The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis
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 enha...
Guardado en:
| Autores principales: | , , , , , , , |
|---|---|
| Lenguaje: | English |
| Publicado: |
Pontificia Universidad Católica de Valparaíso
2016
|
| Materias: | |
| Acceso en línea: | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300004 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:scielo:S0717-34582016000300004 |
|---|---|
| record_format |
dspace |
| spelling |
oai:scielo:S0717-345820160003000042016-07-06The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesisJin,Yuan-yuanLi,Ya-dongSun,WanFan,ShuaiFeng,Xiao-zhouWang,Kang-youHe,Wei-qingYang,Zhao-yong Calcium alginate d-Carbamoyl-p-hydroxyphenylglycine d-Hydantoinase d-Hydroxyphenylglycine Immobilization Whole cell 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.19 n.3 20162016-05-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300004en10.1016/j.ejbt.2016.01.004 |
| institution |
Scielo Chile |
| collection |
Scielo Chile |
| language |
English |
| topic |
Calcium alginate d-Carbamoyl-p-hydroxyphenylglycine d-Hydantoinase d-Hydroxyphenylglycine Immobilization Whole cell |
| spellingShingle |
Calcium alginate d-Carbamoyl-p-hydroxyphenylglycine d-Hydantoinase d-Hydroxyphenylglycine Immobilization Whole cell Jin,Yuan-yuan Li,Ya-dong Sun,Wan Fan,Shuai Feng,Xiao-zhou Wang,Kang-you He,Wei-qing Yang,Zhao-yong The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis |
| description |
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. |
| author |
Jin,Yuan-yuan Li,Ya-dong Sun,Wan Fan,Shuai Feng,Xiao-zhou Wang,Kang-you He,Wei-qing Yang,Zhao-yong |
| author_facet |
Jin,Yuan-yuan Li,Ya-dong Sun,Wan Fan,Shuai Feng,Xiao-zhou Wang,Kang-you He,Wei-qing Yang,Zhao-yong |
| author_sort |
Jin,Yuan-yuan |
| title |
The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis |
| title_short |
The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis |
| title_full |
The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis |
| title_fullStr |
The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis |
| title_full_unstemmed |
The whole-cell immobilization of D-hydantoinase-engineered Escherichia coli for D-CpHPG biosynthesis |
| title_sort |
whole-cell immobilization of d-hydantoinase-engineered escherichia coli for d-cphpg biosynthesis |
| publisher |
Pontificia Universidad Católica de Valparaíso |
| publishDate |
2016 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300004 |
| work_keys_str_mv |
AT jinyuanyuan thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT liyadong thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT sunwan thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT fanshuai thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT fengxiaozhou thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT wangkangyou thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT heweiqing thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT yangzhaoyong thewholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT jinyuanyuan wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT liyadong wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT sunwan wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT fanshuai wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT fengxiaozhou wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT wangkangyou wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT heweiqing wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis AT yangzhaoyong wholecellimmobilizationofdhydantoinaseengineeredescherichiacolifordcphpgbiosynthesis |
| _version_ |
1718441927634845696 |