Foliar Application of CaCO-Rich Industrial Residues on 'Shiraz' Vines Improves the Composition of Phenolic Compounds in Grapes and Aged Wine.

The quality of wine grapes and wine depends on their content of phenolic compounds. Under commercial conditions, the phenolic maturity of grapes is mostly achieved by applying abscisic acid analogues. Some Ca forms represent a cost-effective alternative for these compounds.

Oligosaccharins as Elicitors of Defense Responses in Wheat.

Wheat is a highly relevant crop worldwide, and like other massive crops, it is susceptible to foliar diseases, which can cause devastating losses. The current strategies to counteract wheat diseases include global monitoring of pathogens, developing resistant genetic varieties, and agrochemical applications upon diseases' appearance. However, the suitability of these strategies is far from permanent, so other alternatives based on the stimulation of the plants' systemic responses are being explored.

Comparison of nutritional properties and bioactive compounds between industrial and artisan fresh tortillas from maize landraces.

Consumers are seeking for native-traditional foods to improve their intake of both nutrients and health-promoting phytochemicals. This study was designed to evaluate the difference in content of nutrients and bioactive compounds from handmade tortillas elaborated by a small-scale artisan producer and tortillas sold by a large food retailer available to consumers. All tortillas were analyzed for chemical composition, dietary fiber, calcium and phytochemical content, antioxidant capacity, and phenolic acids profile.

Postharvest application of pectic-oligosaccharides on quality attributes, activities of defense-related enzymes, and anthocyanin accumulation in strawberry.

Background: The postharvest application of pectic-oligosaccharides (POS) as an elicitor to improve the postharvest shelf-life and nutritional quality by stimulating natural defense mechanisms in strawberries was studied. Strawberries (cv. Festival) were treated with POS (at 0, 2, 5, and 9 g L ) and evaluated for firmness, weight loss, color, soluble solids, titratable acidity (TA), total phenolic and anthocyanin content, antioxidant capacity, decay, and some defense-related enzyme activity during storage at 2 ± 0.

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions.

Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main cause of their popularity. This review focuses on these lipase immobilization supports.

Comparative study of the banana pulp browning process of 'Giant Dwarf' and FHIA-23 during fruit ripening based on image analysis and the polyphenol oxidase and peroxidase biochemical properties.

This work presents a novel method to associate the polyphenol oxidase (PPO) and the peroxidase (POD) activities with the ripening-mediated color changes in banana peel and pulp by computational image analysis. The method was used to follow up the de-greening of peel and browning of homogenized pulp from 'Giant Dwarf' (GD: Musa AAA, subgroup Cavendish) and FHIA-23 (tetraploid hybrid, AAAA) banana cultivars. In both cultivars, the color changes of peel during the ripening process clearly showed four stages, which were used to group the fruit into ripening stages.

Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts.

This review discusses the possible roles of polyethylenimine (PEI) in the design of improved immobilized biocatalysts from diverse perspectives. This includes their use to activate supports and immobilize enzymes via ion exchange, as well as to improve immobilized enzymes by coating with PEI. PEI is a polymer containing primary, secondary and tertiary amino groups, having a strong anion exchange capacity under a broad range of conditions, and the capability to chemically react with different moieties on either an enzyme or a support.

Effect of protein load on stability of immobilized enzymes.

Different lipases have been immobilized on octyl agarose beads at 1mg/g and at maximum loading, via physical interfacial activation versus the octyl layer on the support. The stability of the preparations was analyzed. Most biocatalysts had the expected result: the apparent stability increased using the highly loaded preparations, due to the diffusional limitations that reduced the initial observed activity.

Desorption of Lipases Immobilized on Octyl-Agarose Beads and Coated with Ionic Polymers after Thermal Inactivation. Stronger Adsorption of Polymers/Unfolded Protein Composites.

Lipases from (isoform B) and (CALB and RML) have been immobilized on octyl-agarose (OC) and further coated with polyethylenimine (PEI) and dextran sulfate (DS). The enzymes just immobilized on OC supports could be easily released from the support using 2% SDS at pH 7, both intact or after thermal inactivation (in fact, after inactivation most enzyme molecules were already desorbed). The coating with PEI and DS greatly reduced the enzyme release during thermal inactivation and improved enzyme stability.

Relevance of substrates and products on the desorption of lipases physically adsorbed on hydrophobic supports.

Lipase B from Candida antarctica (CALB) has been physically immobilized on octyl-agarose via interfacial activation. The incubation of the enzyme in 80% ethanol at pH 5 and 25°C has not significant effect on enzyme activity. Moreover, the hydrolysis of 100mM tributyrin catalyzed by this biocatalyst exhibited a quite linear reaction course.

Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI).

Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. The enzyme activity was fully maintained during the coating and the thermal stability was marginally improved. The enzyme release from the support by incubation in the non-ionic detergent Triton X-100 was more difficult after the PEI-coating, suggesting that some intermolecular physical crosslinking had occurred, making this desorption more difficult.

Identification and Functional Characterization of a Fructooligosaccharides-Forming Enzyme from Aspergillus aculeatus.

Although fructosyltransferases from Aspergillus aculeatus have received a considerable interest for the prebiotics industry, their amino acid sequences and structural features remain unknown. This study sequenced and characterized a fructosyltransferase from A. aculeatus (AcFT) isolated by heat treatment of Pectinex Ultra SP-L.