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© BrainMass Inc. brainmass.com October 10, 2019, 1:14 am ad1c9bdddf
first of all: your assumption is correct! Bovine Serum Albumin (BSA) is a protein stabilization reagent that is commonly employed in 0.1 to 1.0 % w/v solution in many biochemical assays.
Why is that? Well, I have not been able to find 'hard' scientific evidence that has examined the role of BSA in these experiments, however, one can deduce its role ...
A full solution is provided. The expert examines hydrolysis activity assay.