Isolation and partial characterization of flaxseed (Linum usitatissimum L.) proteins

✍ Scribed by Dev, D. K. ;Sienkiewicz, T. ;Quensel, E. ;Hansen, R.

• Publisher: John Wiley and Sons
• Year: 1986
• Tongue: English
• Weight: 385 KB
• Volume: 30
• Category: Article
• ISSN: 0027-769X
• DOI: 10.1002/food.19860300350

✦ Synopsis

Unlike most other oilseed proteins, proteins from flaxseed have not been extensively studied. Nitrogen solubility of defatted flaxseed meal has been variously investigated [ I . 3 -51. Amino-acid compositions of oil-free meal and isolated proteins from flaxseed have also been reported (2. 3, 61. MADHUSUDHAN et al. [I J recently characterized total proteins of flaxseed by gel filtration. ion-exchange chromatography, elcctrophoresis and ultracentrifugation, and reported the presence of at least 3 components. To obtain further inforination on flaxseed proteins, we performed the fdllowing experiments.

A defatted tlour (DF. particle size <250 pm) obtained from cold-pressed flaxseed meal. a protein isolate ( P I ) prepared by alkaline extraction (NaOH, pH 9.5) and isoelectric precipitation (HCI. pH 4.2) of proteins, and two water-and salt-soluble protein fractions (WSPF and SSPF) obtained by successive extractions of D F with C0,-free distilled water and 0.5 M NaCl, respectively, followed by dialysis against distilled water at 4 'C for 48 h, were studied for their gel electrophoretic pn&rns and amino-acid profiles. The protein preparations were freeze-dried before the studies.