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Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae

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Abstract

Adenylate deaminase (AMPD) is an amino hydrolase that catalyzes the irreversible hydrolysis of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia. In this study, the effect of different hosts on the enzymatic properties of AMPD from Aspergillus oryzae GX-08 was investigated and showed that Bacillus subtilis WB600 was more suitable for producing AMPD with a higher activity of 2540 U/mL. After purification, the optimal temperature and pH of recombinant AMPD were 55 °C and pH 6.0, respectively, and its activity was significantly enhanced by 10 mM Fe3+ with an increase of 236%. More importantly, the recombinant AMPD specifically and effectively catalyzed the conversion between AMP and IMP, in which 10 mL of crude AMPD achieved a conversion ratio of 76.4% after 40 min. Therefore, B. subtilis WB600 provides a potential platform for producing AMPD with excellent catalytic ability and catalytic specificity.

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Acknowledgements

This research was financially supported by the National Natural Science Foundation of China (31560027), Guangxi Natural Science Foundation (2017GXNSFAA198297 and 2016GXNSFAA380247), Guangxi Scholarship Fund of Guangxi Education Department, and the “Bagui Young Scholars” Special Project.

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Authors and Affiliations

  1. College of Light Industry and Food Engineering, Guangxi University, Nanning, 530004, China

    Chengzhu Ke, Shubo Li, Yanyan Cui & Hua Qiu

  2. College of Life Science and Technology, Guangxi University, Nanning, 530005, China

    Zongwen Pang

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  1. Chengzhu Ke
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  2. Shubo Li
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  4. Hua Qiu
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Correspondence to Shubo Li.

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Ke, C., Li, S., Cui, Y. et al. Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae. Bioprocess Biosyst Eng 43, 919–926 (2020). https://doi.org/10.1007/s00449-020-02288-7

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