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Anthrin, R.L., Solheim, B.A., Solheim, L., Autherinen, A.L., Ginefare, J. and Karppelin, S. (1990) A New Bacillus licheniformis Alpha Amylase Capable of Low pH Liquefaction. Starch/Starke, 43, 355-360.

has been cited by the following article:

• TITLE: Characterization of Amylase from Some Aspergillus and Bacillus Species Associated with Cassava Waste Peels

  AUTHORS: Ayantade Dayo Victor Ayansina, Ademola Olasoji Adelaja, Sani Sambo Datsugwai Mohammed

  KEYWORDS: Amylase, Bacillus, Aspegillus, Enzyme Activity

  JOURNAL NAME: Advances in Microbiology, Vol.7 No.4, April 26, 2017

  ABSTRACT: Cassava peels are generated as waste on soils during cassava processing in many tropical countries. This work set out to isolate some microorganisms associated with cassava peel degradation and characterize amylase enzymes responsible for the degradation under some physiological conditions. A total of 30 bacteria was isolated from the peels with Bacillus species occurring the most (46.5%) and Enterobacter species (13.3%) being the next. Frequencies of fungal isolations was Rhizopus sp. (35%); Aspergillus niger (25%); Aspegillus flavus (20%) and Penicillium species (20%). Bacillus cereus, Bacillus substilis Bacillus pumillus, Aspergillus niger and Apergillus flavus were selected and screened for their abilities to produce amylase. Amylase activity was highest at day 4 for B. substilis (39.4 units/ml) and A. flavus (66.1 units/ml); at day 3 for B. cereus (55.6 units/ml) and A. niger (44.6 units/ ml). While maximum amylase activity was obtained at day 6 for B. pumilus (80.2 units/ml). Optimum pH for amylases from the two fungal isolate was 6.0 (A. niger = 53.5 units/ml and A. flavus = 65.4 units/ml). While optimum pH for B.cereus (51.7 units/ ml) and B. pumilus (44.6 units/ml) was 6.5 and for B. substilis (56.1 units/ml) at pH 7.0. Amylase activities increased from 20°C to 40°C for amylase from Bacillus sp. and 20°C to 50°C for amylase from the Aspergillus sp. after which there was a decline in activities as temperature increased to 80°C. Effect of heating duration (at 70°C for 5 minutes) on the amylase showed that A. niger has the highest activity of 127 units/ml. Effect of substrate concentration on amylase activity showed that amylase form A. flavus had the highest activity of 72.2 units/ml at 0.4% substrate concentration. The implications of the findings were discussed.