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Inactivation of Lipoxygenase in Soybeans with Retention of Protein Solubility
Author(s) -
EDIRIWEERA NANDANIE,
AKIYAMA YOSHINOBU,
SAIO KYOKO
Publication year - 1987
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1987.tb06703.x
Subject(s) - lipoxygenase , chemistry , homogenization (climate) , polyunsaturated fatty acid , enzyme , food science , biochemistry , chromatography , fatty acid , biology , biodiversity , ecology
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.