Kyushu University · Biochemistry, Genetics and Molecular Biology
Professor Noriho Kamiya's research lab specializes in developing innovative bioconjugation strategies and biocatalytic systems for precise protein and nucleic acid engineering. The lab focuses on leveraging microbial enzymes such as transglutaminase and lipase to enable site-specific modifications of biomolecules, with applications in protein–protein conjugation, chiral synthesis, and functional biomaterials. A key direction involves designing smart hydrogels and delivery systems through enzyme-mediated cross-linking for regenerative medicine and cell encapsulation. The lab also explores the rational design of biocatalysts for enhanced activity and selectivity in non-aqueous environments.
Figures are computed from collected data and may differ slightly.
Here, we report the N-terminal glycine (Gly) residue of a target protein can be a candidate primary amine for site-specific protein conjugation catalyzed by microbial transglutaminase (MTG) from Streptomyces mobaraensis. Gly5-enhanced green fluorescent protein (EGFP) (EGFP with five additional Gly residues at its N-terminus) was cross-linked with Myc-dihydrofolate reductase (DHFR) (DHFR with the myc epitope sequence at its N-terminus) to yield DHFR-EGFP heterodimers. The reactivities of addition
Abstract Enantioselective esterification of menthol with fatty acids using a surfactant‐coated lipase was carried out in organic media. The surfactant‐coated lipase originating from Candida cylindracea appeared to be highly enantioselective and good biocatalyst for the resolution of racemic menthol. The enzymatic activity of the lipase in organic media was significantly increased by a coating with a nonionic surfactant. The reaction rate of the coated lipase was more than 100 times that of the p
DNA was site-specifically conjugated to a substrate peptide of microbial transglutaminase fused to the N- or C-terminus of target proteins without the loss of the proteins' functions of interest.
Horseradish peroxidase-mediated oxidative cross-linking of a thiolated poly(ethylene glycol) is promoted in the absence of exogenous hydrogen peroxide, by adding a small amount of a phenolic compound under physiological conditions. The prepared hydrogel can encapsulate and release living mammalian cells.
Open papers in the app to read, cite, and organize with AI.
