| Abstract
| - The major globulin (anacardein) in cashew nut (Anacardiumoccidentale) is a 13S globulin. Theglobulin is not a glycoprotein and is composed of at least two majortypes of polypeptides withestimated molecular weights in the range 18000−24000 and30000−37000. The globulin hasA1%280nmof 9.88, 10.56, 9.68, and 9.59 in distilled water, 0.5 M NaCl, 0.02 Msodium phosphate buffer pH7.5, and 0.02 M Tris-HCl buffer pH 8.1, respectively. The Stokesradius of the globulin was 57 ±3.2 Å (n = 17). The isoelectric pH (pI) of the globulin was inthe pH range 6.2−7.2. Hydrophobic,uncharged polar, acidic, and basic amino acids respectively accountedfor 36.4, 19.88, 25.3, and18.4% of the total amino acids. Sulfur amino acids and threoninewere respectively the first andsecond limiting amino acids in the purified globulin. Among theproteinases tested, pepsin was themost efficient in hydrolyzing the globulin invitro. Keywords: Cashew; nuts; globulin; protein; in vitrodigestibility
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