摘要
A lipase from Rhizopus delemar (RhDL) was adsorbed on two tin dioxides with different textural characteristics (nanoSnO(2)-A-RhD and nanoSnO(2)-B-RhD). All biochemical characteristics obtained for them were compared with those for RhDL on silica. NanoSnO(2)-A exhibited the highest protein loading capacity (75%), however, the highest specific activity was measured for nanoSnO(2)-B-RhD (33.8 U/mg prot.). The immobilization enhanced thermal-, pH- and solvent stability of RhDL For example, nanoSnO(2)-A-RhD is still fully active after one-hour heating at 60 degrees C and preserved 70% of its activity at pH 9. When applied in the isoamyl acetate synthesis, a complete conversion of substrates was obtained with nanoSnO(2)-A-RhD in hexane and SBA-15-RhD in hexadecane for 12 h. The performance of the three biocatalysts in several consecutive cycles was estimated as well.
- 出版日期2011-11-30