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KMID : 0545120160260091586
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Journal of Microbiology and Biotechnology
2016 Volume.26 No. 9 p.1586 ~ p.1592
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Functional Study of Lysine Decarboxylases from Klebsiella pneumoniae in Escherichia coli and Application of Whole Cell Bioconversion for Cadaverine Production
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Kim Jung-Ho
Kim Hyun-Joong
Kim Yong-Hyun
Jeon Jong-Min
Song Hun-Suk
Kim Jun-Young
No So-Young
Shin Ji-Hyun
Choi Kwon-Young
Park Kyung-Moon
Yang Yung-Hun
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Abstract
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Klebsiella pneumoniae is a gram-negative, non-motile, rod-shaped, and encapsulated bacterium in the normal flora of the intestines, mouth, skin, and food, and has decarboxylation activity, which results in generation of diamines (cadaverine, agmatine, and putrescine). However, there is no specific information on the exact mechanism of decarboxylation in K. pnuemoniae. Specifically lysine decarboxylases that generate cadaverine with a wide range of applications has not been shown. Therefore, we performed a functional study of lysine decarboxylases. Enzymatic characteristics such as optimal pH, temperature, and substrates were examined by overexpressing and purifying CadA and LdcC. CadA and LdcC from K. pneumoniae had a preference for L-lysine, and an optimal reaction temperature of 37oC and an optimal pH of 7. Although the activity of purified CadA from K. pneumoniae was lower than that of CadA from E. coli, the activity of K. pneumoniae CadA in whole cell bioconversion was comparable to that of E. coli CadA, resulting in 90% lysine conversion to cadaverine with pyridoxal 5’-phosphate L-lysine.
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KEYWORD
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Klebsiella pneumoniae, biotransformation, lysine decarboxylase, cadaverine, optimization
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