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Phylogenetic relationship of the bacterial DNA of the selected isolates to other closely related sequences obtained from the GenBank. *Multiple alignments of the sequences corresponding to the 16S rRNA of the studied isolates were carried out followed by neighbour joining clustering. Bootstrap values expressed as percentages of 1000 replications. 

Phylogenetic relationship of the bacterial DNA of the selected isolates to other closely related sequences obtained from the GenBank. *Multiple alignments of the sequences corresponding to the 16S rRNA of the studied isolates were carried out followed by neighbour joining clustering. Bootstrap values expressed as percentages of 1000 replications. 

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This study is designed to investigate cellulolytic bacteria capable of removing cellulolytic wastes that are produced from cassava during processing. Cellulolytic bacteria isolates from cassava dumpsite soil in Ibadan, Nigeria were characterized and their optimal culture conditions determined. The total viable bacterial count of the sample of cassa...

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... and phylogeny of the isolates CAC1 and CAC2 were determined as Kurthia gibsonii and Myroides odoratimimus using 16S rDNA analysis. The strains showed maximum similarity ratio towards Kurthia gibsonii SP22 (90%), and a similarity of 98% identity with the sequence of 16S rRNA of Myroides odoratimimus respectively using BLAST and hence the isolates were named as Kurthia gibsonii CAC1 and Myroides odoratimimus CAC2. The phylogenetic tree, calculated using the neighbour-joining algorithm, is shown in Figure 1. The morphological characteristics of the selected isolates further confirmed the identity of the bacteria. While K. gibsonii CAC1 was observed to be Gram positive, motile, rod-shaped, aerobic with no pigmentation, M. odoratimimus CAC2 was Gram negative, non- motile, rod-shaped, and aerobic with slight yellowish pigmentation ( Table 3). Figure 2 illustrates the effect of increasing incubation period on the growth of K. gibsonii CAC1 at different temperature range. K. gibsonii CAC1 showed a gradual increase in growth until optimal growth (1.92nm) was observed at 25°C when incubated for 36hrs. After this time, a decline in growth of the isolates was observed. Highest growth was recorded at 37°C when incubated for 30hr after which there was a decline. At higher temperature of 45°C, lesser growth of the bacterium was recorded and there was a gradual increase in growth as the incubation period increased from 6 to 18hrs after which there was a slight decline before it increased to its peak (1.248nm) at 30hr of incubation and beyond this period, the growth of K. gibsonii CAC1 decreased. There was significant (p≥ 0.05) difference in the incubation period of K. gibsonii CAC1 relative to ...

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Citations

... The end product from this enzyme is glucose (Wood and McCrae, 1979). Kurthia gibsonii CAC1 is a motile, aerobic, rod-shaped, non-pigmented and Gram positive bacterium which grow best at incubation temperature of 30 o C and pH 5.5 with lactose and ammonium chloride supplemented medium as best carbon and nitrogen sources respectively (Adu et al., 2014). It has been investigated that Kurthia gibsonii CAC1 isolated from cassava dumpsites are capable of producing cellulase necessary to degrade cellulolytic components of cassava (Adu et al., 2014). ...
... Kurthia gibsonii CAC1 is a motile, aerobic, rod-shaped, non-pigmented and Gram positive bacterium which grow best at incubation temperature of 30 o C and pH 5.5 with lactose and ammonium chloride supplemented medium as best carbon and nitrogen sources respectively (Adu et al., 2014). It has been investigated that Kurthia gibsonii CAC1 isolated from cassava dumpsites are capable of producing cellulase necessary to degrade cellulolytic components of cassava (Adu et al., 2014). Hence, researching into factors that may influence enzymatic activity of the cellulase produced by Kurthia gibsonii CAC1 is the focus of this work. ...
... The end product from this enzyme is glucose (Wood and McCrae, 1979). Kurthia gibsonii CAC1 is a motile, aerobic, rod-shaped, non-pigmented and Gram positive bacterium which grow best at incubation temperature of 30 o C and pH 5.5 with lactose and ammonium chloride supplemented medium as best carbon and nitrogen sources respectively (Adu et al., 2014). It has been investigated that Kurthia gibsonii CAC1 isolated from cassava dumpsites are capable of producing cellulase necessary to degrade cellulolytic components of cassava (Adu et al., 2014). ...
... Kurthia gibsonii CAC1 is a motile, aerobic, rod-shaped, non-pigmented and Gram positive bacterium which grow best at incubation temperature of 30 o C and pH 5.5 with lactose and ammonium chloride supplemented medium as best carbon and nitrogen sources respectively (Adu et al., 2014). It has been investigated that Kurthia gibsonii CAC1 isolated from cassava dumpsites are capable of producing cellulase necessary to degrade cellulolytic components of cassava (Adu et al., 2014). Hence, researching into factors that may influence enzymatic activity of the cellulase produced by Kurthia gibsonii CAC1 is the focus of this work. ...
Research
This experiment reports the physicochemical characterization of cellulase produced by Kurthia gibsonii CAC1 isolated from cassava dumpsites in Ibadan, Nigeria. Lineweaver-Burk plot of cellulase activities of K.gibsonii CAC1 was examined with Kmax and Vmax of the enzyme assayed. At optimal pH of 5.0, 10% increase in enzymatic activities was observed. The enzymatic activities of K. gibsonii CAC1 were optimal at 30o C and were still stable at 60o C with 50% reduction in cellulase activities. Cellulase activities of K. Gibsonii CAC1 showed significant difference (p≥0.05) with the different cations used. There was no significant difference (p≤0.05) observed with increased concentrations (p≤0.05) using two-way ANOVA. Ca2+ highly enhanced the cellulase activities of K.gibsonii CAC1 by 60% at 10mM. Highest inhibition by Hg2+ was observed at 20mM with 50% inhibition. At increasing concentration of the inhibitors, there was no significant difference (p≤0.05) in cellulase activities; although the effect of each inhibitor on the enzymatic activity was significantly different (p≥0.05). Benzoic acid gave the highest inhibition of the cellulase activities in K. gibsonii CAC1 by 30% at 20mM, while Ethylene diamine-tetraacetic acid (EDTA) boosted the enzymatic activities by 10% at 10mM. There was a significant difference (p≥0.05) in the effect of different surfactants on the enzymatic activity but no significant difference (p≤0.05) with the concentration of the surfactants on cellulase activity. Enzymatic activities of the bacterium were enhanced by Polyoxyethylenesorbitan mono-oleate (Tween 80) with a boost of 50%. Increasing the concentration of sodium dodecyl sulphate (SDS) and Polyethylene glycol pisooctylphenylether (Trition X-100) caused a 70% increase in cellulase activities. Cellulase of K. gibsonii CAC1 had Kmax of 7.4 X 10-2 mg/ml and Vmax of 6.7 X 10-1 µg/sec.The cellulase described in this work have many properties that are similar to those obtained from other microbial sources and may be useful for various industrial applications.