Beyond the ‘bad guys’ : unpacking populism, climate skepticism, and climate policy in right-wing party manifestos

This study critically examines the relationship between right-wing populism and climate policy, challenging prevailing assumptions and exploring the complexities of this interplay. Through quantitative and qualitative content analysis of political party manifestos, the study investigates the correlation between populist rhetoric, ideological positioning, climate skepticism, and opposition to climate policies among right-wing parties. The assessment of four democracies (United States, Germany, Australia, and Austria) indicates that, contrary to popular belief, right-wing political parties do not consistently employ more populist language than their left-wing counterparts. Moreover, the findings demonstrate a complex relationship between adopting of climate skeptic discourse and opposition to climate policy. While certain right-wing political parties exhibit strong resistance to ambitious climate policies, the research uncovers a nuanced relationship that transcends a simplistic portrayal of “the climate bad guys”.M-IE

A short history of feminist critiques of language in times of the "star sign". Optional, yes! Obligatory, no!

Der vorliegende Essay nimmt den 2022 etablierten Genderstandard für erwachsenenbildung.at als Ausgangspunkt einer kritischen Auseinandersetzung mit Genderstandards im Allgemeinen und dem Genderstern im Besonderen. Zunächst beschreibt die Autorin die Entwicklungen und die divergierenden Entwürfe feministischer Theorien zur Sprachbildung und die Bemühungen um eine geschlechtergerechte Sprache seit Ende der 1970er Jahre. Im Unterschied zu fluiden Geschlechterkonzepten und einem offen gehaltenen Geschlechterbegriff kritisiert die Autorin heute einen kategorischen Identitätsdiskurs, der auf definitorische Abschottungen setzt. Der Genderstern symbolisiere eine Allgemeinheit und betrifft doch nur einige, banalisiere das Machtgefälle zwischen Männern und Frauen und ignoriere feministische Errungenschaften. Statt einen neuen Standard zu etablieren, plädiert die Autorin für demokratische Pluralität und die Anerkennung unterschiedlichen Sprechens und Schreibens ohne Bevormundung, vor allem in (Erwachsenen-)Bildungskontexten. (DIPF/Orig.)This essay takes the gender standard established in 2022 for erwachsenenbildung.at as the point of departure for a critical examination of gender standards in general and the gender asterisk in particular. First the author describes the developments and diverging drafts of feminist theories on language education and the attempts at gender-inclusive language made since the end of the 1970s. In contrast to fluid concepts of gender and an idea of gender that is intentionally open, she criticizes a categorical identity discourse based on separation by definition. The gender asterisk symbolizes a universality and only applies to some people, trivializing the imbalance in power between men and women and ignoring feminist achievements. Instead of establishing a new standard, the author argues for democratic pluralism and the acceptance of different speech and writing without being patronizing, above all in (adult) educational contexts. (DIPF/Orig.

IFEB – Revitalizing feminist women\u27s and adult education

Seit Jahrzehnten gibt es in der österreichischen Erwachsenenbildungslandschaft zahlreiche kleine, darunter vielfach selbstorganisierte und semi-institutionalisierte feministisch tradierte Frauenbildungsprojekte. Sie leisten mit wenig finanziellen Ressourcen und kaum allgemeiner Würdigung grundlegende Bildungsarbeit. Die großen Erwachsenenbildungsträger hingegen betreiben kaum mehr kritische Aufklärungsarbeit zu gesellschaftspolitischen Themen wie dem ungerechten Geschlechterverhältnis. Vielmehr werden herrschafts- und gesellschaftskritische Bildungsagenden zunehmend eliminiert, weil Effizienz, Arbeitsmarktbezug und standardisierter Kompetenzerwerb im Mittelpunkt stehen und finanziell gefördert werden. Um auf diese Missstände aufmerksam zu machen, hat sich vor ein paar Jahren die „Initiative Feministische Frauen- und Erwachsenenbildung“ (IFEB) gegründet, die hier vorgestellt wird. (DIPF/Orig.)For decades, the Austrian adult education community has included a number of small feminist women’s education projects that provide basic education with few financial resources and hardly any general recognition. Furthermore, adult education providers have marginalized their once critical educational work, which also encompasses gender issues in society. A few years ago, Initiative Feministische Frauen- und Erwachsenenbildung (IFEB, Feminist Women’s and Adult Education Initiative) was founded to raise awareness of this deplorable state of affairs. This article presents this initiative. (DIPF/Orig.

