Please use this identifier to cite or link to this item: http://ir.futminna.edu.ng:8080/jspui/handle/123456789/6879
Title: Production of protease and amylase from Bacillus subtilis and Aspergillus niger using Parkia biglobossa (Africa Locust Beans) as substrate in solid state fermentation
Authors: Oyeleke, Solomon Bankole
Oyewole, Oluwafemi Adebayo
Egwim, Evans Chidi
Keywords: Bacillus subtilis
Aspergillus niger
Amylase
Parkia biglobossa
Protease
Issue Date: 2011
Publisher: Advances in Life Sciences
Citation: Oyeleke S.B., Oyewole O.A. & Egwim, E.C. (2011). Production of protease and amylase from Bacillus subtilis and Aspergillus niger using Parkia biglobossa (Africa Locust Beans) as substrate in solid state fermentation, Advances in Life Sciences, 1(2), 49-53.
Abstract: Bacillus subtilis and Aspergillus niger were utilized for the production of amylase and protease enzymes in this study. Parkia biglobossa (Africa Locust Beans) shell was used as substrate by both organisms for the production of amylase and protease enzyme. The optimum temperature for the activity of amylase and protease enzymes produced by Bacillus subtilis was 50oC, while 30oC and 40oC was recorded for amylase and protease enzyme produced by Aspergillus niger with an activity of 1.1 mg/ml/sec, 0.8 mg/ml/sec for amylase and protease enzyme by Bacillus subtilis and 0.87 mg/ml/sec, 0.77 mg/ml/sec for amylase and protease produced by Aspergillus niger respectively. Optimum pH was attained at pH 9 for amylase and protease enzyme produced by Bacillus subtilis with an activity of 1.2 mg/ml/sec and 0.83 mg/ml/sec respec-tively. The optimum pH for the activity of Aspergillus niger was recorded at pH 5 and pH 6 for amylase and protease with an activity of 0.87 mg/ml/sec and 0.74mg/ml/sec respectively. The result showed that both organisms utilized Parkia biglobossa to produce extracellular amylase and protease, but the activity of amylase enzyme produced by both organisms was greater than the activity of protease enzyme and enzymes produced by Bacillus subtilis showed superior activity which can be useful industrially.
URI: http://repository.futminna.edu.ng:8080/jspui/handle/123456789/6879
Appears in Collections:Microbiology



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