Poly-3-hydroxyalkanoates (PHAs) are biopolymers accumulated as intracellular energy reserves by bacteria under nutrient limiting growth conditions and suitable for plastic production. We report findings from the use of a bacterium isolated from a cassava dumpsite for PHAs production. Isolate C113 was screened for PHAs production using the viable colony and Sudan Black B staining methods and further identified by 16SrRNA sequencing. Its PHA synthase gene, PhaR, was also partially amplified and sequenced. PHAs production was achieved over 96-hour incubation, extracted by NaClO/chloroform method and analysed by FT-IR. Isolate C113 was positive for PHA production in all carbon sources and was identified as a strain of Bacillus cereus. It showed highest biomass accumulation in glucose and starch. It achieved PHAs production of 4.85 % dry cell weight (DCW) in glucose, 33.03 %DCW in glycerol and 6.05 %DCW in sugarcane molasses at 24 hours while 10.58 %DCW was produced in starch at 96 hours. FT-IR spectra showed peaks corresponding to P3HB and P3HB3HV and reveal conformational changes of mcl-PHA and scl-PHA in crystalline and amorphous phases. The 16SrRNA (KY855372.1) and PhaR (MF947451.1) sequences have been accessioned in NCBI-GenBank. The results show that Bacillus cereus C113 demonstrated capacity to utilize a variety of carbon sources for PHAs production.

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.