Characterization and Enzymatic Potential of Bacteria and Fungi From Mwakirunge Dumpsite, Kenya.

Abstract

Accumulation of solid waste is a major global challenge. The conventional waste disposal methods are often ineffective in mitigating solid waste pollution, highlighting the need for other sustainable alternatives. This study is aimed at isolating and identifying potential waste-degrading microorganisms from Mwakirunge dumpsite in Mombasa, Kenya. A total of 16 soil samples were collected using a randomized block design. The samples were inoculated in enriched basal media containing mixed municipal solid waste and incubated at 37°C for 21 days. Microbial identification was conducted using standard morphological, biochemical, and molecular approaches. DNA was extracted using organic isolation methods, and PCR amplification of the 16S rRNA gene for bacteria and the ITS gene for fungi was performed. Phylogenetic analysis grouped bacterial isolates into phylum Bacillota (Firmicutes), Pseudomonadota (Proteobacteria), and Actinomycetota (Actinobacteria) that included members of the genera bacilli, Pseudomonas, brevibacilli, Microbacterium, Ochrobactrum, Paenibacillus, Staphylococcus, Isoptericola, and Streptomyces. Fungal isolates belonged to the genus Aspergillus within the phylum Ascomycota. Three bacterial isolates B4S2 b (MZ571886), B3S1 (MZ571907), and B3S4 B (MZ571915) and one fungal isolate B2S2 a1 (MZ569413) had low sequence similarities with their closely known taxonomic relatives. The ability of the isolates to produce lipase, esterase, cellulase, amylase, and gelatinase enzymes was tested using the agar diffusion method. The results showed a significant level of enzyme production (p < 0.05). Bacillus cereus (MZ571899) exhibited the highest esterase activity; Streptomyces thermocarboxydus (MZ571882) exhibited the highest lipase activity, Bacillus subtilis (MZ571887) exhibited the highest amylase activity, and Bacillus licheniformis (MZ571888) exhibited the highest cellulase activity, while Pseudomonas stutzeri (MZ571900) exhibited the highest gelatinase activity. We recommend further studies to characterize the isolates with low sequence percentage similarities to establish their true identities. In addition, further enzymatic studies are required to quantify, characterize, and purify these enzymes for industrial applications.