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J M Araújo

Publications and source records attributed to J M Araújo.

4 recordsLinked to original sources

Production and characterization of a thermostable glucoamylase from Streptosporangium sp. endophyte of maize leaves.

Thermostable amylolytic enzymes are currently investigated to improve industrial processes of starch degradation. Streptosporangium sp. an endophytic actinomycete isolated from leaves of maize (Zea mays L.) showed glucoamylase production, using starch-Czapek medium, and the highest rate was obtained in the initial growth phase, after incubation for 24 h at pH 8.0. Maximum glucoamylase activity (158 U mg(-1) protein) was obtained at pH 4.5 and 70 degrees C. The isolated enzyme exhibited thermostable properties as indicated by retention of 100% of residual activity at 70 degrees C for 30 min with total inhibition at 100 degrees C. Extracellular enzyme from Streptosporangium sp. was purified by fractionated precipitation with ammonium sulphate. After 60% saturation produced 421 U mg(-1) protein, and yield was 74% with purification 2.7 fold. The enzyme produced by Streptosporangium sp. has potential for industrial applications.

Actinomycetales↗

Production and characterization of a thermostable alpha-amylase from Nocardiopsis sp. endophyte of yam bean.

Thermostable amylolytic enzymes have been currently investigated to improve industrial processes of starch degradation. Studies on production of alpha-amylase by Nocardiopsis sp., an endophytic actinomycete isolated from yam bean (Pachyrhizus erosus L. Urban), showed that higher enzyme levels were obtained at the end of the logarithmic growth phase after incubation for 72 h at pH 8.6. Maximum activity of alpha-amylase was obtained at pH 5.0 and 70 degrees C. The isolated enzyme exhibited thermostable properties as indicated by retention of 100% of residual activity at 70 degrees C, and 50% of residual activity at 90 degrees C for 10 min. Extracellular enzyme from Nocardiopsis sp. was purified by fractional precipitation with ammonium sulphate. After 60% saturation produced 1130 U mg-1 protein and yield was 28% with purification 2.7-fold. The enzyme produced by Nocardiopsis sp. has potential for industrial applications.

Actinomycetales↗