This review summarizes the reactions, catalysts and influence factors in the hydrothermal deoxygenation of lipids and fatty acids to diesel-like hydrocarbons.
The blue-green mold Penicillium italicum is among the most problematic post-harvest plant infections limiting the integrity of citrus and many other crops during storage and transportation, but there is no sensor for its on-site or field detection. We hereby, for the first time, report the development of novel biomolecular sensor for assessing the presence of P. italicum spores and hyphae using carbohydrate-lectin recognitions. Two approaches were developed: (i) lateral tests using standalone poly(amic) acid (PAA) membranes and glass surfaces and (ii) quantitative tests on 96-well polystyrene plates and paper electrodes. In both cases, the surfaces were functionalized with novel derivatized sugar based ligands while staining was performed with gold nanoparticles. Both approaches provided strong signals for 10 spores/mL of P. italicum isolated from experimentally infected lemons as the lowest-reliable concentration. The 96-well plate-based gave the most sensitive detection with a 4 × 10 spores/mL limit of detection, a linear dynamic range between 2.9 × 10 and 6.02 × 10 spores/mL ( R = 0.9939) and standard deviation of less than 5% for five replicate measurements. The selectivity of the ligands was tested against Trichaptum biforme, Glomerulla cingulata ( Colletotrichum gloeosporioides), and Aspergillus nidulans fungi species. The highest selectivity was obtained using the sugar-based gold-nanoparticles toward both the spores and the hyphae of P. italicum. The advanced specificity was provided by the utilized sugar ligands employed in the synthesis of gold nanoparticles and was independent from size and shapes of the AuNPs. Accuracy of the sensor response showed dramatic dependence on the sample preparation. In the case of 5-10 min centrifugation at 600 rpm, the spores can be isolated free from hyphae and conidiophore, for which spiked recovery was up to 95% (std ±4). In contrast, for gravity-based precipitation of hyphae, the spiked recovery was 88% (std 11).
Maltose syrups have got wide-range utilizations in a variety of applications from bakery to drug-development. α-Amylases are among the most widely utilized industrial enzymes due to their high specificity in production of maltose syrup from starch. However, enzymes are not stable in ex vivo conditions towards alteration in pH, temperature, and such other parameters as high salt concentrations and impurities, where immobilization is required to advance the stability of the enzyme with which approach the requirement of isolation of the enzyme from media is eliminated as well. In this study, Termamyl α-amylase was immobilized on the none-modified chitosan beads (NMCB), L-lysine-modified chitosan beads (LMCB), and L-asparagine-modified chitosan beads (AMCB) to assess effects of the support material on optimum conditions and kinetic parameters of the α-amylase activity in production of maltose from starch. Immobilization on NMCB, LMCB, and AMCB puts a strong influence on optimum pH, optimum temperature, stability, and kinetic parameters of α-amylase. Modification of chitosan beads with L-lysine and L-asparagine dramatically altered the overall immobilization yield, and enzyme's response to pH and temperature variations and the kinetic parameters. AMCB provided the best immobilization yield (49%), while LMCB only improved the yield by 2% from 22 to 24%.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2025 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.