Verma, M.L.; Chaudhary, R.; Tsuzuki, T.; Barrow, C.J.; Puri, M.
초록
The objective of the present work was to develop a thermostable β-glucosidase through immobilization on a nanoscale carrier for potential application in biofuel production. β-Glucosidase (BGL) from Aspergillus niger was immobilized to functionalized magnetic nanoparticles by covalent binding. Immobilized nanoparticles showed 93% immobilization binding. Immobilized and free BGL were characterized using Transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FTIR) techniques. Free and immobilized enzyme exhibited different pH-optima at pH 4.0 and 6.0, respectively, but had the same temperature optima at 60<SUP>o</SUP>C. Michaelis constant (K<SUB>M</SUB>) was 3.5 and 4.3mM for free and immobilized BGL. Thermal stability of the immobilized enzyme was enhanced at 70<SUP>o</SUP>C. The immobilized nanoparticle-enzyme conjugate retained more than 50% enzyme activity up to the 16th cycle. Maximum glucose synthesis from cellobiose hydrolysis by immobilized BGL was achieved at 16h.