2 results match your criteria: "Division of Biotechnology The Catholic University of Korea[Affiliation]"
J Microbiol Biotechnol
February 2017
Division of Biotechnology The Catholic University of Korea, Bucheon 14662, Republic of Korea.
Lysine decarboxylase (CadA) converts -lysine into cadaverine (1,5-pentanediamine), which is an important platform chemical with many industrial applications. Although there have been many efforts to produce cadaverine through the soluble CadA enzyme or whole cells overexpressing the CadA enzyme, there have been few reports concerning the immobilization of the CadA enzyme. Here, we have prepared a cross-linked enzyme aggregate (CLEA) of CadA and performed bioconversion using CadA.
View Article and Find Full Text PDFJ Microbiol Biotechnol
October 2014
Division of Biotechnology The Catholic University of Korea, Bucheon 420-743, Republic of Korea.
Proteus vulgaris K80 lipase was expressed in Escherichia coli BL21 (DE3) cells and immobilized on amine-terminated magnetic microparticles (Mag-MPs). The immobilization yield and activity retention were 84.15% and 7.
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