Dong‐Woo Lee
Yonsei University · 生化学・遺伝学・分子生物学
研究室紹介
Professor Dong-Woo Lee's research lab specializes in microbial biotechnology and industrial enzymology, focusing on thermophilic and hyperthermophilic microorganisms for sustainable bioprocesses. The lab investigates novel enzymes such as lipases and isomerases from extremophiles, with applications in biofuel production, bioremediation, and plant-based meat analogs. Key research directions include metabolic engineering, post-translational protein modification (e.g., lysine acetylation), and the development of advanced bioprocesses using non-traditional biomass feedstocks. The lab also explores the structural and functional characterization of microbial enzymes to enhance their industrial utility under extreme conditions.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15A thermophilic microorganism, Bacillus thermoleovorans ID-1, isolated from hot springs in Indonesia, showed extracellular lipase activity and high growth rates on lipid substrates at elevated temperatures. On olive oil (1.5%, w/v) as the sole carbon source, the isolate ID-1 grew very rapidly at 65 degrees C with its specific growth rate (2.50 h(-1)) and its lipase activity reached the maximum value of 520 U l(-1) during the late exponential phase and then decreased. In addition to this, isolate
The araA gene encoding L-arabinose isomerase (AI) from the hyperthermophilic bacterium Thermotoga maritima was cloned and overexpressed in Escherichia coli as a fusion protein containing a C-terminal hexahistidine sequence. This gene encodes a 497-amino-acid protein with a calculated molecular weight of 56,658. The recombinant enzyme was purified to homogeneity by heat precipitation followed by Ni(2+) affinity chromatography. The native enzyme was estimated by gel filtration chromatography to be
The burgeoning demand for plant-based meat analogs (PBMAs) stems from environmental, health, and ethical concerns, yet replicating the sensory attributes of animal meat remains challenging. This comprehensive review explores recent innovations in PBMA ingredients and methodologies, emphasizing advancements in texture, flavor, and nutritional profiles. It chronicles the transition from soy-based first-generation products to more diversified second- and third-generation PBMAs, showcasing the utili
Current fossil-based commercial products pose a serious threat to global reserves of natural resources and the preservation of the natural environment. During recent decades, great efforts have been made to increase the availability of non-utilizable biomass as alternative feedstocks and reduce environmental pollution to achieve a more sustainable bioeconomy. Several bio-sectors have emerged for the production of bio-based products to replace fossil-based equivalents through bioprocesses using b
Recent analysis of prokaryotic N(ε)-lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the N(ε)-lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides repres
Poultry feathers consist mainly of the protein keratin, which is rich in β-pleated sheets and consequently resistant to proteolysis. Although many keratinases have been identified, the reasons for their substrate specificity towards β-keratin remain unclear due to difficulties in preparing a soluble feather keratin substrate for use in activity assays. In the present study, we overexpressed Gallus gallus chromosomes 2 and 27 β-keratin-encoding genes in Escherichia coli, purified denatured recomb
The gadB gene encoding glutamate decarboxylase (GAD) from Lactobacillus plantarum was cloned and expressed in Escherichia coli. The recombinant enzyme exhibited maximal activity at 40 °C and pH 5.0. The 3D model structure of L. plantarum GAD proposed that its C-terminal region (Ile454-Thr468) may play an important role in the pH dependence of catalysis. Accordingly, C-terminally truncated (Δ3 and Δ11 residues) mutants were generated and their enzyme activities compared with that of the wild-type
Bioactive peptides (BPs) play key roles in regulating cellular metabolism, and are therefore of special interest to the nutraceutical and pharmaceutical industries. Protein digestion is a major route to production of BPs. Biocatalyst-aided processes are advantageous in that they generate protein hydrolysates with high specificity that are non-immunogenic and resistant to proteolysis in the gastrointestinal tract. On the other hand, these approaches are limited by their high production cost and p
Keratin degradation is of great interest for converting agro-industrial waste into bioactive peptides and is directly relevant for understanding the pathogenesis of superficial infections caused by dermatophytes. However, the mechanism of this process remains unclear. Here, we obtained the complete genome sequence of a feather-degrading, extremely thermophilic bacterium, Fervidobacterium islandicum AW-1 and performed bioinformatics-based functional annotation. Reverse transcription PCR revealed
Production of reactive oxygen species (ROS) induces oxidative damages, decreases cellular energy conversion efficiencies, and induces metabolic diseases in humans. During respiration, cytochrome bc(1) efficiently oxidizes hydroquinone to quinone, but how it performs this reaction without any leak of electrons to O(2) to yield ROS is not understood. Using the bacterial enzyme, here we show that a conserved Tyr residue of the cytochrome b subunit of cytochrome bc(1) is critical for this process. S