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Efficient agmatine production using an arginine decarboxylase with substrate‐specific activity
Author(s) -
Sun Anran,
Song Wei,
Qiao Weihua,
Chen Xiulai,
Liu Jia,
Luo Qiuling,
Liu Liming
Publication year - 2017
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.5245
Subject(s) - agmatine , arginine decarboxylase , arginine , substrate (aquarium) , substrate specificity , production (economics) , chemistry , biochemistry , enzyme , biology , economics , amino acid , ecology , macroeconomics
BACKGROUND Agmatine is a valuable pharmaceutical intermediate biosynthesised from l ‐arginine by arginine decarboxylase (EC 4.1.1.19). It has various potential therapeutic functions in neurotransmitter systems, nitric oxide synthesis, and polyamine metabolism. To establish a green and efficient process for agmatine production, a novel arginine decarboxylase ( Sp A9) from Shewanella putrefaciens was identified, overexpressed, and functionally characterised in this study. RESULTS The Sp A9 gene from S. putrefaciens was overexpressed in Escherichia coli BL21(DE3), and the recombinant Sp A9 was purified 7.7‐fold. The recombinant Sp A9 exhibited a higher K cat / K m value (4.8 s −1 mM −1 ). Furthermore, Sp A9 showed the highest activity at pH 8.5 and 37°C towards l ‐arginine. The highest enzyme activity of 1281 U mL −1 was achieved by optimising the nutrient, culture, and induction conditions. Under optimum transformation conditions, the maximum conversion yield of agmatine was 92.6%, with a space‐time yield of 276.88 g L −1 ·day −1 at a 1 L scale. CONCLUSIONS To our best knowledge, this bioprocess produced the highest yield and conversion rate of any biocatalyst method reported yet. It is also a greener and more cost‐effective method for agmatine production compared with other available methods in the pharmaceutical industry. © 2017 Society of Chemical Industry