TY - JOUR
T1 - A general strategy for site-directed enzyme immobilization by using NiO nanoparticle decorated mesoporous silica
AU - Ling, Daishun
AU - Gao, Liqian
AU - Wang, Jianpeng
AU - Shokouhimehr, Mohammadreza
AU - Liu, Jiahui
AU - Yu, Yongsheng
AU - Hackett, Michael J.
AU - So, Pui Kin
AU - Zheng, Bo
AU - Yao, Zhongping
AU - Xia, Jiang
AU - Hyeon, Taeghwan
PY - 2014/6/23
Y1 - 2014/6/23
N2 - Mesoporous materials have recently gained much attention owing to their large surface area, narrow pore size distribution, and superior pore structure. These materials have been demonstrated as excellent solid supports for immobilization of a variety of proteins and enzymes for their potential applications as biocatalysts in the chemical and pharmaceutical industries. However, the lack of efficient and reproducible methods for immobilization has limited the activity and recyclability of these biocatalysts. Furthermore, the biocatalysts are usually not robust owing to their rapid denaturation in bulk solvents. To solve these problems, we designed a novel hybrid material system, mesoporous silica immobilized with NiO nanoparticles (SBA-NiO), wherein enzyme immobilization is directed to specific sites on the pore surface of the material. This yielded the biocatalytic species with higher activity than free enzyme in solution. These biocatalytic species are recyclable with minimal loss of activity after several cycles, demonstrating an advantage over free enzymes. Site-directed enzyme immobilization onto the pore surface of NiO nanoparticle decorated mesoporous silica (SBA) leads to a species with higher activity than the free enzyme in solution (see figure). These biocatalysts are recyclable with minimal loss of activity after five cycles, demonstrating an advantage over free enzymes. KGaA, Weinheim.
AB - Mesoporous materials have recently gained much attention owing to their large surface area, narrow pore size distribution, and superior pore structure. These materials have been demonstrated as excellent solid supports for immobilization of a variety of proteins and enzymes for their potential applications as biocatalysts in the chemical and pharmaceutical industries. However, the lack of efficient and reproducible methods for immobilization has limited the activity and recyclability of these biocatalysts. Furthermore, the biocatalysts are usually not robust owing to their rapid denaturation in bulk solvents. To solve these problems, we designed a novel hybrid material system, mesoporous silica immobilized with NiO nanoparticles (SBA-NiO), wherein enzyme immobilization is directed to specific sites on the pore surface of the material. This yielded the biocatalytic species with higher activity than free enzyme in solution. These biocatalytic species are recyclable with minimal loss of activity after several cycles, demonstrating an advantage over free enzymes. Site-directed enzyme immobilization onto the pore surface of NiO nanoparticle decorated mesoporous silica (SBA) leads to a species with higher activity than the free enzyme in solution (see figure). These biocatalysts are recyclable with minimal loss of activity after five cycles, demonstrating an advantage over free enzymes. KGaA, Weinheim.
KW - enzyme catalysis
KW - immobilization
KW - mesoporous materials
KW - nanoparticles
KW - proteins
UR - http://www.scopus.com/inward/record.url?scp=84902980198&partnerID=8YFLogxK
U2 - 10.1002/chem.201403071
DO - 10.1002/chem.201403071
M3 - Journal article
C2 - 25212493
SN - 0947-6539
VL - 20
SP - 7916
EP - 7921
JO - Chemistry - A European Journal
JF - Chemistry - A European Journal
IS - 26
ER -