PMID- 34622894 OWN - NLM STAT- MEDLINE DCOM- 20220203 LR - 20220203 IS - 1477-9234 (Electronic) IS - 1477-9226 (Linking) VI - 50 IP - 42 DP - 2021 Nov 2 TI - A POM-based copper-coordination polymer crystal material for phenolic compound degradation by immobilizing horseradish peroxidase. PG - 15198-15209 LID - 10.1039/d1dt02644e [doi] AB - A new polyoxometalate (POM)-based organic-inorganic hybrid Cu-coordination polymer, namely ((Cu(bipy))(2)(mu-PhPO(3))(2)Cu(bipy))(2)H(PCuW(11)O(39)).3H(2)O(n) (denoted as compound 1, bipy = 2,2'-bipyridine, PhPO(3) = phenylphosphonate), was self-assembled hydrothermally. Single-crystal X-ray diffraction (SC-XRD) analysis shows that two unique types of 1D chains are present in compound 1, i.e. Cu(II)-organophosphine and organonitrogen complex cation ([((Cu(bipy))(2)(mu-PhPO(3))(2)Cu(bipy))(2)](4+)) chains and Cu-monosubstituted Keggin-type polyoxoanion ([PCuW(11)O(39)](5-)) chains, forming a hetero-POM. Crystalline compound 1 as a new enzyme immobilization support exhibited a high horseradish peroxidase (HRP) loading capacity (268 mg g(-1)). The powder X-ray diffraction (PXRD), FTIR, zeta potential, confocal laser scanning microscopy (CLSM) and circular dichroism (CD) results show that HRP is only immobilized on the surface of compound 1 through simple physical adsorption without a secondary structure change. This POM-immobilized enzyme (HRP/1) was first used for degradation of pollutants in wastewater, and it showed a high degradation efficiency and TOC removal efficiency for phenol, 4-chlorophenol (4-CP) and 2,4-dichlorophenol (2,4-DCP) within 30 min reaction time. Moreover, HRP/1 exhibited better operational and storage stabilities and reusability compared with free HRP. This work suggests that POMs can be used as new supports for enzyme immobilization and POM-immobilized enzymes may be used as a new kind of biocatalyst for degradation of phenolic pollutants. FAU - Lu, Ying AU - Lu Y AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. FAU - Zhang, Tong AU - Zhang T AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. FAU - Zhang, Yue-Xian AU - Zhang YX AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. FAU - Sang, Xiao-Jing AU - Sang XJ AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. FAU - Su, Fang AU - Su F AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. FAU - Zhu, Zai-Ming AU - Zhu ZM AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. FAU - Zhang, Lan-Cui AU - Zhang LC AUID- ORCID: 0000-0001-6352-9292 AD - School of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian, 116029, P.R. China. sufang031@lnnu.edu.cn. LA - eng PT - Journal Article DEP - 20211102 PL - England TA - Dalton Trans JT - Dalton transactions (Cambridge, England : 2003) JID - 101176026 RN - EC 1.11.1.- (Horseradish Peroxidase) SB - IM MH - *Horseradish Peroxidase EDAT- 2021/10/09 06:00 MHDA- 2022/02/04 06:00 CRDT- 2021/10/08 08:45 PHST- 2021/10/09 06:00 [pubmed] PHST- 2022/02/04 06:00 [medline] PHST- 2021/10/08 08:45 [entrez] AID - 10.1039/d1dt02644e [doi] PST - epublish SO - Dalton Trans. 2021 Nov 2;50(42):15198-15209. doi: 10.1039/d1dt02644e.