Food waste has been widely valorized in the past years in order to develop eco-friendly materials. Among others, bread waste is currently of increasing interest, as it is considered a huge global issue with serious environmental impacts and significant economic losses that have become even greater in the post-pandemic years due to an increase in cereal prices, which has led to higher production costs and bread prices. Owing to its richness in polysaccharides, bread waste has been previously studied for its physico-chemical characteristics and its numerous biotechnological applications.
View Article and Find Full Text PDFLeather industry is making significant contributions to economic development. However, it is notably leading to a serious environmental pollution. Recently, the enzyme technology developments offer new opportunities for enzymatic application in leather making.
View Article and Find Full Text PDFIn this study, chemical composition and in vitro biological activities of artichoke by-products (leaves, floral stems and bracts) issued from two Tunisian varieties were evaluated. Analysis was performed by means of high-performance liquid chromatography with diode array detection coupled to electrospray ionization mass spectrometric (LC/DAD/ESI-MS). Total phenolic (TPC) and flavonoid (TFC) contents as well as the antioxidant activity conducted by three complementary methods, DPPH, ABTS and FRAP tests, were performed for each sample.
View Article and Find Full Text PDFThe discovery of in-vitro systematic evolution of ligands by exponential enrichment (SELEX) process has considerably broaden the utility of aptamer as bio-recognition element, providing the high binding affinity and specificity against the target analytes. Recent research has focused on the development of structure switching signaling aptamer assay, transducing the aptamer- target recognition event into an easily detectable signal. In this paper, we demonstrate the development of structure switching aptamer assay for determination of aflatoxin M1 (AFM1) employing the quenching-dequenching mechanism.
View Article and Find Full Text PDFPlants are constantly confronted to both abiotic and biotic stresses that seriously reduce their productivity. Plant responses to these stresses are complex and involve numerous physiological, molecular, and cellular adaptations. Recent evidence shows that a combination of abiotic and biotic stress can have a positive effect on plant performance by reducing the susceptibility to biotic stress.
View Article and Find Full Text PDFAppl Biochem Biotechnol
November 2010
A new, simple, and original method is described for specific measurement of polyunsaturated fatty acid content in olive oil. This analytical system uses coupled enzymes, lipase and lipoxygenase. The system consists of lipase-catalyzed hydrolysis of triacylglycerol and subsequent lipoxygenation of liberated polyunsaturated fatty acids.
View Article and Find Full Text PDFA novel biosensor assay format for aflatoxin based on acetylcholinesterase (AChE) inhibition by aflatoxin B(1) (AFB(1)) is proposed. The AChE was present in solution and an amperometric choline oxidase biosensor was used for monitoring its residual activity. To create the biosensor, the choline oxidase was immobilized by cross-linking onto screen-printed electrodes modified with Prussian Blue (PB) and these were used to detect the H(2)O(2) at low potential (-0.
View Article and Find Full Text PDFLipase activity against triacylglycerols has been measured using an amperometric enzyme biosensor based on glycerol dehydrogenase/NADH oxidase. A Prussian Blue modified screen-printed electrode was selected as substrate for the two immobilised-enzyme systems due to their higher operative stability reported in previous works. Various parameters such as cofactor (flavin mononucleotide FMN) concentration (1 mM), NAD+ coenzyme concentration (2 mM), pH effect (phosphate buffer pH 6 to 8, Tris buffer pH 8-10) response time and storage stability were evaluated and optimised.
View Article and Find Full Text PDFA new method for lipase activity determination is described, in which liberation of fatty acids by lipase-catalyzed hydrolysis is coupled to lipoxygenation. The second reaction forms hydroperoxy-fatty acids containing a conjugated double bond that are detected at 234 nm. The method is sensitive, cheap and easy to use when compared to a titration method.
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