Part:BBa_K3895004
Keratinase kerBteQ7
KerBteQ7 is a serine keratinase originally found in Bacillus tequilensis Q7. 6x His-tags were added to both sides of the sequence for purification, and constructed into PET-28a(+) (BBa_K3895008). The length of KerBteQ7 is 1214 bp.
Name of keratinase | IPTG concentration/mM | Temperature/°C | Time/h |
---|---|---|---|
KerBteQ7 | 5 | 16 | 12 |
Modeling
The biological activity of a protein is not only determined by the primary structure of the protein molecule but also closely related to its specific spatial structure. Elucidating the process of protein folding in functional and structural details will be of great significance to evaluate their keratinotic functions. According to the amino acid sequences in the enzyme active sites and associated catalytic mechanisms, proteases can be classified into seven broad groups: serine, cysteine, threonine, aspartic and glutamic proteases, metalloproteases and asparagine peptide lyases. According to the nature of their active site, keratinases belong to serine- and metalloproteases or serine metalloproteases. Moreover, the enzymatic degradation of keratin is a multistage process that requires the following steps: adsorption of the keratinases to the surface of macromolecule by electrostatic and hydrophobic interactions, followed by catalytic action [2]. Hence we used Swiss Model to predict their hydrophobic region and serine groups.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 457
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 1156
References
Zaraî Jaouadi, N., Rekik, H., Ben Elhoul, M., Zohra Rahem, F., Gorgi Hila, C., Slimene Ben Aicha, H., Badis, A., Toumi, A., Bejar, S., & Jaouadi, B. (2015). A novel keratinase from Bacillus tequilensis strain Q7 with promising potential for the leather bating process. International Journal of Biological Macromolecules, 79, 952–964. https://doi.org/10.1016/j.ijbiomac.2015.05.038
Vidmar, Beti, and Maša Vodovnik. “Microbial Keratinases: Enzymes with Promising Biotechnological Applications.” Food technology and biotechnology vol. 56,3 (2018): 312-328. doi:10.17113/ftb.56.03.18.5658
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