Abstract
Egyptian peanut (Arachis hypogaea L.) samples were roasted at 180°C for different time periods (0, 3, 5, 10, 20, and 45 min). Different protein fractions (total soluble protein, albumin, globulin and sodium dodecyl sulfate–2-mercapto ethanol) were separated using different solvents. Activities of acid phosphatase (AP), lipoxygenase (LOX), POX and polyphenol oxidase (PPO) were estimated in the total soluble protein fraction of roasted peanut. The results showed that peanut protein solubilities were variable and dependent on roasting temperature. Most of the albumin bands of roasted peanut samples changed after 20 min roasting time as well as the major arachin globulin protein starting to disappear. AP, LOX, POX, esterase, catalase and PPO activities showed significant decrease as a result of the roasting process.
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Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.