TY - JOUR
T1 - Influence of silica-derived nano-supporters on cellobiase after immobilization
AU - Wang, Peng
AU - Hu, Xiaoke
AU - Cook, Sean
AU - Hwang, Huey Min
N1 - Funding Information:
Acknowledgements The research is supported by: (1) the Department of Energy (DOE-MAT-SBI Program), grant number DE-FG36-05G085002 with subcontract #07-08-001 to Jackson State University (JSU) from University of Mississippi (P.I. Dr. Clint Williford), via management of Mr. Sumesh Arora of Mississippi Technology Alliance; (2) U.S. Department of the Army Research and Development grant # W912H2-04-2-0002 to JSU.
PY - 2009/7
Y1 - 2009/7
N2 - Core shell magnetite nanoparticle (CSMN) was successfully synthesized with diameter around 125 nm according to the determination with scanning electronic microscopy. SBA-15 with diameter around 31 nm was synthesized in our previous work as another supporter for immobilized degradation enzymes. The aim of this study was to investigate the influence of silica-derived nano-supporters on cellobiase after immobilization. With covalent method, glutaraldehyde was introduced to immobilize cellobiase. The immobilized enzyme efficiency, specific activity, and its characterization, including optimum pH, pH stability, optimum temperature for enzyme reaction, and enzyme thermal stability were investigated. Results show that the method of enzyme immobilization on both nano-supporters could improve cellobiase stability under low pH and high temperature conditions compared with the free enzyme. In the aspect of immobilization efficiency, SBA had higher amount of bounded protein than that of CSMN, but had lower specific enzyme activity than CSMN, assumably due to the change in silica surface properties caused by process of supporter synthesis.
AB - Core shell magnetite nanoparticle (CSMN) was successfully synthesized with diameter around 125 nm according to the determination with scanning electronic microscopy. SBA-15 with diameter around 31 nm was synthesized in our previous work as another supporter for immobilized degradation enzymes. The aim of this study was to investigate the influence of silica-derived nano-supporters on cellobiase after immobilization. With covalent method, glutaraldehyde was introduced to immobilize cellobiase. The immobilized enzyme efficiency, specific activity, and its characterization, including optimum pH, pH stability, optimum temperature for enzyme reaction, and enzyme thermal stability were investigated. Results show that the method of enzyme immobilization on both nano-supporters could improve cellobiase stability under low pH and high temperature conditions compared with the free enzyme. In the aspect of immobilization efficiency, SBA had higher amount of bounded protein than that of CSMN, but had lower specific enzyme activity than CSMN, assumably due to the change in silica surface properties caused by process of supporter synthesis.
KW - Cellobiase
KW - Core shell magnetite nanoparticle
KW - Immobilization
KW - SBA
UR - https://www.scopus.com/pages/publications/70349573908
U2 - 10.1007/s12010-008-8321-1
DO - 10.1007/s12010-008-8321-1
M3 - Article
C2 - 18679593
AN - SCOPUS:70349573908
SN - 0273-2289
VL - 158
SP - 88
EP - 96
JO - Applied Biochemistry and Biotechnology
JF - Applied Biochemistry and Biotechnology
IS - 1
ER -