期刊
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
卷 44, 期 6, 页码 558-571出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/10826068.2013.835732
关键词
alpha-amylase; genotoxicity; immobilization; SnO2-NPs; starch hydrolysis
类别
资金
- University Grants Commission, New Delhi, India
Immobilization of biologically important molecules on a myriad of nanosized materials has attracted great attention due to their small size, biocompatibility, higher surface-to-volume ratio, and lower toxicity. These properties make nanoparticles (NPs) a superior matrix over bulk material for the immobilization of enzymes and proteins. In the present study, Bacillus amyloliquefaciens -amylase was immobilized on SnO2 nanoparticles by a simple adsorption mechanism. Nanoparticle-adsorbed enzyme retained 90% of the original enzyme activity. Thermal stability of nanosupport was investigated by thermogravimetric and differential thermal analysis. Scanning electron microscopic studies showed that NPs have porous structure for the high-yield immobilization of -amylase. The genotoxicity of SnO2-NPs was analyzed by pUC(19) plasmid nicking and comet assay and revealed that no remarkable DNA damage occurred in lymphocytes. The pH-optima was found to be the same for both free and SnO2-NPs bound enzyme, while the temperature-optimum for NPs-adsorbed -amylase was 5 degrees C higher than its free counterpart. Immobilized enzyme retained more than 70% enzyme activity even after its eight repeated uses.
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