Abstract
Lipase plays a pivotal role in the rancidity pathway of lipids and it hinders the industrial development of oat products. The existing methods to inactivate lipase are energy intensive and cause nutrient loss. Understanding the structure and characteristics of oat lipase could lead to better inactivation methods. Oat Lipase was extracted, partially purified, and its characteristics and structure were studied. The partially purified protein matched the Os06g0157000 protein with 36.5 kDa and belonged to the ‘GDSL’ lipolytic enzyme family. Oat lipase showed highest catalytic activity at 40 °C, pH 7.5 and held stability below 50 °C and at pH 7.0–8.0. Cu2+, Fe3+, Ba2+, K+ and Mg2+ all inhibited oat lipase activity, with Fe3+ having the strongest effect. The oat lipase showed high specificity for hydrolysis of oat oil. The results of molecular docking and molecular dynamics analysis showed that avenanthramides (AVAS), rutin, and ferulic acid were potential lipase inhibitors, with ferulic acid having the greatest effect. In storage experiments of pearled oats, ferulic acid delayed lipid hydrolysis and lipid oxidation degradation. In the present study, we found a natural lipase inhibition that is safe and nutritional.
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