Publications by authors named "F Mulaa"

Article Synopsis
  • The study investigates how fungi can enhance the breakdown of soil organochlorine pesticides (OCPs) by aiding in nutrient transfer to bacteria in nutrient-poor environments.
  • Researchers used model ecosystems with a legacy pesticide (hexachlorocyclohexane or HCH), a non-degrading fungus (Fusarium equiseti K3), and a degrading bacterium (Sphingobium sp. S8) to track the interaction and nutrient flow between them.
  • Results showed that fungal nutrients significantly boosted the bacteria's ability to degrade HCH, with the interaction leading to twice the pesticide removal compared to bacteria alone, highlighting the importance of fungal-bacterial relationships in environmental cleanup
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The draft genome sequences of two strains that are hexachlorocyclohexane (HCH) degraders are presented. The strains were isolated from HCH-contaminated soil in Kitengela, Kenya. Both genomes possess the genes responsible for HCH degradation and gene clusters for degradation of other xenobiotic compounds.

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We present the draft genome sequence of Fusarium equiseti strain K3, a fungus isolated from a hexachlorocyclohexane (HCH)-contaminated soil (Kitengela, Kenya). The 37.88-Mb draft genome sequence consists of 206 contigs, 12,311 predicted protein-coding sequences, and 261 tRNA sequences.

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The development of novel anti-infectives against Kinetoplastids pathogens targeting proteins is a big problem occasioned by the antigenic variation in these parasites. This is also a global concern due to the zoonosis of these parasites, as they infect both humans and animals. Therefore, we need not only to create novel antibiotics, but also to speed up the development pipeline for these antibiotics.

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Objectives: To search for new alkaliphilic cellulases and to improve their efficiency on crystalline cellulose through molecular engineering RESULTS: Two novel cellulases, BpGH9 and BpGH48, from a Bacillus pumilus strain were identified, cloned and biochemically characterized. BpGH9 is a modular endocellulase belonging to the glycoside hydrolase 9 family (GH9), which contains a catalytic module (GH) and a carbohydrate-binding module belonging to class 3 and subclass c (CBM3c). This enzyme is extremely tolerant to high alkali pH and remains significantly active at pH 10.

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