<b>NWB2023_The SDGs and publications of University of Helsinki: tracking contributions responsibly</b>

The United Nations 2030 Agenda for Sustainable Development launched in 2015 introduced 17 Sustainable Development Goals (SDGs). Ever since then, Universities have been interested in evaluating how their research relates to these goals. In University of Helsinki, for example, we are developing ways of monitoring and analysing the share of publications related to sustainable development. Several analytical tools for tracking SDG contributions have cropped up in recent years. Major citation databases such as Scopus, Web of Science and Dimensions now come with SDG-information. However, SDGs are very general in scope and consequently their interpretation at the level of publications can often be ambiguous. Major databases tend to use different methods for relating publications under various SDGs. For example, SciVal uses AI enhanced keyword searches whereas InCites uses citation-based clusters (Citation Topics). We wanted to find out how these differences in methodology are reflected in the resulting SDG distributions for our university. We gathered all peer-reviewed University of Helsinki publications between the years 2020-2022 with a DOI-identifier (22563 publications in total) and analysed their SDG distributions in InCites and SciVal. We compared the distributions and looked at their overlaps.The results were that there were significant differences in SDG attributions with up to quadruple amounts of publications for certain SDGs depending on the database used. More problematic, however, was that the overlaps in publications tended to be very small (4.7% to 37.5% for InCites in SciVal and 5.5% to 80.3% for SciVal in InCites). Some implications were considered.</p

Deciphering Design Principles of Förster Resonance Energy Transfer-Based Protease Substrates: Thermolysin-Like Protease from Geobacillus stearothermophilus as a Test Case

Protease activity is frequently assayed using short peptides that are equipped with a Förster resonance energy transfer (FRET) reporter system. Many frequently used donor–acceptor pairs are excited in the ultraviolet range and suffer from low extinction coefficients and quantum yields, limiting their usefulness in applications where a high sensitivity is required. A large number of alternative chromophores are available that are excited in the visible range, for example, based on xanthene or cyanine core structures. These alternatives are not only larger in size but also more hydrophobic. Here, we show that the hydrophobicity of these chromophores not only affects the solubility of the resulting FRET-labeled peptides but also their kinetic parameters in a model enzymatic reaction. In detail, we have compared two series of 4–8 amino acid long peptides, designed to serve as substrates for the thermolysin-like protease (TLP-ste) from Geobacillus stearothermophilus. These peptides were equipped with a carboxyfluorescein donor and either Cy5 or its sulfonated derivative Alexa Fluor 647 as the acceptor. We show that the turnover rate <i>k</i>_cat is largely unaffected by the choice of the acceptor fluorophore, whereas the <i>K</i>_M value is significantly lower for the Cy5- than for the Alexa Fluor 647-labeled substrates. TLP-ste is a rather nonspecific protease with a large number of hydrophobic amino acids surrounding the catalytic site, so that the fluorophore itself may form additional interactions with the enzyme. This hypothesis is supported by the result that the difference between Cy5- and Alexa Fluor 647-labeled substrates becomes less pronounced with increasing peptide length, that is, when the fluorophore is positioned at a larger distance from the catalytic site. These results suggest that fluorophores may become an integral part of FRET-labeled peptide substrates and that <i>K</i>_M and <i>k</i>_cat values are generally only valid for a specific combination of the peptide sequence and FRET pair

Interfacial Activation of <i>Candida antarctica</i> Lipase B: Combined Evidence from Experiment and Simulation

Lipase immobilization is frequently used for altering the catalytic properties of these industrially used enzymes. Many lipases bind strongly to hydrophobic surfaces where they undergo interfacial activation. <i>Candida antarctica</i> lipase B (CalB), one of the most commonly used biocatalysts, is frequently discussed as an atypical lipase lacking interfacial activation. Here we show that CalB displays an enhanced catalytic rate for large, bulky substrates when adsorbed to a hydrophobic interface composed of densely packed alkyl chains. We attribute this increased activity of more than 7-fold to a conformational change that yields a more open active site. This hypothesis is supported by molecular dynamics simulations that show a high mobility for a small “lid” (helix α5) close to the active site. Molecular docking calculations confirm that a highly open conformation of this helix is required for binding large, bulky substrates and that this conformation is favored in a hydrophobic environment. Taken together, our combined approach provides clear evidence for the interfacial activation of CalB on highly hydrophobic surfaces. In contrast to other lipases, however, the conformational change only affects large, bulky substrates, leading to the conclusion that CalB acts like an esterase for small substrates and as a lipase for substrates with large alcohol substituents