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Provedor de dados:  Electron. J. Biotechnol.
País:  Chile
Título:  The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis
Autores:  Jin,Yuan-yuan
Li,Ya-dong
Sun,Wan
Fan,Shuai
Feng,Xiao-zhou
Wang,Kang-you
He,Wei-qing
Yang,Zhao-yong
Data:  2016-05-01
Ano:  2016
Palavras-chave:  Calcium alginate
D-Carbamoyl-p-hydroxyphenylglycine
D-Hydantoinase
D-Hydroxyphenylglycine
Immobilization
Whole cell
Resumo:  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.
Tipo:  Journal article
Idioma:  Inglês
Identificador:  http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300004
Editor:  Pontificia Universidad Católica de Valparaíso
Formato:  text/html
Fonte:  Electronic Journal of Biotechnology v.19 n.3 2016
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