Abstract
As ethanol can be made from insoluble starches, liquefaction of tapioca using α-amylase immobilised on MCF-(9.2T-3D) silica is studied to observe characteristics of the process. The free a-amylase SQzyme BAP was immobilised on the support via adsorption. During immobilisation, temperature and and agitation speed showed low effects on the process, but pH of buffer solution affected the process highly. The optimum enzyme immobilisation occurred at the temperature of 50°C, pH 6 and speed of 60-100 rpm giving the immobilisation efficiency of more than 80%. Liquefaction of the insoluble starch (tapioca) was conducted with the immobilised α-amylase. The maximum result of ± 50% DE was obtained. The experimental factors of buffer pH, temperature and agitation speed changed the DE significantly, but concentration of immobilised enzyme and substrate affected the process lowly. The optimum pH, agitation speed, immobilised enzyme concentration and temperature were 6, 100 rpm, 84.8 U and 80°C, respectively.
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