TY - JOUR
T1 - Lipase immobilization on functionalized mesoporous TiO2
T2 - Specific adsorption, hyperactivation and application in cinnamyl acetate synthesis
AU - Gao, Zhen
AU - Chu, Jianlin
AU - Jiang, Tianyue
AU - Xu, Tingting
AU - Wu, Bin
AU - He, Bingfang
N1 - Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2018/1
Y1 - 2018/1
N2 - According to the purification characteristics of lipase from Burkholderia ambifaria YCJ01, mesoporous TiO2 was functionalized by phenylaminopropyl trimethoxysilane (Ph-TiO2) for lipase immobilization. This support permitted one step immobilization and purification of lipase YCJ01 via hydrophobic interactions from crude fermentation supernatant. The activity of immobilized lipase was 6119.2 U/g support with 12.8 mg/g support of enzyme loading. The ratio of the activity of immobilized lipase to decrease activity in the supernatant after immobilization reached 2.2, which indicated that the immobilized lipase molecules exhibited a dramatic hyperactivation. In comparison with free lipase, immobilized lipase showed significantly improved pH stability and thermalstability. The Ph-TiO2/YCJ01 biocomposite was analyzed by scanning electron microscopy, Fourier transform infrared spectroscopy and thermogravimetric analysis. The result indicated lipase was efficiently immobilized on Ph-TiO2 surface. Finally, the research about cinnamyl acetate synthesis suggested that Ph-TiO2/YCJ01 had enhanced catalytic efficiency compared with free lipase. In solvent free medium, the yield of 96.9% was obtained after one operation, and maintained more than 80% of yield after ten reaction cycles.
AB - According to the purification characteristics of lipase from Burkholderia ambifaria YCJ01, mesoporous TiO2 was functionalized by phenylaminopropyl trimethoxysilane (Ph-TiO2) for lipase immobilization. This support permitted one step immobilization and purification of lipase YCJ01 via hydrophobic interactions from crude fermentation supernatant. The activity of immobilized lipase was 6119.2 U/g support with 12.8 mg/g support of enzyme loading. The ratio of the activity of immobilized lipase to decrease activity in the supernatant after immobilization reached 2.2, which indicated that the immobilized lipase molecules exhibited a dramatic hyperactivation. In comparison with free lipase, immobilized lipase showed significantly improved pH stability and thermalstability. The Ph-TiO2/YCJ01 biocomposite was analyzed by scanning electron microscopy, Fourier transform infrared spectroscopy and thermogravimetric analysis. The result indicated lipase was efficiently immobilized on Ph-TiO2 surface. Finally, the research about cinnamyl acetate synthesis suggested that Ph-TiO2/YCJ01 had enhanced catalytic efficiency compared with free lipase. In solvent free medium, the yield of 96.9% was obtained after one operation, and maintained more than 80% of yield after ten reaction cycles.
KW - Cinnamyl acetate synthesis
KW - Lipase immobilization
KW - Mesoporous TiO
KW - Specific adsorption
KW - Surface modification
UR - http://www.scopus.com/inward/record.url?scp=85029546795&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2017.09.011
DO - 10.1016/j.procbio.2017.09.011
M3 - 文章
AN - SCOPUS:85029546795
SN - 1359-5113
VL - 64
SP - 152
EP - 159
JO - Process Biochemistry
JF - Process Biochemistry
ER -