Purification and Properties of Saccharogenic Amylase from Piricularia oryzae

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Abstract
Piricularia oryzae, the pathogenic fungus of rice blast disease, produced a glucoamylase as a sole amylolytic enzyme with little concomitant activity of other related enzymes. The purified enzyme preparation showed a single band on electrophoresis. The enzyme had optimum pH at 6.5 and optimum temperature between 50 and 55°C. It was completely inactivated by heating for 15 min at 60°C. The molecular weight of the enzyme was estimated as about 94,000. The enzyme hydrolyzed various kinds of amylaceous substrates and some malto‐oligosaccharides into glucose. Glucobioses such as isomaltose, nigerose, kojibiose, α,α‐trehalose, β,β‐trehalose as well as phenyl‐α‐glucoside were also hydrolyzed.