Engineering of carbohydrate oxidoreductases for sensors and bio-fuelcells

Pyranose dehydrogenase (PDH) and pyranose 2-oxidase (POx) are flavoproteins that catalyze the oxidation of free, non-phosphorylated sugars to the corresponding ketosugars. Pyranose dehydrogenase has a broad substrate specificity for monosaccharides (and few disaccharides), but is limited to a narrow range of electron acceptors and reacts extremely slowly with dioxygen, whereas pyranose 2-oxidase shows pronounced specificity for glucose and displays high oxidase as well as dehydrogenase activity. For bio-fuelcell and sensor applications, oxygen reactivity is undesirable as it leads to electron leakage and the formation of damaging hydrogen peroxide; for biocatalytic applications, oxygen reactivity is advantageous, as oxygen is freely available and obviates downstream removal of undesired electron acceptors. Site-saturation mutagenesis libraries of eleven (POx) and twelve (PDH) residues around the active sites were screened for oxidase and dehydrogenase activities. In POx, variants T166R, Q448H, L545C, L547R and N593C displayed reduced oxidase activities (between 40% and 0.2% of the wildtype) concomitant with unaffected or even increased dehydrogenase activity, dependent on the electron acceptor used (DCPIP, 1,4-benzoquinone or ferricenium ion). Kinetic characterization showed that both affinity and turnover numbers can be affected. The switch from oxidase to dehydrogenase activity was also observed electrochemically using screen-printed electrodes. In this miniaturized set-up with a reaction volume of only 50 µL the dehydrogenase activity of variant N593C was entirely preserved in the presence of a suitable mediator, shuttling electrons from the FAD cofactor to the electrode surface. The oxidase activity, utilizing molecular oxygen as acceptor, is abolished in this variant. Of all variants of PDH that were produced by saturation mutagenesis, only variants of one position displayed increased oxygen reactivity to a minor degree. Histidine 103, carrying the covalently attached FAD cofactor, was substituted by tyrosine, phenylalanine, tryptophan and methionine. Variant H103Y displayed a five-fold increase of oxygen reactivity. Stopped flow analysis revealed that the mutation slowed down the reductive half-reaction whereas the oxidative half-reaction was affected to a minor degree. No alterations in the secondary structure were observed, but disruption of the FAD bond had negative effects on thermal and conformational stability. We also engineered PDH by systematically removing several N-glycosylation sites, in order to improve performance by reducing the distance of the active site to the electrode surface, improving accessibility for redox polymers and facilitate denser enzyme packing on the electrode. One glycosylation site, N319, was found to be indispensable for functional expression and folding of the enzyme, as no active variants could be obtained. A variant with two sites, N75 and N175 near the active site entrance, exchanged against G and Q, respectively, showed significantly improved properties when used on electrodes with Osmium-based redox polymers (Mediated Electron Transfer) and a low level of Direct Electron Transfer. The lack of two glycosylation sites results in minor negative effects on expression yield and stability. Removal of a third site, N252, on the opposite side of the active site entrance, does not bring further improvements in catalysis and electron transfer, but is detrimental to functional expression and stability. The bulk of hyperglycosylation of the recombinantly expressed enzyme (observed in both Pichia pastoris and Saccharomyces cerevisiae) is located only on this one glycosylation site. Please click Additional Files below to see the full abstract

Semi-rational engineering of cellobiose dehydrogenase for improved hydrogen peroxide production

