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El Amerany, F.; Rhazi, M.; Balcke, G.; Wahbi, S.; Meddich, A.; Taourirte, M.; Hause, B.;The effect of chitosan on plant physiology, wound response, and fruit quality of tomatoPolymers145006(2022)DOI: 10.3390/polym14225006
In agriculture, chitosan has become popular as a metabolic enhancer; however, no deep information has been obtained yet regarding its mechanisms on vegetative tissues. This work was conducted to test the impact of chitosan applied at different plant growth stages on plant development, physiology, and response to wounding as well as fruit shape and composition. Five concentrations of chitosan were tested on tomato. The most effective chitosan doses that increased leaf number, leaf area, plant biomass, and stomatal conductance were 0.75 and 1 mg mL−1. Chitosan (1 mg mL−1) applied as foliar spray increased the levels of jasmonoyl–isoleucine and abscisic acid in wounded roots. The application of this dose at vegetative and flowering stages increased chlorophyll fluorescence (Fv/Fm) values, whereas application at the fruit maturation stage reduced the Fv/Fm values. This decline was positively correlated with fruit shape and negatively correlated with the pH and the content of soluble sugars, lycopene, total flavonoids, and nitrogen in fruits. Moreover, the levels of primary metabolites derived from glycolysis, such as inositol phosphate, lactic acid, and ascorbic acid, increased in response to treatment of plants with 1 mg mL−1- chitosan. Thus, chitosan application affects various plant processes by influencing stomata aperture, cell division and expansion, fruit maturation, mineral assimilation, and defense responses.
Publikation
Tang, N.; Naumann, C.;Native protein purification of ferroxidase LPR1 from leaf extracts of a transgenic Arabidopsis thaliana lineSTAR Protocols3101733(2022)DOI: 10.1016/j.xpro.2022.101733
(LOW PHOSPHATE ROOT 1), a bacterial-type plant ferroxidase, is crucial for local root phosphate (Pi) sensing. Here, we present a detailed protocol for native (tag-free) protein purification of LPR1 from leaf extracts by differential ammonium sulfate precipitation, size exclusion, and cation exchange chromatography of a transgenic Arabidopsis thaliana line overexpressing LPR1. We outline steps for LPR1 purification tracking via immune blot analysis and ferroxidase activity assay. The protocol yields highly pure and active LPR1 protein for biochemical analysis. For complete details on the use and execution of this protocol, please refer to Naumann et al. (2022)