Relationship between in vitro Fe and Zn dialysability and peptide composition of albumin and globulins extracted from cooked bean (Phaseolus vulgaris L.)

References

• AOAC. Official Method of Analysis, 14th edn. Association of Official Analytical Chemists, Arlington, VA 1984
   Google Scholar
• Bodwell C E, Satterlee L D, Hackler L R. Protein digestibility of the same protein preparations by human and rat assays and by in vitro enzymic digestion methods. Am. J. Clin. Nutr. 1980; 33: 677–686
   PubMed Web of Science ®Google Scholar
• Bressani R, Elias L G. The nutritional role of polyphenols in beans. Polyphenols in Cereals and Legumes, J H Hulse. IDRIC, Ottawa 1980; 61–68
   Google Scholar
• Carbonaro M, Marletta L, Carnovale E. Factors affecting cystine reactivity in proteolytic digests of Phaseolus vulgaris. J. Agric. Food Chem. 1992; 40: 169–174
   Web of Science ®Google Scholar
• Carbonaro M, Vecchini P, Carnovale E. Protein solubility of raw and cooked beans (Phaseolus vulgaris): role of the basic residues. J. Agric. Food Chem. 1993; 41: 1169–1175
   Web of Science ®Google Scholar
• Carbonaro M, Lombardi-Boccia G, Carnovale E. Influence of the method of protein extraction on the in vitro evaluation of mineral dialysability from legumes. Food Chem. 1995; 53: 249–252
   Web of Science ®Google Scholar
• Cook J D, Monsen E. Vitamin C, the common cold, and iron absorption. Am. J. Clin. Nutr. 1977; 30: 235–241
   PubMed Web of Science ®Google Scholar
• Cook J D, Morck T A, Lynch S R. The inhibitory effect of soy products on none heme iron absorption in man. Am. J. Clin. Nutr. 1981; 34: 2622–2629
   PubMed Web of Science ®Google Scholar
• Duncan D B. Multiple range and multiple F test. Biometrics 1955; 11: 1–42
   Web of Science ®Google Scholar
• Gujska E, Khan K. High temperature extrusion effect on protein solubility and distribution in navy and pinto beans. J. Food Sci. 1991; 56: 1013–1016
   Web of Science ®Google Scholar
• Hallberg L, Rossander L. Effect of soy protein on nonheme iron absorption in man. Am. J. Clin. Nutr. 1982; 36: 514–520
   PubMed Web of Science ®Google Scholar
• Hallberg L, Rossander L, Skanberg A B. Phytates and the inhibitory effect of bran on iron absorption in man. Am. J. Clin. Nutr. 1987; 45: 988–996
   PubMed Web of Science ®Google Scholar
• Harland B F, Oberleas D. Anion-exchange method for determination of phytate in foods: collaborative study. J. Assoc. Off. Anal. Chem. 1986; 64(4)667–670
   Google Scholar
• Hurrell R F, Juillerat M A, Reddy M B, Lynch S R, Dassenko S A, Cook J D. Soy protein, phytate, and iron absorption in humans. Am. J. Clin. Nutr. 1992; 56: 573–578
   PubMed Web of Science ®Google Scholar
• Kane A P, Miller D D. In vitro estimation of the effects of selected proteins on iron bioavailability. Am. J. Clin. Nutr. 1984; 39: 393–401
   PubMed Web of Science ®Google Scholar
• Lombardi-Boccia G, Di Lullo G, Carnovale E. In vitro iron dialysability from legumes: influence of phytate and extrusion-cooking. J. Sci. Food Agric. 1991; 55: 599–605
   Web of Science ®Google Scholar
• Lombardi-Boccia G, Carbonaro M, Di Lullo G, Carnovale E. Influence of protein components (G1, G2 and albumin) on Fe and Zn dialysability from bean (Phaseolus vulgaris). J. Food Sci. Nutr. 1994; 49: 183–190
   Google Scholar
• Lombardi-Boccia G, De Santis N, Di Lullo G, Carnovale E. Impact of processing on Fe dialysability from bean (Phaseolus vulgaris L.). Food Chem. 1995; 53: 191–195
   Web of Science ®Google Scholar
• Lowry O H, Rosebrough N J, Farr A L, Randall R J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Lynch S R, Dassenko S A, Cook J D, Juillerat M A, Hurrell R. Inhibitory effect of soybean protein-related moiety on iron absorption in humans. Am. J. Clin. Nutr. 1994; 60: 567–572
   PubMed Web of Science ®Google Scholar
• Macfarlane B J, Van der Riet W B, Bothwell T H, Baynes R D, Siegenberg D, Schmidt U, Tal A, Taylor J RN, Mayet F. Effect of traditional oriental soy products on iron absorption. Am. J. Clin. Nutr. 1990; 51: 873–880
   PubMed Web of Science ®Google Scholar
• McWatters K H, Holmes M R. Influence of moist heat on solubility and emulsification properties of soy and peanut flours. J Food Sci. 1979; 44: 774–776
   Web of Science ®Google Scholar
• Marletta L, Carbonaro M, Carnovale E. In vitro protein and sulphur amino acid availability as a measure of bean protein quality. J. Sci. Food Agric. 1992; 59: 497–504
   Web of Science ®Google Scholar
• Marquez U M, Lajolo F M. Composition and digestibility of albumin, globulins and glutelins from Phaseolus vulgaris. J. Agric. Food Chem. 1981; 29: 1068–1074
   PubMed Web of Science ®Google Scholar
• Miller D D, Schricker B R, Rasmussen R R, Van Campen D. An in vitro method for estimation of iron availability from meals. Am. J. Clin. Nutr. 1981; 34: 2248–2256
   PubMed Web of Science ®Google Scholar
• Moore S, Spackman D M, Stein W H. Chromatography of amino acids on sulphonated polystyrene resins. Anal. Chem. 1958; 30: 1185–1190
   Web of Science ®Google Scholar
• Reddy N R, Sathe S K, Salunkhe D K. Phytates in legumes and cereals. Adv. Food Res. 1982; 28: 1–92
   PubMed Web of Science ®Google Scholar
• Sandstrom B, Almgren A, Kivisto B, Cederblad A. Effect of protein level and protein source on zinc absorption in humans. J. Nutr. 1989; 119: 48–53
   PubMed Web of Science ®Google Scholar
• Sathe S H, Iyer V, Salunkhe D K. Functional properties of the Great Northern bean (Phaseolus vulgaris L.) proteins. Amino acid composition, in vitro digestibility and application to cookies. J. Food Sci. 1981; 47: 8–11
   Web of Science ®Google Scholar
• Schnepf M, Satterlee L D. The interaction of iron with proteins and peptides. Interactions of Food Components, G G Birch, M G Lindley. Elsevier Applied Science, London 1986; 43–62
   Google Scholar
• Schram E, Moore S, Bigwood E J. Chromatographic determination of cystine as cysteic acid. Biochem. J. 1954; 57: 33–57
   PubMed Web of Science ®Google Scholar
• Sun S M, McLeester R C, Bliss F A, Hall T C. Reversible and irreversible dissociation of globulin from Phaseolus vulgaris seed. J. Biol. Chem. 1974; 249: 2118–2121
   PubMed Web of Science ®Google Scholar
• Zahler W L, Cleland W W. A specific and sensitive assay for disulfides. J. Biol. Chem. 1968; 243: 716–719
   PubMed Web of Science ®Google Scholar