ABSTRACTLipoxygenase (LOX) from fresh asparagus was partially purified by extraction of acetone‐washed asparagus powder with pH 4.5 potassium phosphate, ammonium sulfate fractionation and carboxymethyl‐cellulose (CMC) chromatography. Asparagus LOX purified by ammonium sulfate fractionation had a pH activity optimum of 5.5–6.0 and was stable at pH 4.5–8.0 when stored at 2°C. Asparagus LOX was active on monolinolein as well as linoleic acid, but activity was very low on di‐ or tri‐linolein. The CMC fractions with greatest LOX activity were nearly free of peroxidase activity while the protein fractions which did not bind with CMC at pH 5 were peroxidase active. The LOX activity in the purified asparagus extract was 90 inhibited by 1 mM cyanide when preincubated for 30
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