A5010102341- Enzyme Structure and Function
- Enzyme Production and Characterization
- Biofuel production and bioconversion
- Enzyme-mediated dye degradation
- Enzyme Catalysis and Immobilization
- Amino Acid Enzymes and Metabolism
- melanin and skin pigmentation
- Microbial Metabolism and Applications
- Diet, Metabolism, and Disease
- Polysaccharides and Plant Cell Walls
- Biochemical and Molecular Research
- Metal-Catalyzed Oxygenation Mechanisms
- Microbial Metabolites in Food Biotechnology
- Photosynthetic Processes and Mechanisms
- Biochemical and biochemical processes
- Analytical Chemistry and Chromatography
- Catalysis for Biomass Conversion
- Analytical chemistry methods development
- Microbial Metabolic Engineering and Bioproduction
- Metabolism and Genetic Disorders
- Plant nutrient uptake and metabolism
- Adrenal Hormones and Disorders
- Tannin, Tannase and Anticancer Activities
- Protein purification and stability
- Diet and metabolism studies
University of Eastern Finland
2016-2025
Finland University
2023
Joensuu Science Park
2002
The crystal structures of thermophilic xylanases from Chaetomium thermophilum and Nonomuraea flexuosa were determined at 1.75 2.1 A resolution, respectively. Both enzymes have the overall fold typical to family 11 with two highly twisted beta-sheets forming a large cleft. comparison 12 both mesophilic organisms showed that different are very similar. sequence identity differences correlated well structural differences. Several minor modifications appeared be responsible for increased thermal...
Laccases are copper-containing enzymes used in various applications, such as textile bleaching. Several crystal structures of laccases from fungi and bacteria available, but ascomycete types fungal (asco-laccases) have been rather unexplored, to date only the structure Melanocarpus albomyces laccase (MaL) has published. We now solved another asco-laccase, Thielavia arenaria (TaLcc1), at 2.5 Å resolution. The loops near T1 copper, forming substrate-binding pockets two asco-laccases, differ...
The C-terminus of the fungal laccase from Melanocarpus albomyces (MaL) is processed during secretion at a processing site conserved among ascomycete laccases. three-dimensional structure MaL has been solved as one first complete structures. According to crystal MaL, four C-terminal amino acids mature protein penetrate into tunnel leading towards trinuclear site. carboxylate group forms hydrogen bond with side chain His140, which also coordinates type 3 copper. In order analyze role...
Crystal structures of native and α‐ d ‐galactose‐bound Bacillus circulans sp. alkalophilus β‐galactosidase (Bca‐β‐gal) were determined at 2.40 2.25 Å resolutions, respectively. Bca‐β‐gal is a member family 42 glycoside hydrolases, forms 460 kDa hexameric structure in crystal. The protein consists three domains, which the catalytic domain has an (α/β) 8 barrel with cluster sulfur‐rich residues inside β‐barrel. shape active site clearly more open compared to only homologous available Protein...
The fungal secondary metabolite patulin is a mycotoxin widespread in foods and beverages which poses serious threat to human health. However, no enzyme was known be able degrade this mycotoxin. For the first time, we discovered that manganese peroxidase (MrMnP) from Moniliophthora roreri can efficiently patulin. MrMnP gene cloned into pPICZα(A) then recombinant plasmid transformed Pichia pastoris X-33. strain produced extracellular with an activity of up 3659.5 U/L. rapidly patulin,...
The manganese peroxidase (MnP) can degrade multiple mycotoxins including deoxynivalenol (DON) efficiently; however, the lignin components abundant in foods and feeds were discovered to interfere with DON catalysis. Herein, using MnP from Ceriporiopsis subvermispora (CsMnP) as a model, it was demonstrated that desired catalysis of DON, but not futile reactions lignin, reaction systems containing could be achieved by engineering supplementing boosting reactant. Specifically, two successive...
Engineering of protein oligomeric state or quaternary structure is a promising approach to adjust proteins for utilization in different applications and research. This study provides detailed investigation oligomerization within IlvD/EDD superfamily. A large 255 kDa tetrameric the superfamily, L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii, was engineered create dimeric form containing [2Fe-2S] catalytic center. Four variants, which contain mutations at two locations...
Abstract In this work, deoxyribose-5-phosphate aldolase ( Ec DERA, EC 4.1.2.4) from Escherichia coli was chosen as the protein engineering target for improving substrate preference towards smaller, non-phosphorylated aldehyde donor substrates, in particular acetaldehyde. The initial broad set of mutations directed to 24 amino acid positions active site or close vicinity, based on 3D complex structure E. DERA wild-type aldolase. specific activity variants containing one three characterised...
We present a novel crystal structure of the IlvD/EDD family enzyme, l-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii (RlArDHT, EC 4.2.1.25), which catalyzes conversion to 2-dehydro-3-deoxy-l-arabinonate. The enzyme is tetramer consisting dimer dimers, where each monomer composed two domains. active site contains catalytically important [2Fe-2S] cluster and Mg2+ ion buried between domains, also at interface. Lys129 was found be carbamylated. Ser480 Thr482 were shown...
Cortisol is a steroid hormone that produced by the adrenal gland. It primary stress increases glucose levels in blood stream. High concentrations of cortisol body can be used as biomarker for acute and chronic related mental physiological disorders. Therefore, accurate quantification fluids essential clinical diagnosis. In this article, we describe isolation recombinant anti-cortisol antibodies with high affinity discover their cross-reactivity other glucocorticoids. To binding site...
The Ilv/ED dehydratase protein family includes dihydroxy acid-, gluconate-, 6-phosphogluconate- and pentonate dehydratases. members of this are involved in various biosynthetic carbohydrate metabolic pathways. Here, we describe the first crystal structure D-xylonate from Caulobacter crescentus (CcXyDHT) at 2.7 Å resolution compare it with other available enzyme structures IlvD/EDD family. quaternary CcXyDHT is a tetramer, each monomer composed two domains which N-terminal domain forms...