The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis
Electron. j. biotechnol
; 19(3): 43-48, May 2016. ilus
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| ID: lil-787006
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ABSTRACT
Background:
D-Hydroxyphenylglycine is considered to be an important chiral molecular building-block of antibiotic reagents such as pesticides, and β-lactam antibiotics. The process of its production is catalyzed by D-hydantoinase and D-carbamoylase in a two-step enzyme reaction. How to enhance the catalytic potential of the two enzymes is valuable for industrial application. In this investigation, an Escherichia coli strain genetically engineered with D-hydantoinase was immobilized by calcium alginate with certain adjuncts to evaluate the optimal condition for the biosynthesis of D-carbamoyl-p-hydroxyphenylglycine (D-CpHPG), the compound further be converted to D-hydroxyphenylglycine (D-HPG) by carbamoylase.Results:
The optimal medium to produce D-CpHPG by whole-cell immobilization was a modified Luria-Bertani (LB) added with 3.0% (W/V) alginate, 1.5% (W/V) diatomite, 0.05% (W/V) CaCl2 and 1.00 mM MnCl2.The optimized diameter of immobilized beads for the whole-cell biosynthesis here was 2.60 mm. The maximized production rates of D-CpHPG were up to 76%, and the immobilized beads could be reused for 12 batches.Conclusions:
This investigation not only provides an effective procedure for biological production of D-CpHPG, but gives an insight into the whole-cell immobilization technology.Palabras clave
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Asunto principal:
Escherichia coli
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Amidohidrolasas
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Idioma:
En
Revista:
Electron. j. biotechnol
Asunto de la revista:
BIOTECNOLOGIA
Año:
2016
Tipo del documento:
Article