Mart Loog
Petri-Jaan Lahtvee
Kaspar Valgepea
Lauri Vares
Research group of microbial genetics
Prof. Maia Kivisaar
Soil bacterium Pseudomonas putida could potentially be used as cell factories in various biotechnological settings because of its good genetic accessibility, metabolic versatility and high tolerance to toxic and harsh conditions met in industrial processes. P. putida has also a great potential in lignin valorization. The research group of Maia Kivisaar has studied molecular mechanisms of bacterial evolution under stressful conditions and physiological adaptation of bacteria to environmental stress by using soil bacterium P. putida as a model organism. The research group has also a long-term experience in characterization of phenolic compounds degradation genes and investigation of regulation of these genes in pseudomonads. The competence of the research group can be used for genetic manipulation of P. putida, monitoring stability and stress levels of engineered strains and further optimization of engineered strains by adaptive laboratory evolution (ALE).
Laboratory of recalcitrant polysaccharides
Dr. Priit Väljamäe
Structural polysaccharides, cellulose and chitin (collectively referred to as recalcitrant polysaccharides) are the most abundant biopolymers in Nature and have great potential as a renewable energy- and carbon source. These polysaccharides can be valorized to a plethora of different value-added products like fuels, chemicals, and nanomaterials. Enzyme-aided valorization provides an environment friendly and sustainable alternative to the traditional chemical and mechanical processes. The design of cost-efficient enzyme technologies implies detailed knowledge on the enzyme mechanism and kinetics. With more than 20 years of experience in the field, we have established a solid framework for in-depth characterization of enzymes involved in degradation of recalcitrant polysaccharides. Our strength is in application of in-house developed state-of-the-art methods that enable to pinpoint the rate limiting steps in complex heterogeneous enzyme catalysis. Information about these kinetic bottlenecks is used to overcome the substrate recalcitrance by designing novel enzymes and their combinations.