2026-03-06T21:20:15Z https://iwate-u.repo.nii.ac.jp/oai

oai:iwate-u.repo.nii.ac.jp:00009094 2023-05-16T11:15:48Z 1504:1510

Microbial resolution of Nε-acetyl-DL-lysine with Rhodococcus sp. AIU Z-35-1 Isobe, Kimiyasu Tamauchi, Hiroshi Nagasawa, Shouko Nα-benzyloxycarbonyl-l-lysine Nα-benzyloxycarbonyl-d-lysine Nε-acetyl-l-lysine Nε-acetyl-d-lysine 6-Acetylamino-2-oxohexanoic acid An enantioselective resolution of Nε-acetyl-dl-lysine was investigated using cells from Rhodococcus sp. AIU Z-35-1 cultivated with l-lysine medium. Nε-Acetyl-l-lysine was deaminated by the resting cells, and 6-acetylamino-2-oxohexanoic acid was formed, but Nε-acetyl-d-lysine was not. This reaction was optimum at pH 6.5 and 30 °C, and the highest reaction speed was obtained by cells harvested after 1 day of cultivation. When 150 mM Nε-acetyl-dl-lysine was incubated at pH 6.5 and 30 °C for 5 days with cells harvested after 1 day of cultivation, more than 98% of the Nε-acetyl-l-lysine was converted to 6-acetylamino-2-oxohexanoic acid, and Nε-acetyl-d-lysine completely remained. Thus, Nε-acetyl-d-lysine was enantioselectively produced from Nε-acetyl-dl-lysine by the cell reaction with Rhodococcus sp. AIU Z-35-1. This cell reaction was also useful for the efficient production of 6-acetylamino-2-oxohexanoic acid from Nε-acetyl-l-lysine. journal article Elsevier B.V. 2009-07-01 AM application/pdf Journal of Molecular Catalysis B: Enzymatic 1-3 59 47 51 1381-1177 https://iwate-u.repo.nii.ac.jp/record/9094/files/jmcbe-v59i1-3p47-51.pdf https://iwate-u.repo.nii.ac.jp/records/9094 10.1016/j.molcatb.2008.12.019 Copyright © 2009 Elsevier B.V