Purification, characterization, and biocatalytic potential of a novel dextranase from Chaetomium globosum
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We aimed to identify new high-yield dextranase strains and study the catalytic potential of dextranase from the strain in industrial applications.
Dextranase-producing strains were screened from soil samples, and a potential strain was identified as Chaetomium globosum according to its phenotype, biochemical characteristics, and rDNA analysis. Crude dextranase was purified to reach 10.97-fold specific activity and 18.7% recovery. The molecular weight of the enzyme was 53 kDa with an optimum temperature and pH of 60 °C and 5.5, respectively. Enzyme activity was stable at pH 4.0–7.0 and displayed sufficient thermal stability at temperatures < 50 °C. Mn2+ (10 mM) enhanced dextranase activity by 134.44%. The enzyme was identified as an endodextranase. It displayed very high hydrolytic affinity toward high-molecular weight dextran T2000, reaching 97.9% hydrolysis within 15 min at 2 U/mL.
Collectively, these results suggest that Chaetomium globosum shows higher production and specificity of dextranase than that from other reported strains. These findings may offer new insights into the potential of dextranase in the sugar, medical, and food industries.
KeywordsDextranase Chaetomium globosum Dextran Hydrolysis
This work was supported by the National Science Foundation (No. 31601558), the Fundamental Research Funds for the Central Universities (JUSRP51402A).
Supplementary Fig. 1—Kinetic study of Chaetomium globosum dextranase. (a) Dextran T20 as the substrate. (b) Dextran T40 as the substrate. (c) Dextran T2000 as the substrate.
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Conflict of interest
The authors declare no conflicts of interest.
Research involving human participants or animals
The authors declare that there are no studies conducted with human participants or animals.
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