Author
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SATHE, S - FLORIDA STATE UNIV |
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SZE-TAO, K - FLORIDA STATE UNIV |
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WOLF, WALTER |
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HAMAKER, B - PURDUE UNIV |
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Submitted to: Institute of Food Technology
Publication Type: Abstract Only Publication Acceptance Date: 6/26/1996 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Cashews are a good source of high quality protein. Detailed biochemical characterization of cashew proteins has not been accomplished. In an earlier investigation we have reported that only one protein dominated the total cashew protein composition. The purpose of this investigation was to isolate, purify, and biochemically characterize this major protein in cashew nut. Defatted cashew flour was extracted with 2 M NaCl (flour to solvent ratio 1:10 w/v) with constant magnetic stirring, filtered, and the filtrate centrifuged (12,000 X g, 4 deg C, 10 min). The major protein was purified from the supernatant using Sephacryl S300 HR column chromatography. The isolated protein was homogeneous based on elution off gel filtration and DEAE DE-53 columns, ultracentrifuge analysis (single peak with estimated sedimentation value of 11S), and nondenaturing nondissociating gel electrophoretic analysis. This protein was composed of major polypeptides with estimated molecular weights in the range of 20,000 to 60,000. Glycoprotein staining of the gels indicated that this is not a glycoprotein. The Stokes' radius of the protein was 57 +/ 3.2 Angstroms. 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 theonine were, respectively, the first and second limiting amino acids in the purified protein. |
