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Bioreaction Engineering Lab
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The lab assembles proteins and enzymes in new ways to bring out new functions.
AboutAbout the lab
Bringing out new functions through new encounters between enzymes.
The Bioreaction Engineering Lab is the lab of Professor Sosaku Ichikawa and Associate Professor Hidehiko Hirakawa.
The lab's website, presented as Associate Professor Hirakawa's Hirakawa Lab, describes research that combines multiple enzymes and proteins to bring out new functions.
Because multiple enzymes work together inside living organisms, the lab believes that combining enzymes can bring out even more of their power.
For graduation research, the lab accepts students from the Applied Life Chemistry Course of the College of Agro-Biological Resource Sciences.
Key terms
- Enzyme
- A protein that acts as a catalyst to drive chemical reactions in living organisms. Enzymes are widely used in pharmaceuticals, detergents, food processing, and more.
- Cytochrome P450
- A group of heme-containing proteins. They cleave carbon-hydrogen bonds and catalyze diverse reactions such as hydroxylation.
- Transpeptidase
- An enzyme that cuts a specific sequence in a protein and re-forms a bond with another protein or peptide.
NewsLab news
From the 2027 academic year, the lab's graduate school affiliation will change to the Graduate School of Interdisciplinary Creation
An undergraduate student received the FY2024 (Reiwa 6) College of Agro-Biological Resource Sciences Outstanding Graduation Research Award
An undergraduate student received the FY2024 (Reiwa 6) Applied Life Chemistry Course Graduation Research Award (Biochemical Engineering)
ResearchResearch themes
All activities of living organisms are based on chemical reactions catalyzed by enzymes. This lab brings together multiple enzymes and proteins in unprecedented combinations and assemblies, aiming to achieve new functions and improve existing ones.
*Illustrative imageGathering enzymes with a scaffold protein
Using a subunit of archaeal PCNA as a linking unit, cytochrome P450, an electron transfer protein, and a reductase assemble simply by being mixed. The resulting self-sufficient enzyme, PUPPET, works on its own and shows high catalytic activity.
*Illustrative imageMastering enzymes that join proteins
Sortase A, a transpeptidase, joins proteins and peptides in aqueous solution, but the reaction is reversible, so the yield does not reach 100%. By adding a sequence that makes the product adopt a stable secondary structure, the lab suppressed the reverse reaction and greatly improved the yield.
MembersFaculty
- ProfessorSosaku Ichikawa
- Associate ProfessorHidehiko Hirakawa
VoicesStudent voices
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Report an errorAbout the images
The top and research theme images are illustrative and were not taken at the lab. They are cropped from Wikimedia Commons images. Cropped CC BY-SA images are provided under the same CC BY-SA license as the original (version shown on each line).
- Top image: “P04971 homology model thrombin-like enzyme batroxobin” Fvasconcellos (talk · contribs) / Public domain (cropped)
- Gathering enzymes with a scaffold protein: “1K6F Crystal Structure Of The Collagen Triple Helix Model Pro- Pro-Gly103 05” Nevit Dilmen / CC BY-SA 3.0 (cropped)
- Mastering enzymes that join proteins: “Electrophoresis - Filling 1D gel wells with proteins mixture” Jean-Etienne Poirrier / CC BY-SA 2.0 (cropped)
- Related lab (Food Functional Chemistry Lab): “Tissue glass Dounce homogenizer-03” Lilly_M / CC BY-SA 3.0 (cropped)
- Related lab (Environmental Molecular Microbiology Lab): “Bacteria on everyday objects” Manjunaf / CC BY-SA 4.0 (cropped)
- Related lab (Industrial Microbial Resources Lab): “Microbiological seeding” Nycterixnycterix / CC BY 4.0 (cropped)
- Related lab (Cell Function Development Engineering Lab): “Small cell culture flat flask” Lilly_M / CC BY-SA 3.0 (cropped)
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