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    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

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    Solution Preview

    Hi there,

    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 ...

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