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Efficient aspartic acid production by a psychrophile-based simple biocatalyst
Takahisa Tajima1,2, Mai Hamada3, Yutaka Nakashimada3,4
1Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1, Kagamiyama, Higashi-Hiroshima, 739-8530, Japan. ttajima@hiroshima-u.ac.jp.
This study introduces a novel biocatalyst system (PSCat) for efficient aspartic acid production from fumaric acid. The system prevents L-malic acid byproduct formation, enhancing yield for biotechnological applications.
Area of Science:
- Biotechnology
- Enzyme Engineering
- Metabolic Engineering
Background:
- Aspartic acid biosynthesis competes with L-malic acid production in Escherichia coli.
- Psychrophile-based Simple bioCatalyst (PSCat) systems utilize heat-inactivated enzymes for specific bioconversions.
Purpose of the Study:
- To develop a PSCat system for selective conversion of fumaric acid to aspartic acid.
- To investigate the impact of heat inactivation on competing enzymatic activities.
- To evaluate the efficiency and reusability of the PSCat system for aspartic acid production.
Main Methods:
- Expression of E. coli aspartase in psychrophilic Shewanella livingstonensis Ac10.
- Heat treatment of the engineered psychrophilic host at 50 °C for 15 min to create the PSCat.
- Alginate immobilization of the PSCat for repeated use in fumaric acid conversion.
Main Results:
- The PSCat successfully converted fumaric acid to aspartic acid.
- Formation of L-malic acid was prevented due to heat inactivation of endogenous fumarase.
- Alginate-immobilized PSCat achieved high yields and was reusable for nine cycles.
Conclusions:
- The PSCat system offers a viable strategy for selective aspartic acid production.
- Heat inactivation of competing enzymes is effective in enhancing target compound yield.
- PSCat technology presents a promising approach for biotechnological production of valuable compounds.
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