Abstract Background The ability of fungal cellobiose dehydrogenase (CDH) to generate H2O2 in-situ is highly interesting for biotechnological applications like cotton bleaching, laundry detergents or antimicrobial functionalization of medical devices. CDH’s ability to directly use polysaccharide derived mono- and oligosaccharides as substrates is a considerable advantage compared to other oxidases such as glucose oxidase which are limited to monosaccharides. However CDH’s low activity with oxygen as electron acceptor hampers its industrial use for H2O2 production. A CDH variant with increased oxygen reactivity is therefore of high importance for biotechnological application. Uniform expression levels and an easy to use screening assay is a necessity to facilitate screening for CDH variants with increased oxygen turnover. Results A uniform production and secretion of active Myriococcum thermophilum CDH was obtained by using Saccharomyces cerevisiae as expression host. It was found that the native secretory leader sequence of the cdh gene gives a 3 times higher expression than the prepro leader of the yeast α-mating factor. The homogeneity of the expression in 96-well deep-well plates was good (variation coefficient <15%). A high-throughput screening assay was developed to explore saturation mutagenesis libraries of cdh for improved H2O2 production. A 4.5-fold increase for variant N700S over the parent enzyme was found. For production, N700S was expressed in P. pastoris and purified to homogeneity. Characterization revealed that not only the kcat for oxygen turnover was increased in N700S (4.5-fold), but also substrate turnover. A 3-fold increase of the kcat for cellobiose with alternative electron acceptors indicates that mutation N700S influences the oxidative- and reductive FAD half-reaction. Conclusions Site-directed mutagenesis and directed evolution of CDH is simplified by the use of S. cerevisiae instead of the high-yield-host P. pastoris due to easier handling and higher transformation efficiencies with autonomous plasmids. Twelve clones which exhibited an increased H2O2 production in the subsequent screening were all found to carry the same amino acid exchange in the cdh gene (N700S). The sensitive location of the five targeted amino acid positions in the active site of CDH explains the high rate of variants with decreased or entirely abolished activity. The discovery of only one beneficial exchange indicates that a dehydrogenase’s oxygen turnover is a complex phenomenon and the increase therefore not an easy target for protein engineering.The authors thank the European Commission (FP7 243529-2-COTTONBLEACH) for financial support. CKP thanks the Austrian Science Fund (FWF) for financial support (grant P22094). IK is a member of the doctoral program BioToP (Biomolecular Technology of Proteins) of the Austrian Science Fund (FWF; W1224). MA thanks the Spanish Government for financial support (BIO2010-19697).Peer Reviewe

Simple and efficient expression of Agaricus meleagris pyranose dehydrogenase in Pichia pastoris

Pyranose dehydrogenase (PDH) is a fungal flavin-dependent sugar oxidoreductase that is highly interesting for applications in organic synthesis or electrochemistry. The low expression levels of the filamentous fungus Agaricus meleagris as well as the demand for engineered PDH make heterologous expression necessary. Recently, Aspergillus species were described to efficiently secrete recombinant PDH. Here, we evaluate recombinant protein production with expression hosts more suitable for genetic engineering. Expression in Escherichia coli resulted in no soluble or active PDH. Heterologous expression in the methylotrophic yeast Pichia pastoris was investigated using two different signal sequences as well as a codon-optimized sequence. A 96-well plate activity screening for transformants of all constructs was established and the best expressing clone was used for large-scale production in 50-L scale, which gave a volumetric yield of 223 mg L−1 PDH or 1,330 U L−1 d−1 in space–time yield. Purification yielded 13.4 g of pure enzyme representing 95.8% of the initial activity. The hyperglycosylated recombinant enzyme had a 20% lower specific activity than the native enzyme; however, the kinetic properties were essentially identical. This study demonstrates the successful expression of PDH in the eukaryotic host organism P. pastoris paving the way for protein engineering. Additionally, the feasibility of large-scale production of the enzyme with this expression system together with a simplified purification scheme for easy high-yield purification is shown