Abstract：
:The Pseudomonas putida arginine deiminase (ADI), a natural cytosolic enzyme, and Thermobifida fusca cutinase were co-expressed in Escherichia coli, and the optimized cutinase gene was used for increasing its expression level. 90.9% of the total ADI protein was released into culture medium probably through a nonspecific leaking mechanism caused by the co-expressed cutinase. The enzymatic properties of the extracellular ADI were found to be similar to those of ADI prepared by conventional cytosolic expression. Extracellular production of ADI was further scaled up in a 3-L fermentor. When the protein expression was induced by IPTG (25.0μM) and lactose (0.1gL(-1)h(-1)) at 30°C, the extracellular ADI activity reached 101.2UmL(-1), which represented the highest ADI production ever reported. In addition, the enzymatic synthesis of l-citrulline was performed using the extracellularly expressed ADI, and the conversion rate reached 100% with high substrate concentration at 650gL(-1).
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Su L,Ma Y,Wu Jdoi
10.1016/j.biortech.2015.07.081subject
Has Abstractpub_date
2015-11-01 00:00:00pages
176-83eissn
0960-8524issn
1873-2976pii
S0960-8524(15)01043-3journal_volume
196pub_type
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