affinity for 13-Ln OOH. The enzyme is rapidly inhibited by its substrate (13-Ln OOH), but preincubation with the other five hydroperoxides, which are not degraded by the enzyme, also resulted in activity inhibition. Dialysis could not restore the activity. When 13-Ln OOH is reduced in its corresponding alcohol or converted to its methyl ester, the inhibition is reduced.
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