Bioproduction of ethylenediamine-N,N'-disuccinic acid using immobilized fumarase-free EDDS lyase |
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| Institution: | 1. School of Life Science, Taizhou University, 1139 Shifu Rd., Taizhou 318000, China;2. College of Life Sciences, Shanghai Normal University, 100 Guilin Road, Shanghai 200234, China;3. Taizhou Bona Chemical Co. Ltd., 399 Yunxi Road, Taizhou 318000, China;4. Shanghai Institute of Technology, 120 Caobao Rd., Shanghai 200235，China;1. Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, Harbin 150030, PR China;2. College of Resources and Environmental Science, Northeast Agriculture University, Harbin, 150030, PR China;1. College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, Zhejiang, China;2. The Third Affiliated Hospital of Qiqihar Medical College, Qiqihar, Heilongjiang, China;1. State Key Laboratory of Bioreactor Engineering, Department of Food Science and Technology, School of Biotechnology, East China University of Science and Technology, Shanghai 200237, People’s Republic of China;2. State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, People’s Republic of China;3. Shanghai Collaborative Innovation Center for Biomanufacturing (SCICB), Shanghai 200237, People’s Republic of China;1. School of Lifescience, Taizhou University, 1139 Shifu Rd., Taizhou 318000, China;2. Taizhou Z-starpharm Co.Ltd., Taizhou 318000, China |
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| Abstract: | Ethylenediamine-N,N'-disuccinic acid (EDDS) is a promising chelating agent for the remediation of heavy metal-contaminated soil. In general, EDDS is produced through a chemical method. In this study, we report an efficient biotechnological approach for EDDS production using an immobilized enzyme. We expressed the EDDS lyase in E. coli and obtained 19.8 g/L of EDDS through a reaction catalyzed by crude enzymes, containing EDDS lyase and fumarase. After performing metal affinity chromatography-mediated purification, we thoroughly eliminated the fumarase activity, which could result in the unnecessary formation of malate. Then, the purified EDDS lyase was immobilized on a glutaraldehyde-activated amino carrier, and the immobilized enzyme was used in 11 batches (864.5 h). After optimization, 209.3 g/L EDDS was obtained in a 100 mL reaction system, resulting in 20.2 g of EDDS product with a purity of 99.8 % after isolation. The yields of reaction and isolation were 94.0 % and 91.8 %, respectively. In conclusion, this study describes a promising bioproduction process for industrial-level EDDS production. |
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| Keywords: | EDDS IMAC Amino carrier Immobilized enzyme |
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