Ethylenediaminetetraacetic acid enhances structural stability and thermotolerance of recombinant cyclomaltodextrinase from Geobacillus thermopakistaniensis at higher temperatures
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Plant Science,Genetics,Molecular Biology,Animal Science and Zoology,Biochemistry,Ecology, Evolution, Behavior and Systematics
Link
https://link.springer.com/content/pdf/10.1007/s11756-023-01542-z.pdf
Reference29 articles.
1. Ali R, Shafiq MI (2015) Sequence, structure, and binding analysis of cyclodextrinase (TK1770) from T. kodakarensis (KOD1) using an in silico approach. Archaea 2015:179196. https://doi.org/10.1155/2015/179196
2. Aroob I, Ahmad N, Aslam M, Shaeer A, Rashid N (2019) A highly active α-cyclodextrin preferring cyclomaltodextrinase from Geobacillus thermopakistaniensis. Carbohydr Res 481:1–8. https://doi.org/10.1016/j.carres.2019.06.004
3. Aroob I, Ahmad N, Rashid N (2021) Cyclodextrin-preferring glycoside hydrolases: properties and applications. Amylase 5:23–37. https://doi.org/10.1515/amylase-2021-0003
4. Aroob I, Javed M, Ahmad N, Aslam M, Rashid N (2022) Investigating the role of carbohydrate-binding module 34 in cyclomaltodextrinase from Geobacillus thermopakistaniensis: structural and functional analyses. 3 Biotech 12:1–12. https://doi.org/10.1007/s13205-021-03089-9
5. Bernfeld P (1955) Amylases, alpha and beta. Methods Enzymol 1:149–158
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