Glucoamylase is an enzyme that hydrolyses 1,4α and 1,6β-glucosidic linkages in polysaccharides yielding glucose. Aspergillus niger strains 1, 2 and 3 were locally isolated from cassava peel dumpsite for the production of glucoamylase enzyme. A. niger strains 1, 2 and 3 were screened for their hyper producing ability on potato dextrose agar using plate assay method fortified with starch agar, and showed zone of clearance of 17.0, 23.0 and 8.0 mm, respectively. The glucoamylase activity for A. niger strains 1 and 2 were 13 000.0 and 11 740.0, respectively. These values were however higher than the activity as obtained from the commercial enzyme with 2 500.0. Investigations on the protein (mg/ml), and specific activity (units/mg) on glucoamylase produced by A. niger strains 1 and 2 was 24.20, 537.19, 23.13 and 507.57, respectively. Fractionation of the enzyme ammonium sulphate (% w/v) using 60, 80 and 100% showed that the enzyme activities were 33 179.86, 47 985.86 and 19 167.65 units/ml, respectively. Protein concentrations were 16.29, 16.29 and 21.55 units/mg, respectively, while specific activities were 2 036.82, 2 945.725 and 889.45 units/mg, respectively. The production, packaging, and commercialization of glucoamylase in Nigeria will save a lot of foreign exchange earnings, and boost the economy of Nigeria.
Microbial alkaline protease is one of the dominant industrial enzymes which function in splitting polypeptides chain of protein into monomers of amino acids and peptides. This study aimed to identify alkaline protease produced by Bacillus sp. Soil samples were aseptically collected from dump sites in FIIRO, Lagos state, Nigeria. The samples were serially diluted, and bacteria were isolated using pour plate method. The resulting isolates were screened and morphologically characterized. The isolate with the highest protease production potential was subjected to biochemical characterization using Analytical Profile Index (API) identification kit system and 16S rRNA sequencing. The selected isolate was used to produce alkaline protease by solid state fermentation using rice bran as a substrate. Out of the 18 bacteria isolated, 11 isolates showed alkaline protease production potential. Isolate C3a-FIIRO was selected for its maximal alkaline protease produced as indicated by a 56 mm zone of clearance. Morphological and biochemical characterization revealed isolate C3a-FIIRO as a member of the genus Bacillus. The 16S rRNA gene sequencing confirmed the isolate as Bacillus subtilis C3a-FIIRO (MW577298) with closest homology to Bacillus subtilis Y17B. The enzyme activity of 6848.171 U/ml ± 0.11 and protein concentration of 152.13 mg/ml ± 0.003 showed that Bacillus subtilis C3a-FIIRO has potential for sustainable alkaline protease production.
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