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- W4385800455 abstract "Abstract Ethylenediaminetetraacetic acid (EDTA), a chelating agent, has shown the ability to enhance the thermostability of cyclomaltodextrinase from Geobacillus thermopakistaniensis (CDase Gt ). There was a 5-fold and 3-fold enhancement in the half-life of the enzyme at 70 and 75°C, respectively, when purified in the presence of EDTA. To further investigate, recombinant CDase Gt was subjected to molecular-level characterization using various techniques including circular dichroism spectroscopy, fluorescence spectroscopy, and fourier-transform infrared spectroscopy in the presence and absence of EDTA. Presence of EDTA caused several changes in the secondary structure of CDase Gt , specifically in terms of chirality and relocation of hydrophobic patches. No disturbance in the functional groups were observed with the addition of EDTA. The affinity analysis displayed a favorable binding and attractive electrostatic interactions between CDase Gt and EDTA. These findings provide insights into CDase Gt −EDTA interactions for better understanding of the structure-function relationship. The findings from this study contribute to our understanding of enzyme stability and provide valuable information for the development of more efficient and stable enzymes with a wide range of practical applications." @default.
- W4385800455 created "2023-08-15" @default.
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- W4385800455 date "2023-08-14" @default.
- W4385800455 modified "2023-09-27" @default.
- W4385800455 title "Ethylenediaminetetraacetic acid enhances structural stability and thermotolerance of recombinant cyclomaltodextrinase from Geobacillus thermopakistaniensis at higher temperatures." @default.
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- W4385800455 doi "https://doi.org/10.21203/rs.3.rs-3235108/v1" @default.
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