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Bromelain was purified from Korean pineapple, Ananas comosus, L. The enzyme was purified about 21 fold by DEAF-cellulose ion-exchange chromatography and gel filtration on Sephadex G-150. Purified enzyme was confirmed as active single band by polyacrylamide electrophoresis and the molecular weight was estimated to be about 22,000 by SDS-PAGE. The optimum pH and temperature were 6.0 and 60℃, respectively. The range of its stability to the pH and temperature were respectively 5.0 to 7.0 and below 50℃. It was found that Mn^(2+) increased the enzyme activity, whereas Mg^(2+) and Fe^(2+) decreased it abruptly. The purified enzyme was inhibited by ρ-chloromercuribenzoic acid, indicating that reactive SH groups are required for the enzyme activity. The reaction of the enzyme followed typical Michaelis-Menten kinetics with Km value of 5.747×10^(-4) M and Vmax of 131.58 ㎍/min for casein. When meat was treated with the enzyme, free soluble nitrogen and amino acid nitrogen increased as enzyme concentration increased.
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