TY - JOUR
T1 - Step-Up Synthesis of Periodic Mesoporous Organosilicas with a Tyrosine Framework and Performance in Horseradish Peroxidase Immobilization
AU - Wang, Jianqiang
AU - Zhang, Wenqi
AU - Gu, Changqing
AU - Zhang, Wenpei
AU - Zhou, Man
AU - Wang, Zhiwei
AU - Guo, Cheng
AU - Sun, Linbing
N1 - Publisher Copyright:
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
PY - 2017/12/14
Y1 - 2017/12/14
N2 - New amino-acid-bridged periodic mesoporous organosilicas (PMOs) were constructed by hydrolysis and condensation reactions under acid conditions in the presence of a template. The tyrosine bissilylated organic precursor (TBOS) was first prepared through a multistep reaction by using tyrosine (a natural amino acid) as the starting material. PMOs with the tyrosine framework (Tyr-PMOs) were constructed by simultaneously using TBOS and tetraethoxysilane as complex silicon sources in the condensation process. All the Tyr-PMOs materials were characterized by XRD, FTIR spectroscopy, N2 adsorption–desorption, TEM, SEM, and solid-state 29Si NMR spectroscopy to confirm the structure. The horseradish peroxidase (HRP) enzyme was first immobilized on these new Tyr-PMOs materials. Optimal conditions for enzyme adsorption included a temperature of 40 °C, a time of 8 h, and a pH value of 7. Furthermore, the novel Tyr-PMOs materials could store HRP for approximately 40 days and maintained the enzymatic activity, and the Tyr-PMOs–10 % HRP with the best immobilization effect could be reused at least eight times.
AB - New amino-acid-bridged periodic mesoporous organosilicas (PMOs) were constructed by hydrolysis and condensation reactions under acid conditions in the presence of a template. The tyrosine bissilylated organic precursor (TBOS) was first prepared through a multistep reaction by using tyrosine (a natural amino acid) as the starting material. PMOs with the tyrosine framework (Tyr-PMOs) were constructed by simultaneously using TBOS and tetraethoxysilane as complex silicon sources in the condensation process. All the Tyr-PMOs materials were characterized by XRD, FTIR spectroscopy, N2 adsorption–desorption, TEM, SEM, and solid-state 29Si NMR spectroscopy to confirm the structure. The horseradish peroxidase (HRP) enzyme was first immobilized on these new Tyr-PMOs materials. Optimal conditions for enzyme adsorption included a temperature of 40 °C, a time of 8 h, and a pH value of 7. Furthermore, the novel Tyr-PMOs materials could store HRP for approximately 40 days and maintained the enzymatic activity, and the Tyr-PMOs–10 % HRP with the best immobilization effect could be reused at least eight times.
KW - amino acids
KW - immobilization
KW - mesoporous materials
KW - organosilicas
KW - tyrosine-bridged organosilicas
UR - http://www.scopus.com/inward/record.url?scp=85034100800&partnerID=8YFLogxK
U2 - 10.1002/asia.201701285
DO - 10.1002/asia.201701285
M3 - 文章
C2 - 29045027
AN - SCOPUS:85034100800
SN - 1861-4728
VL - 12
SP - 3162
EP - 3171
JO - Chemistry - An Asian Journal
JF - Chemistry - An Asian Journal
IS - 24
ER -