S
Soo-Jin Yeom
Researcher at Korea Research Institute of Bioscience and Biotechnology
Publications - 70
Citations - 1696
Soo-Jin Yeom is an academic researcher from Korea Research Institute of Bioscience and Biotechnology. The author has contributed to research in topics: Isomerase & Chemistry. The author has an hindex of 24, co-authored 63 publications receiving 1496 citations. Previous affiliations of Soo-Jin Yeom include Konkuk University.
Papers
More filters
Journal ArticleDOI
A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments
Dae-Hee Lee,Dae-Hee Lee,Su-Lim Choi,Eugene Rha,Soo Jin Kim,Soo-Jin Yeom,Jae Hee Moon,Seung-Goo Lee,Seung-Goo Lee +8 more
TL;DR: The presented mAP enzyme is the first thermolabile AP found in cold-adapted marine metagenomes and may be useful for efficient dephosphorylation of linearized DNA.
Journal ArticleDOI
A synthetic microbial biosensor for high-throughput screening of lactam biocatalysts
Soo-Jin Yeom,Moonjeong Kim,Kil Koang Kwon,Yaoyao Fu,Eugene Rha,Sung Hyun Park,Hye Won Lee,Haseong Kim,Dae-Hee Lee,Dong-Myung Kim,Seung-Goo Lee +10 more
TL;DR: A sensitive transcription factor-based biosensor for high-throughput screening of marine metagenome and find a cyclase that can cyclize ω-amino fatty acids to lactam.
Journal ArticleDOI
Increase of lycopene production by supplementing auxiliary carbon sources in metabolically engineered Escherichia coli
TL;DR: In the fed-batch culture of glycerol using a metabolically engineered strain of Escherichia coli, supplementation with glucose as an auxiliary carbon source increased Lycopene production due to a significant increase in cell mass, despite a reduction in specific lycopene content.
Journal ArticleDOI
Improvement in the thermostability of D-psicose 3-epimerase from Agrobacterium tumefaciens by random and site-directed mutagenesis.
TL;DR: The results suggest that the I33L S213C variant may be useful as an industrial producer of d-psicose and the improvement in thermostability in these variants may have resulted from increased putative hydrogen bonds and formation of new aromatic stacking interactions.
Journal ArticleDOI
Biochemical characterization and FAD-binding analysis of oleate hydratase from Macrococcus caseolyticus.
TL;DR: The putative fatty acid hydratase is an FAD-dependent enzyme, and the residues G29, G31, S34, E50, and E56 are essential for F AD-binding.