Hi Amal Senevirathne ,

tricky questions. About the glycosilation state of the protein: If there is no literature available on that, you could search Proteomic databases (i.e. PRIDE) for LC-MS raw data i.e. about Engyodontium album (f.k.a. Tritirachium album). If there are some measurements available you can run a peptide identification search with glycosilation as a fixed and as a variable modification. If your are lucky Proteinase K is found in the MS data and by comparing your two searches you can get an idea if there is a glycositic modification on that protein and if so, how much of it is glycosilated.

Sorry that I can't really help you with the other questions. I guess that is try an error. The protein is about 384 AA long. I think this not a super larger protein - hence it is likely that it could be robustly expressed in a transgenic bacterial culture.

Dear Hannes Reinwald,

Thank you for your detailed answer and for introducing me important databases. I will try the way that you have suggested. I hope I can get an idea about my proteins' state of glycosylation. Once again, thank you very much.

Regards,

Amal.

Check https://www.sciencedirect.com/topics/nursing-and-health-professions/proteinase-k

Kindly check this paper.

https://www.pnas.org/content/87/21/8262.full.pdf

Hi Dr Amal Senevirathne . See the following link: https://www.sciencedirect.com/topics/nursing-and-health-professions/proteinase-k

See the following RG link: Article Protein glycosylation analysis by HILIC-LC-MS of Proteinase ...

See also the following link: https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/protein-glycosylation.html

I will second Hannes Reinwald here, if you will.

Dear Chinaza Godswill Awuchi, Kiprotich Kiptum, and Aref Wazwaz thank you all for your recommendations to solve my problem.

Thank you,

Amal.