Efficient agmatine production using an arginine decarboxylase with substrate‐specific activity. Issue 9 (28th March 2017)
- Record Type:
- Journal Article
- Title:
- Efficient agmatine production using an arginine decarboxylase with substrate‐specific activity. Issue 9 (28th March 2017)
- Main Title:
- Efficient agmatine production using an arginine decarboxylase with substrate‐specific activity
- Authors:
- Sun, Anran
Song, Wei
Qiao, Weihua
Chen, Xiulai
Liu, Jia
Luo, Qiuling
Liu, Liming - Abstract:
- Abstract: BACKGROUND: Agmatine is a valuable pharmaceutical intermediate biosynthesised froml ‐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 towardsl ‐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
- Is Part Of:
- Journal of chemical technology & biotechnology. Volume 92:Issue 9(2017)
- Journal:
- Journal of chemical technology & biotechnology
- Issue:
- Volume 92:Issue 9(2017)
- Issue Display:
- Volume 92, Issue 9 (2017)
- Year:
- 2017
- Volume:
- 92
- Issue:
- 9
- Issue Sort Value:
- 2017-0092-0009-0000
- Page Start:
- 2383
- Page End:
- 2391
- Publication Date:
- 2017-03-28
- Subjects:
- l‐arginine decarboxylase -- agmatine -- Escherichia coli recombinant -- biocatalysts
Biotechnology -- Periodicals
Chemistry, Technical -- Periodicals
Chemical engineering -- Periodicals
Industries -- Environmental aspects -- Periodicals
660 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-4660 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jctb.5245 ↗
- Languages:
- English
- ISSNs:
- 0268-2575
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4957.089000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2951.xml