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Two Lipoxygenases from Germinated Barley‐Heat and Kilning Stability
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ABSTRACT
Using ammonium sulfate precipitation followed by hydrophobic and ion exchange chromatography, two lipoxygenase isoenzymes, LOX 1 and LOX 2, were 18.3‐ and 44.5‐fold purified from germinated barley, with 18 and 24% recovery of activity respectively. LOX 1 and LOX 2 were characterized by isoelectric points 4.9 and 6.4, and molecular weights of 90 kd and 110 kd, respectively. Apparent Km values for linoleic acid were 0.06 mM for LOX 1 and 0.18 mM for LOX 2. LOX 1 converted linoleic acid to 9 and 13 hydroperoxides at about 4:1, whereas the 13 hydroperoxide was the major product formed by LOX 2 (ratio 3:7). For both isoforms, thermal inactivation data indicated first order kinetics with activation energies influenced by ionic strength and pH. Isoenzymes composition was analyzed for three kilning schemes: the 1:3 ratio between LOX 1 and LOX 2 observed in germinated barley increased during the course of kilning.
Title: Two Lipoxygenases from Germinated Barley‐Heat and Kilning Stability
Description:
ABSTRACT
Using ammonium sulfate precipitation followed by hydrophobic and ion exchange chromatography, two lipoxygenase isoenzymes, LOX 1 and LOX 2, were 18.
3‐ and 44.
5‐fold purified from germinated barley, with 18 and 24% recovery of activity respectively.
LOX 1 and LOX 2 were characterized by isoelectric points 4.
9 and 6.
4, and molecular weights of 90 kd and 110 kd, respectively.
Apparent Km values for linoleic acid were 0.
06 mM for LOX 1 and 0.
18 mM for LOX 2.
LOX 1 converted linoleic acid to 9 and 13 hydroperoxides at about 4:1, whereas the 13 hydroperoxide was the major product formed by LOX 2 (ratio 3:7).
For both isoforms, thermal inactivation data indicated first order kinetics with activation energies influenced by ionic strength and pH.
Isoenzymes composition was analyzed for three kilning schemes: the 1:3 ratio between LOX 1 and LOX 2 observed in germinated barley increased during the course of kilning.
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