Inactivation of Lipoxygenase in Soybeans with Retention of Protein Solubility
1987
EDIRIWEERA, NANDANIE | AKIYAMA, YOSHINOBU | SAIO, KYOKO
The enzyme lipoxygenase, in soybeans, catalyzes the oxidation of polyunsaturated fatty acids containing a cis, cis 1:4 pcntadiene unit, resulting in rancid off‐flavors and poor storage stability. The effects of various processing conditions such as soaking, heating. pH and shearing action on the inactivation of lipoxygenase were investigated. The results showed that lipoxygenase activity was decreased by homogenization and by modcrate heating. Of the three isozymes of lipoxygenase. resistance to inactivation by homogenization and heating was in the order LI > L2 >L3. Total inactivation of soybean lipoxygenase was achicvcd by soaking the seeds at pH 8.5 at about 50°C for a minimum of 3–4 hr. followed by homogenization with water at about 60°C. for 15–30 min at 20,000 rpm.
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