Investigating the role of carbohydrate-binding module 34 in cyclomaltodextrinase from Geobacillus thermopakistaniensis: structural and functional analyses

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 puri ed in the presence of EDTA. To further investigate, recombinant CDase Gt was subjected to molecular-level characterization using various techniques including circular dichroism spectroscopy, uorescence 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 , speci cally in terms of chirality and relocation of hydrophobic patches. No disturbance in the functional groups were observed with the addition of EDTA. The a nity analysis displayed a favorable binding and attractive electrostatic interactions between CDase Gt and EDTA. These ndings provide insights into CDase Gt −EDTA interactions for better understanding of the structure-function relationship. The ndings from this study contribute to our understanding of enzyme stability and provide valuable information for the development of more e cient and stable enzymes with a wide range of practical applications.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Investigating the role of carbohydrate-binding module 34 in cyclomaltodextrinase from Geobacillus thermopakistaniensis: structural and functional analyses

Cited by 2 publications

References 52 publications

Pcal_0976, a pullulanase homologue from Pyrobaculum calidifontis, displays a glycoside hydrolase activity but no pullulanase activity

Pcal_0976, a pullulanase homologue from Pyrobaculum calidifontis, displays a glycoside hydrolase activity but no pullulanase activity

Ethylenediaminetetraacetic acid enhances structural stability and thermotolerance of recombinant cyclomaltodextrinase from Geobacillus thermopakistaniensis at higher temperatures

Contact Info

Product

Resources

About