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dc.creatorJin,Yuan-yuan
dc.creatorLi,Ya-dong
dc.creatorSun,Wan
dc.creatorFan,Shuai
dc.creatorFeng,Xiao-zhou
dc.creatorWang,Kang-you
dc.creatorHe,Wei-qing
dc.creatorYang,Zhao-yong
dc.date2016-05-01
dc.date.accessioned2019-05-03T12:45:24Z
dc.date.available2019-05-03T12:45:24Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300004
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/85542
dc.descriptionBackground: 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.
dc.formattext/html
dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.relation10.1016/j.ejbt.2016.01.004
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.19 n.3 2016
dc.subjectCalcium alginate
dc.subjectd-Carbamoyl-p-hydroxyphenylglycine
dc.subjectd-Hydantoinase
dc.subjectd-Hydroxyphenylglycine
dc.subjectImmobilization
dc.subjectWhole cell
dc.titleThe whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis


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