DICP OpenIR
学科主题物理化学
Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment
Liu, Jia1,2; Bai, Shiyang1,2; Jin, Qianru1,2; Zhong, Hua1; Li, Can1; Yang, Qihua1; Yang QH(杨启华); Li C(李灿)
刊名LANGMUIR
2012-06-26
DOI10.1021/la301330s
28期:25页:9788-9796
收录类别SCI
文章类型Article
部门归属5
项目归属506;503
产权排名1,1
WOS标题词Science & Technology ; Physical Sciences ; Technology
类目[WOS]Chemistry, Multidisciplinary ; Chemistry, Physical ; Materials Science, Multidisciplinary
研究领域[WOS]Chemistry ; Materials Science
关键词[WOS]RHIZOMUCOR-MIEHEI LIPASE ; SOL-GEL MATERIALS ; LYSOZYME ADSORPTION ; INTERFACIAL ADSORPTION ; HYDROPHOBIC SUPPORTS ; IMMOBILIZATION ; ENZYMES ; HYPERACTIVATION ; BIOCATALYSIS
英文摘要The highly ordered mesoporous silicas with elaborately controlled microenvironment were synthesized via covalent incorporation of long-chain polymers (M-w = 2000 g mol(-1)) bearing specific hydrophilic/hydrophobic balance. The microenvironment (hydrophilicity/hydrophobicity) of the mesoporous silicas was quantitatively determined by gas adsorption experiments and investigated by lysozyme (LYZ) adsorption. The relative activity of lipase from Pseudomonas cepacia (PCL) encapsulated in the mesoporous silica with moderate hydrophobic microenvironment (hereafter denoted as MHM) reaches up to 281% compared with the free PCL, notably higher than that of PCL accommodated in the mesoporous silicas with hydrophilic or strong hydrophobic microenvironment (20.7-26.2% relative to the free PCL). Moreover, PCL entrapped in the nanochannels with MHM affords the highest initial rate in the kinetic resolution of (R,S)-1-phenylethanol relative to other immobilized PCL. The above results suggest that the MHM could render the active center of PCL entirely exposed to the substrates without interrupting its native conformation in the "interfacial activation". In addition, the nano channels with MHM could markedly improve the thermal stability of PCL (preserving nearly 60% of the initial activity after the incubation at 70 degrees C for 2 h) and facilitate the recycling of the immobilized PCL in both aqueous and organic media. Our work demonstrates that the subtle modulation of the microenvironment of mesoporous silicas for enzyme immobilization designates a very promising strategy to fabricate the highly active and stable heterogeneous biocatalysts for industrial application.
语种英语
WOS记录号WOS:000305661400073
引用统计
被引频次:30[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/118384
专题中国科学院大连化学物理研究所
通讯作者Yang QH(杨启华); Li C(李灿)
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Catalysis, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714
Liu, Jia,Bai, Shiyang,Jin, Qianru,et al. Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment[J]. LANGMUIR,2012,28(25):9788-9796.
APA Liu, Jia.,Bai, Shiyang.,Jin, Qianru.,Zhong, Hua.,Li, Can.,...&李灿.(2012).Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment.LANGMUIR,28(25),9788-9796.
MLA Liu, Jia,et al."Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment".LANGMUIR 28.25(2012):9788-9796.
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