I am conducting an activity assay to assess the Enzymatic Hydrolysis of 4-Nitrophenyl ?-D-Glucopyranoside by ?-D-Glucosidase. I am happy with the assay, however one of the components is bovine serum albumin ( 0.2% solution in phosphate buffer, to which my enzyme solution is added).
I initially assumed that the BSA acted as somesort of stabiliser to my enzyme, however I am unsure and would like this verified or corrected, and potentially explained how/why is plays this role and why it does not interfere (i hope!) with my enzyme and role!
PS - I am not using the BSA as a control
This question was answered on: Sep 16, 2020
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