DICP OpenIR
Subject Area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)
Source PublicationLANGMUIR
2012-06-26
DOI10.1021/la301330s
Volume28Issue:25Pages:9788-9796
Indexed BySCI
SubtypeArticle
Department5
Funding Project506;503
Contribution Rank1,1
WOS HeadingsScience & Technology ; Physical Sciences ; Technology
WOS SubjectChemistry, Multidisciplinary ; Chemistry, Physical ; Materials Science, Multidisciplinary
WOS Research AreaChemistry ; Materials Science
WOS KeywordRHIZOMUCOR-MIEHEI LIPASE ; SOL-GEL MATERIALS ; LYSOZYME ADSORPTION ; INTERFACIAL ADSORPTION ; HYDROPHOBIC SUPPORTS ; IMMOBILIZATION ; ENZYMES ; HYPERACTIVATION ; BIOCATALYSIS
AbstractThe 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.
Language英语
WOS IDWOS:000305661400073
Citation statistics
Cited Times:36[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/118384
Collection中国科学院大连化学物理研究所
Corresponding AuthorYang QH(杨启华); Li C(李灿)
Affiliation1.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
Recommended Citation
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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