PMID: 36168May 10, 1979

Characterization of byssochlamyopeptidase A

Biochimica Et Biophysica Acta
P S Sun, F S Chu

Abstract

The enzyme properties of byssochlamyopeptidase A, a chymosin-like enzyme produced by Byssochlamys fulva were studied. The enzyme was shown to be electrophoretically and immunochemically pure. Most metallic cations had negligible effect, whereas Hg2+ greatly suppressed the enzyme activity. N-Bromosuccinimide and I2 completely inactivated the enzyme. For milk clotting at pH 4.6-6.6, the enzyme was less sensitive to pH than pepsin. The substrate specificity of the enzyme was studied by incubation of the enzyme at 37 degrees C with whole and individual casein fractions at pH 6.6 and pH 3.0, respectively. The proteolysis by the enzyme was found to be most extensive for alphas-, less for kappa-, and least for beta-casein. Studies with different synthetic dipeptides and tripeptides revealed that byssochlamyopeptidase A exhibits specificity for Phe-Tyr and Gly-Phe-Phe, but the enzyme did not hydrolyze Ac-Phe-Tyr(I2).

Related Concepts

Casein allergenic extract
Caseins
Immune Sera
Endopeptidases
Blood Coagulation Disorders
Endomycopsis
Cations
Enzyme Activity
Substrate Specificity
Blood Enzyme Activity (Lab Test)

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