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Division of Biochemistry, The Agricultural and Technical College of North Carolina, Greensboro
ABSTRACT
An esterase from bovine liver acetone powder has been concentrated 60-fold by water extraction and precipitation with acetone. The activity of the enzyme toward various low molecular weight substrates was studied. Triacetin was adopted as a substrate for comparative activity studies. Under the conditions of the assay, the optimum pH for esterase activity was found by using phosphate buffer to be approximately 8.0.
With reference to tenulin, an acetic acid ester, it was observed that bovine liver esterase was without action upon the ester linkage.
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