Characterizations of two α-amylases from different sources
學 期: 111上
摘 要: Microbial α-amylases have a broad spectrum of industrial applications as they are more stable than plant and animal α-amylases, and they have broad biochemical diversity, feasibility of mass culture and ease of genetic manipulation (Chakrabortya et al., 2009). In this study, two α-amylases from different sources were investigated. First α-amylase was produced by Bacillus amyloliquefaciens BH072 and second α-amylase was produced by Bacillus lichenformis (JQ946317). The optimum temperature and pH for the purified BH072 α-amylase were 60°C and pH 7, respectively. The enzyme also showed high activity over a wide range of temperatures (50-80°C) and pH values (6.0-8.0). The activity of the α-amylase was Ca2+ independent and stable in the presence of surfactant, oxidizing and bleaching agents. Purified JQ946317 α-amylase exhibited maximum activity at pH 7.0, performed stable over a broad range of pH 6–8 and was optimally active at 35°C. The produced enzyme activity was highest at 48 hours of incubation under solid state fermentation. These findings suggest that the α amylase produced by Bacillus amyloliquefaciens BH072 and Bacillus lichenformis (JQ946317) would be a potent tool for the industrial applications.