Abstract
ABSTRACT The subunit composition, and thermal and molecular conformation properties of arachin from six peanut varieties are characterized and compared. The thermal and molecular conformation properties including the thermal stability, steady flow properties, surface hydrophobicity, and sulfhydryl content were determined. Two groups of arachin were identified: one containing the 35.5 kDa subunit and the other one without this specific subunit. The results showed that arachin with the 35.5 kDa subunit was more heat-sensitive (Tonset <100°C), had a significant lower initial denaturation temperature, less disulfide bonds, and more hydrophobic groups. The arachin without the 35.5 kDa subunit was less heat-sensitive to temperature (Tonset >100°C), and a more compact globular structure. The presence or absence of 35.5 kDa subunit in arachin significantly influenced the thermal and molecular conformation properties of arachin. Furthermore, the 35.5 kDa subunit was sequenced by Q-TOF and identified as an isoform of Ara h3. This study can provide useful information for processing peanut protein products with good thermal stability and hypoallergenic properties.
Highlights
Peanut (Arachis hypogaea) is an important legume crop and its proteins represent 11% of the world protein consumption
The results showed that arachin with the 35.5 kDa subunit was more heat-sensitive (Tonset
According to the content of the four arachin bands, the six varieties were categorized into two groups: one containing the 35.5 kDa subunit and the other one without this specific subunit
Summary
Peanut (Arachis hypogaea) is an important legume crop and its proteins represent 11% of the world protein consumption. By SDS-PAGE, arachin was confirmed to be composed by four polypeptides bands with molecular weight of 40.5–42 kDa, 37.5–39, 35.5–36 kDa, and 22–23.5 kDa.[4,9,10]
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