Acetaldehyde Detoxification Using Resting Cells of Recombinant Escherichia coli Overexpressing Acetaldehyde Dehydrogenase |
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Authors: | Zhengying Yao Chong Zhang Junfeng Zhao Fengxia Lu Xiaomei Bie Zhaoxin Lu |
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Affiliation: | 1. College of Food Science and Technology, Nanjing Agricultural University, 1 Weigang, Nanjing, 210095, People’s Republic of China 2. Nanjing Institute for Comprehensive Utilization of Wild Plants, 4 Jiangwangmiao Street, Nanjing, 210042, People’s Republic of China 3. College of Food Science and Engineering, Henan University of Science and Technology, Tianjing Road, Luoyang, 471003, People’s Republic of China
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Abstract: | Acetaldehyde dehydrogenase (E.C. 1.2.1.10) plays a key role in the acetaldehyde detoxification. The recombinant Escherichia coli cells producing acetaldehyde dehydrogenase (ist-ALDH) were applied as whole-cell biocatalysts for biodegradation of acetaldehyde. Response surface methodology (RSM) was employed to enhance the production of recombinant ist-ALDH. Under the optimum culture conditions containing 20.68 h post-induction time, 126.75 mL medium volume and 3 % (v/v) inoculum level, the maximum ist-ALDH activity reached 496.65?±?0.81 U/mL, resulting in 12.5-fold increment after optimization. Furthermore, the optimum temperature and pH for the catalytic activity of wet cells were 40 °C and pH 9.5, respectively. The biocatalytic activity was improved 80 % by permeabilizing the recombinant cells with 0.075 % (v/v) Triton X-100. When using 2 mmol/L NAD+ as coenzyme, the permeabilized cells could catalyze 98 % of acetaldehyde within 15 min. The results indicated that the recombinant E. coli with high productivity of ist-ALDH might be highly efficient and easy-to-make biocatalysts for acetaldehyde detoxification. |
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