Analysis and thermal stability of porcine thyroglobulin-binding lectins in the major Phaseolus vugaris L. G2/albumin groups

Porcine thyroglobulin (PTG)-binding lectins from cultivars representing the five major G2/albumin groups of Phaseolus vulgaris L. were quantified and assayed for thermal stability with PTG-Sepharose affinity chromatography and the Folin-Ciocalteau protein assay. Lectin concentrations of the five cul...

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Veröffentlicht in:Journal of food science 1992-09, Vol.57 (5), p.1056-1059
Hauptverfasser: Bonorden, W.R. (University of Wisconsin-Madison, Madison, WI), Swanson, B.G
Format: Artikel
Sprache:eng
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Zusammenfassung:Porcine thyroglobulin (PTG)-binding lectins from cultivars representing the five major G2/albumin groups of Phaseolus vulgaris L. were quantified and assayed for thermal stability with PTG-Sepharose affinity chromatography and the Folin-Ciocalteau protein assay. Lectin concentrations of the five cultivars were 30, 25, 21, 21 and 15 mg g-1 dry flour, for Jamapa (M(G2)), ICA-Pijao (B(G2)), California Light Red Kidney (T(G2)), Black Turtle Soup (V(G2)) and Sanilac (S(G2)), respectively. Heat stabilities of the five major lectin-containing G2/albumin groups were M(G2) = B(G2) V(G2) S(G2) T(G2). Thermally processing whole beans at 89 degrees C for 60-130 min inactivated the lectins in all G2/albumin groups
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.1992.tb11261.x