No abstract

The almond major storage protein, amandin, was prepared by column chromatography (amandin-1), cryoprecipitation (amandin-2), and isoelectric precipitation (amandin-3) methods. Amandin is a legumin type protein characterized by a sedimentation value of 14S. Amandin is composed of two major types of polypeptides with estimated molecular weights of 42-46 and 20-22 kDa linked via disulfide bonds. Several additional minor polypeptides were also present in amandin. Amandin is a storage protein with an estimated molecular weight of 427,300 +/- 47,600 Da (n = 7) and a Stokes radius of 65.88 +/- 3.21 A (n = 7). Amandin is not a glycoprotein. Amandin-1, amandin-2, and amandin-3 are antigenically related and have similar biochemical properties. Amandin-3 is more negatively charged than either amandin-1 or amandin-2. Methionine is the first essential limiting amino acid in amandin followed by lysine and threonine.

No abstract

The major globulin (anacardein) in cashew nut (Anacardium occidentale) is a 13S globulin. The globulin is not a glycoprotein and is composed of at least two major types of polypeptides with estimated molecular weights in the range 18000−24000 and 30000−37000. The globulin has A 1% 280nm of 9.88, 10.56, 9.68, and 9.59 in distilled water, 0.5 M NaCl, 0.02 M sodium phosphate buffer pH 7.5, and 0.02 M Tris-HCl buffer pH 8.1, respectively. The Stokes radius of the globulin was 57 ± 3.2 Å (n = 17). The isoelectric pH (pI) of the globulin was in the pH range 6.2−7.2. Hydrophobic, uncharged polar, acidic, and basic amino acids respectively accounted for 36.4, 19.88, 25.3, and 18.4% of the total amino acids. Sulfur amino acids and threonine were respectively the first and second limiting amino acids in the purified globulin. Among the proteinases tested, pepsin was the most efficient in hydrolyzing the globulin in vitro. Keywords: Cashew; nuts; globulin; protein; in vitro digestibility