Väitös (biokemia): MSc Mohsin Imran
Aika
12.6.2025 klo 12.00 - 16.00
MSc Mohsin Imran esittää väitöskirjansa ”Structural studies of enzymes from thermophilic organisms and identification of their thermostability factors” julkisesti tarkastettavaksi Turun yliopistossa torstaina 12.6.2025 klo 12.00 (Turun yliopisto, Medisiina C, Osmo Järvi -luentosali, Kiinamyllynkatu 10, Turku).
Vastaväittäjänä toimii professori Matthew Groves (University of Groningen, Alankomaat) ja kustoksena professori Jyrki Heino (Turun yliopisto). Tilaisuus on englanninkielinen. Väitöksen alana on biokemia.
Väitöskirja yliopiston julkaisuarkistossa: https://urn.fi/URN:ISBN:978-952-02-0184-5 (kopioi linkki selaimeen).
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Tiivistelmä väitöstutkimuksesta:
Structural studies of enzymes from thermophilic organisms and identification of their thermostability factors
Thermophilic enzymes are characterized by high stability at elevated temperatures and have emerged as valuable tools in industrial biotechnology and bioenergy in recent years. They have the potential to make chemical processes more sustainable and less harmful to the environment. This dissertation presents structural and functional characterization of four thermophilic enzymes: three from fungal sources and one from a bacterial source.
High-resolution X-ray crystallography was employed to determine the three-dimensional structures of each enzyme, revealing distinct features that underlie their catalytic function and thermostability. More specifically, a Thermoascus aurantiacus copper-dependent monooxygenase involved in cellulose degradation displayed structural differences in glycosylation patterns, electrostatic interactions, and in surface loops compared to other monooxygenases. A Chaetomium thermophilum ß-glucosidase implicated in cellobiose to glucose catalysis, demonstrated variations in linker regions and glycosylation patterns. A Chaetomium thermophilum superoxide dismutase attributed to carry out redox reactions, exhibited stability-associated characteristics, including oligomerization, increased ratio of polar residues, and interface area. Finally, a Caloramator australiacus carbonic anhydrase ascribed in reversible hydration of CO2, revealed variations in loop regions, charged residues, and hydrophobic interactions.
These results could help us understand better how enzymes adapt to high temperatures and which structural changes are significant to develop improved enzymes through protein engineering. As the demand for environmentally sustainable technologies continues to grow, thermophilic enzymes hold promise for applications in renewable energy production, waste reduction, and green manufacturing. Thus, this work contributes to our scientific knowledge of protein stability and could help creating new ideas for the use of enzymes in circular chemistry and biotechnology.
Vastaväittäjänä toimii professori Matthew Groves (University of Groningen, Alankomaat) ja kustoksena professori Jyrki Heino (Turun yliopisto). Tilaisuus on englanninkielinen. Väitöksen alana on biokemia.
Väitöskirja yliopiston julkaisuarkistossa: https://urn.fi/URN:ISBN:978-952-02-0184-5 (kopioi linkki selaimeen).
***
Tiivistelmä väitöstutkimuksesta:
Structural studies of enzymes from thermophilic organisms and identification of their thermostability factors
Thermophilic enzymes are characterized by high stability at elevated temperatures and have emerged as valuable tools in industrial biotechnology and bioenergy in recent years. They have the potential to make chemical processes more sustainable and less harmful to the environment. This dissertation presents structural and functional characterization of four thermophilic enzymes: three from fungal sources and one from a bacterial source.
High-resolution X-ray crystallography was employed to determine the three-dimensional structures of each enzyme, revealing distinct features that underlie their catalytic function and thermostability. More specifically, a Thermoascus aurantiacus copper-dependent monooxygenase involved in cellulose degradation displayed structural differences in glycosylation patterns, electrostatic interactions, and in surface loops compared to other monooxygenases. A Chaetomium thermophilum ß-glucosidase implicated in cellobiose to glucose catalysis, demonstrated variations in linker regions and glycosylation patterns. A Chaetomium thermophilum superoxide dismutase attributed to carry out redox reactions, exhibited stability-associated characteristics, including oligomerization, increased ratio of polar residues, and interface area. Finally, a Caloramator australiacus carbonic anhydrase ascribed in reversible hydration of CO2, revealed variations in loop regions, charged residues, and hydrophobic interactions.
These results could help us understand better how enzymes adapt to high temperatures and which structural changes are significant to develop improved enzymes through protein engineering. As the demand for environmentally sustainable technologies continues to grow, thermophilic enzymes hold promise for applications in renewable energy production, waste reduction, and green manufacturing. Thus, this work contributes to our scientific knowledge of protein stability and could help creating new ideas for the use of enzymes in circular chemistry and biotechnology.
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