TY - JOUR
T1 - Spacer arm-facilitated tethering of laccase on magnetic polydopamine nanoparticles for efficient biocatalytic water treatment
AU - Chen, Chao
AU - Sun, Wen
AU - Lv, Hangya
AU - Li, Hui
AU - Wang, Yibing
AU - Wang, Ping
N1 - Publisher Copyright:
© 2018 Elsevier B.V.
PY - 2018/10/15
Y1 - 2018/10/15
N2 - Development of high performance biocatalysts generally seeks enhanced specific enzyme activities under intensified reaction conditions. This work reports a novel polydopamine fabricated Fe3O4 nanoparticles for incorporation with enzymes through the formation of flexible spacer arms using dialdehyde starch (DAS). It appeared that the biocompatible microenvironment and flexible tethering at the particle interface could effectively improve performance of the immobilized enzyme. In a test with laccase, such fabricated nanoparticles could reach enzyme loadings as high as 242 mg/g, while retained 69% specific enzyme activity. At the same time, the spacer arm-facilitated immobilization reduced the conformation changes with the control of interfacial action between enzyme and nanoparticles. Furthermore, the immobilized enzyme showed much improved stability against pH and thermal inactivation compared to free laccase. As a result, the immobilized laccase exhibited high degradation efficiency and reusability when tested for removal of 2,4-dichlorophenol and more contaminants from water. The results demonstrated a new strategy in fabricating nanomaterials using bio-based polymers for preparation of high performance biocatalysts.
AB - Development of high performance biocatalysts generally seeks enhanced specific enzyme activities under intensified reaction conditions. This work reports a novel polydopamine fabricated Fe3O4 nanoparticles for incorporation with enzymes through the formation of flexible spacer arms using dialdehyde starch (DAS). It appeared that the biocompatible microenvironment and flexible tethering at the particle interface could effectively improve performance of the immobilized enzyme. In a test with laccase, such fabricated nanoparticles could reach enzyme loadings as high as 242 mg/g, while retained 69% specific enzyme activity. At the same time, the spacer arm-facilitated immobilization reduced the conformation changes with the control of interfacial action between enzyme and nanoparticles. Furthermore, the immobilized enzyme showed much improved stability against pH and thermal inactivation compared to free laccase. As a result, the immobilized laccase exhibited high degradation efficiency and reusability when tested for removal of 2,4-dichlorophenol and more contaminants from water. The results demonstrated a new strategy in fabricating nanomaterials using bio-based polymers for preparation of high performance biocatalysts.
KW - Enzyme immobilization
KW - Laccase
KW - Magnetic nanoparticles
KW - Polydopamine (PDA)
KW - dialdehyde starch (DAS)
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U2 - 10.1016/j.cej.2018.06.008
DO - 10.1016/j.cej.2018.06.008
M3 - Article
AN - SCOPUS:85048384966
SN - 1385-8947
VL - 350
SP - 949
EP - 959
JO - Chemical Engineering Journal
JF - Chemical Engineering Journal
ER -