Hochschule für Life Sciences FHNW

Dauerhafte URI für den Bereichhttps://irf.fhnw.ch/handle/11654/22

Listen

Bereich: Suchergebnisse

Gerade angezeigt 1 - 7 von 7
  • Vorschaubild
    Publikation
    Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor
    (Royal Society of Chemistry, 20.06.2023) 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, Manuel
    Metal complexes introduced into esterase enzyme scaffolds can generate versatile biomimetic catalysts endowed with oxidoreductase activity.
    01A - Beitrag in wissenschaftlicher Zeitschrift
  • Vorschaubild
    Publikation
    Enzymes for consumer products to achieve climate neutrality
    (Oxford University Press, 15.03.2023) 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, Manuel
    Abstract Today, 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 Zeitschrift
  • Vorschaubild
    Publikation
    Enzymes for consumer products to achieve climate neutrality
    (Oxford University Press, 15.03.2023) 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, Manuel
    Today, 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 Zeitschrift
  • Publikation
    Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles
    (Royal Society of Chemistry, 2021) Nazemi, Seyed; Olesinska, Magdalena; Pezzella, Cinzia; Varriale, Simona; Lin, Chia-Wei; Corvini, Philippe; Shahgaldian, Patrick
    We report a method of glycosylated enzymes’ surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica layer of controlled thickness is grown at the silica surface, entrapping the enzyme and thus avoiding enzyme leaching. We demonstrate that this approach results not only in high and durable activity retention but also enzyme stabilisation.
    01A - Beitrag in wissenschaftlicher Zeitschrift
  • Publikation
    Immobilization of an artificial imine reductase within silica nanoparticles improves its performance
    (Royal Society of Chemistry, 2016) Hestericová, Martina; Correro, Maria Rita; Lenz, Markus; Corvini, Philippe; Shahgaldian, Patrick; Ward, Thomas R.
    Silica nanoparticles equipped with an artificial imine reductase (biotinylated iridium complex conjugated with streptavidin) display marked redn. activity toward cyclic imines and NAD. The method, based on immobilization and protection of streptavidin on silica nanoparticles, shields the biotinylated metal cofactor against deactivation yielding >46,​000 turnovers in pure samples and 4000 turnovers in crude cellular exts.
    01A - Beitrag in wissenschaftlicher Zeitschrift
  • Publikation
    Production of superparamagnetic nanobiocatalysts for green chemistry applications
    (Springer, 23.04.2016) Gasser, Christoph; Ammann, Erik; Schäffer, Andreas; Shahgaldian, Patrick; Corvini, Philippe
    Immobilization of enzymes on solid supports is a convenient method for increasing enzymatic stability and enabling enzyme reuse. In the present work, a sorption-assisted surface conjugation method was developed and optimized to immobilize enzymes on the surface of superparamagnetic nanoparticles. An oxidative enzyme, i.e., laccase from Trametes versicolor was used as model enzyme. The immobilization method consists of the production of superparamagnetic nanoparticles by co-precipitation of FeCl2 and FeCl3. Subsequently, the particle surface is modified with an organosilane containing an amino group. Next, the enzymes are adsorbed on the particle surface before a cross-linking agent, i.e., glutaraldehyde is added which links the amino groups on the particle surface with the amino groups of the enzymes and leads to internal cross-linking of the enzymes as well. The method was optimized using response surface methodology regarding optimal enzyme and glutaraldehyde amounts, pH, and reaction times. Results allowed formulation of biocatalysts having high specific enzymatic activity and improved stability. The biocatalysts showed considerably higher stability compared with the dissolved enzymes over a pH range from 3 to 9 and in the presence of several chemical denaturants. To demonstrate the reusability of the immobilized enzymes, they were applied as catalysts for the production of a phenoxazinone dye. Virtually, 100 % of the precursor was transformed to the dye in each of the ten conducted reaction cycles while on average 84.5 % of the enzymatic activity present at the beginning of a reaction cycle was retained after each cycle highlighting the considerable potential of superparamagnetic biocatalysts for application in industrial processes.
    01A - Beitrag in wissenschaftlicher Zeitschrift