Institut für Chemie und Bioanalytik
Dauerhafte URI für die Sammlunghttps://irf.fhnw.ch/handle/11654/24
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Ergebnisse nach Hochschule und Institut
Publikation Enzymes for consumer products to achieve climate neutrality(Oxford University Press, 2023) Molina-Espeja, Patricia; Sanz-Aparicio, Julia; Golyshin, Peter N.; Robles-Martín, Ana; Guallar, Víctor; Beltrametti, Fabrizio; Müller, Markus; Yakimov, Michail M.; Modregger, Jan; van Logchem, Moniec; Corvini, Philippe; Shahgaldian, Patrick; Degering, Christian; Wieland, Susanne; Timm, Anne; de Carvalho, Carla C. C. R.; Re, Ilaria; Daniotti, Sara; Thies, Stephan; Jaeger, Karl-Erich; Chow, Jennifer; Streit, Wolfgang R.; Lottenbach, Roland; Rösch, Rainer; Ansari, Nazanin; Ferrer, ManuelToday, the chemosphere’s and biosphere’s compositions of the planet are changing faster than experienced during the past thousand years. CO2 emissions from fossil fuel combustion are rising dramatically, including those from processing, manufacturing and consuming everyday products; this rate of greenhouse gas emission (36.2 gigatons accumulated in 2022) is raising global temperatures and destabilizing the climate, which is one of the most influential forces on our planet. As our world warms up, our climate will enter a period of constant turbulence, affecting more than 85% of our ecosystems, including the delicate web of life on these systems, and impacting socioeconomic networks. How do we deal with the green transition to minimize climate change and its impacts while we are facing these new realities? One of the solutions is to use renewable natural resources. Indeed, nature itself, through the working parts of its living systems, the enzymes, can significantly contribute to achieve climate neutrality and good ecological/biodiversity status. Annually they can help decreasing CO2 emissions by 1–2.5 billion-tons, carbon demand by about 200 million-tons, and chemical demand by about 90 million-tons. With current climate change goals, we review the consequences of climate change at multiple scales and how enzymes can counteract or mitigate them. We then focus on how they mobilize sustainable and greener innovations in consumer products that have a high contribution to global carbon emissions. Finally, key innovations and challenges to be solved at the enzyme and product levels are discussed.01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor(Royal Society of Chemistry, 2023) Fernandez-Lopez, Laura; Cea-Rama, Isabel; Alvarez-Malmagro, Julia; Ressmann, Anna K.; Gonzalez-Alfonso, Jose L.; Coscolín, Cristina; Shahgaldian, Patrick; Plou, Francisco J.; Modregger, Jan; Pita, Marcos; Sanz-Aparicio, Julia; Ferrer, ManuelMetal complexes introduced into esterase enzyme scaffolds can generate versatile biomimetic catalysts endowed with oxidoreductase activity.01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Nanobiocatalysts with inbuilt cofactor recycling for oxidoreductase catalysis in organic solvents(Royal Society of Chemistry, 2023) Sahlin, Jenny; Wu, Congyu; Buscemi, Andrea; Schärer, Claude; Nazemi, Seyed Amirabbas; S. K., Rejaul; Herrera-Reinoza, Nataly; Jung, Thomas A.; Shahgaldian, PatrickThe major stumbling block in the implementation of oxidoreductase enzymes in continuous processes is their stark dependence on costly cofactors that are insoluble in organic solvents. We describe a chemical strategy that allows producing nanobiocatalysts, based on an oxidoreductase enzyme, that performs biocatalytic reactions in hydrophobic organic solvents without external cofactors. The chemical design relies on the use of a silica-based carrier nanoparticle, of which the porosity can be exploited to create an aqueous reservoir containing the cofactor. The nanoparticle core, possessing radial-centred pore channels, serves as a cofactor reservoir. It is further covered with a layer of reduced porosity. This layer serves as a support for the immobilisation of the selected enzyme yet allowing the diffusion of the cofactor from the nanoparticle core. The immobilised enzyme is, in turn, shielded by an organosilica layer of controlled thickness fully covering the enzyme. Such produced nanobiocatalysts are shown to catalyse the reduction of a series of relevant ketones into the corresponding secondary alcohols, also in a continuous flow fashion. © 2023 RSC.01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Development and validation of a liquid chromatography-triple quadrupole mass spectrometry method for the determination of isopeptide ε-(γ-glutamyl) lysine in human urine as biomarker for transglutaminase 2 cross-linked proteins(Elsevier, 21.06.2023) Dejager, Lien; Jairaj, Mark; Jones, Kieran; Johnson, Timothy; Dudal, Sherri; Dudal, Yves; Shahgaldian, Patrick; Correro, Rita; Qu, Jun; An, Bo; Lucey, Richard; Szarka, Szabolcs; Wheller, Robert; Pruna, Alina; Kettell, Sarah; Pitt, Andrew; Cutler, Paul01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Design of a biocatalytic flow reactor based on hierarchically structured monolithic silica for producing galactooligosaccharides (GOSs)(Schweizerische Chemische Gesellschaft, 2023) Dejoma, Riccardo; Buscemi, Andrea; Cutrona, Emilio; Shahgaldian, PatrickClimate change mitigation requires the development of greener chemical processes. In this context, biocatalysis is a pivotal key enabling technology. The advantages of biocatalysis include lower energy consumption levels, reduced hazardous waste production and safer processes. The possibility to carry out biocatalytic reactions under flow conditions provides the additional advantage to retain the biocatalyst and to reduce costly downstream processes. Herein, we report a method to produce galactooligosaccharides (GOSs) from a largely available feedstock (i.e. lactose from dairy production) using a flow reactor based on hierarchically structured monolithic silica. This reactor allows for fast and efficient biotransformation reaction in flow conditions.01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Plasmonic photothermal activation of an organosilica shielded cold-adapted lipase co-immobilised with gold nanoparticles on silica particles(Royal Society of Chemistry, 01.01.2023) Giunta, Carolina; Nazemi, Seyed Amirabbas; Olesińska, Magdalena; Shahgaldian, PatrickGold nanoparticles (AuNPs), owing to their intrinsic plasmonic properties, are widely used in applications ranging from nanotechnology and nanomedicine to catalysis and bioimaging. Capitalising on the ability of AuNPs to generate nanoscale heat upon optical excitation, we designed a nanobiocatalyst with enhanced cryophilic properties. It consists of gold nanoparticles and enzyme molecules, co-immobilised onto a silica scaffold, and shielded within a nanometre-thin organosilica layer. To produce such a hybrid system, we developed and optimized a synthetic method allowing efficient AuNP covalent immobilisation on the surface of silica particles (SPs). Our procedure allows to reach a dense and homogeneous AuNP surface coverage. After enzyme co-immobilisation, a nanometre-thin organosilica layer was grown on the surface of the SPs. This layer was designed to fulfil the dual function of protecting the enzyme from the surrounding environment and allowing the confinement, at the nanometre scale, of the heat diffusing from the AuNPs after surface plasmon resonance photothermal activation. To establish this proof of concept, we used an industrially relevant lipase enzyme, namely Lipase B from Candida Antarctica (CalB). Herein, we demonstrate the possibility to photothermally activate the so-engineered enzymes at temperatures as low as −10 °C.01A - Beitrag in wissenschaftlicher Zeitschrift