文摘
Highly efficient raw starch digesting α-amylase was produced after 24 h of batch fermentation of Bacillus licheniformis ATCC 9945a in laboratory bioreactor at 37 °C. The enzyme was purified by gel filtration chromatographies with 6-fold increase of specific activity and 38 % recovery and showed a molecular mass of 31 kDa by SDS-PAGE. The purified enzyme had an optimum pH of 6.5 and optimum temperature of 90 °C. The purified α-amylase in the presence of CaCl2 retained 55 % of its activity after 6 h of incubation at 70 °C. Co2+, Ni2+ and Ca2+ slightly stimulated, while Hg2+ completely inhibited α-amylase activity. Hydrolysis rates of raw triticale, wheat, potato, horseradish and corn starches, at 1 % concentration were 63, 60, 59, 52 and 37 % , respectively, in a period of 4 h. The properties of the purified enzyme proved its high efficacy for digesting diverse raw starches below gelatinization temperature and, hence, its potential commercial value to use as an industrial enzyme.