Enzymatic production of 4-hydroxyphenylacetaldehyde by oxidation of the amino group of tyramine with a recombinant primary amine oxidase |
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| Institution: | 1. School of Life Sciences, Ludong University, Yantai 264025, China;2. School of Agriculture, Ludong University, Yantai 264025, China;1. Engineering Research Center of Bio-Process of Ministry of Education, School of Food and Biological Engineering, Hefei University of Technology, Hefei, 230009, PR China;2. Hefei Preschool Education College, Hefei, 230013, PR China;1. Department of Biology, Concordia University, Montréal, Québec H4B 1R6, Canada;2. Centre for Structural and Functional Genomics, Concordia University, Montréal, Québec H4B 1R6, Canada;3. Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94704, USA;1. College of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, 310015, PR China;2. Institute of Quality and Standard for Agriculture Products, Zhejiang Academy of Agricultural Science, Hangzhou, 310021, PR China;3. School of Food Science and Technology, Jiangnan University, Wuxi 214122, PR China;1. Microbial Engineering Group, International Centre for Genetic Engineering and Biotechnology, New Delhi, 110067, India;2. Systems Biology for Biofuel Group, International Centre for Genetic Engineering and Biotechnology, New Delhi, 110067, India;3. DBT-ICGEB Centre for Advanced Bioenergy Research, International Centre for Genetic Engineering and Biotechnology, New Delhi, 110067, India;4. DBT-ICT Centre for Energy Biosciences, Institute of Chemical Technology, Mumbai 400019, India;1. School of Life Sciences, Jilin University, Changchun 130021, PR China;2. School of Stomatology, Jilin University, Changchun 130000, PR China |
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| Abstract: | In this study, an efficient enzymatic process for the synthesis of 4-hydroxyphenylacetaldehyde (4-HPAA) from tyramine was developed using whole cells of recombinant Escherichia coli co-expressing primary amine oxidase (PrAO) from E. coli and catalase (CAT) from Bacillus pumilus. The reaction conditions for the synthesis of 4-HPAA were systematically optimized starting from a monophasic aqueous buffer. The optimum reaction temperature, pH, and biocatalyst loading were 33 °C, 7.5, and 20 g/L wet cells, respectively. Substrate feeding strategies were employed to alleviate substrate inhibition, providing a 14.8 % increase in yield. A biphasic catalytic system was explored to avoid product inhibition and thus further improve the 4-HPAA yield. Ethyl acetate was found to be the best organic solvent, and the optimum volume ratio of the organic phase to the aqueous phase was 40 % (v/v). Under the optimized conditions on a 1 L scale, a yield of 76.5 % was obtained with a substrate concentration of 120 mM. Thus, the bioconversion was more efficient in the ethyl acetate/buffer biphasic system than in the monophasic aqueous system, and the yield of 4-HPAA was improved 1.89-fold. |
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| Keywords: | Primary amine oxidase 4-hydroxyphenylacetaldehyde Biotransformation Biphasic biocatalytic system |
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