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LXYL-P1-2 immobilized on magnetic nanoparticles and its potential application in paclitaxel production
Zou, Sen; Chen, Tian-Jiao; Li, Dan-Yang; Fan, Shuai; Yang, Zhao-Yong; Zhu, Ping.
  • Zou, Sen; Chinese Academy of Medical Sciences & Peking Union Medical College. Institute of Medicinal Biotechnology. Key Laboratory of Biotechnology of Antibiotics. Beijing. CN
  • Chen, Tian-Jiao; Chinese Academy of Medical Sciences & Peking Union Medical College. Institute of Materia Medica. NHC Key Laboratory of Biosynthesis of Natural Products. Beijing. CN
  • Li, Dan-Yang; Chinese Academy of Medical Sciences & Peking Union Medical College. Institute of Medicinal Biotechnology. Key Laboratory of Biotechnology of Antibiotics. Beijing. CN
  • Fan, Shuai; Chinese Academy of Medical Sciences & Peking Union Medical College. Institute of Medicinal Biotechnology. Key Laboratory of Biotechnology of Antibiotics. Beijing. CN
  • Yang, Zhao-Yong; Chinese Academy of Medical Sciences & Peking Union Medical College. Institute of Medicinal Biotechnology. Key Laboratory of Biotechnology of Antibiotics. Beijing. CN
  • Zhu, Ping; Chinese Academy of Medical Sciences & Peking Union Medical College. Institute of Materia Medica. NHC Key Laboratory of Biosynthesis of Natural Products. Beijing. CN
Electron. j. biotechnol ; 50: 10-15, Mar. 2021. ilus, graf, tab
Article in English | LILACS | ID: biblio-1292308
ABSTRACT

BACKGROUND:

LXYL-P1-2 is the first reported glycoside hydrolase that can catalyze the transformation of 7-b-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT) by removing the D-xylosyl group at the C7 position. Successful synthesis of paclitaxel by one-pot method combining the LXYL-P1-2 and 10- deacetylbaccatin III-10-b-O-acetyltransferase (DBAT) using XDT as a precursor, making LXYL-P1-2 a highly promising enzyme for the industrial production of paclitaxel. The aim of this study was to investigate the catalytic potential of LXYL-P1-2 stabilized on magnetic nanoparticles, the surface of which was modified by Ni2+-immobilized cross-linked Fe3O4@Histidine.

RESULTS:

The diameter of matrix was 20­40 nm. The Km value of the immobilized LXYL-P1-2 catalyzing XDT (0.145 mM) was lower than that of the free enzyme (0.452 mM), and the kcat/Km value of immobilized enzyme (12.952 mM s 1 ) was higher than the free form (8.622 mM s 1 ). The immobilized form maintained 50% of its original activity after 15 cycles of reuse. In addition, the stability of immobilized LXYL-P1-2, maintained 84.67% of its initial activity, improved in comparison with free form after 30 d storage at 4 C.

CONCLUSIONS:

This investigation not only provides an effective procedure for biocatalytic production of DT, but also gives an insight into the application of magnetic material immobilization technology.
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Full text: Available Index: LILACS (Americas) Main subject: Paclitaxel / Glycoside Hydrolases Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2021 Type: Article Affiliation country: China Institution/Affiliation country: Chinese Academy of Medical Sciences & Peking Union Medical College/CN

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Full text: Available Index: LILACS (Americas) Main subject: Paclitaxel / Glycoside Hydrolases Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2021 Type: Article Affiliation country: China Institution/Affiliation country: Chinese Academy of Medical Sciences & Peking Union Medical College/CN