The invention discloses a high-efficiency
lysine decarboxylase
mutant and an application of the high-efficiency
lysine decarboxylase
mutant in synthesis of pentamethylene
diamine. A series of mutants including a single
mutant (such as N218G, T222V, C244P and the like), a
double mutant and a three mutant are obtained by carrying out multi-site
mutation on
wild type lysine decarboxylase (SEQ ID NO.2) from
Klebsiella grimontii. The
catalytic efficiency of the mutant is remarkably improved, and the activity of the mutant is improved by 5.0-10.2 times compared with that of a
wild type enzyme. According to the method disclosed by the invention, the substrate conversion rate of 99% or above can be realized within 2 hours through an optimized process of constructing an
expression vector and a
genetically engineered bacterium, inducing expression of
lysine decarboxylase and synthesizing 1, 5-pentanediamine by utilizing a whole-
cell catalysis technology. Compared with a traditional chemical method and a natural
enzyme method, the method disclosed by the invention has the advantages of simplified process, high
catalytic efficiency, low production cost and the like, and is suitable for producing bio-based 1, 5-pentamethylene
diamine and nylon 56 salt.