title: The degradation of lectins, phaseolin and trypsin inhibitors during germination of white kidney beans, Phaseolus vulgaris L.
abstract: White kidney beans (Phaseolus vulgaris), cv Processor, contain a relatively high content of phaseolin (storage protein), lectins and a special group of glycoproteins as well as a considerable amount of protein-type trypsin inhibitors. Protein digestion of raw 'Processor' beans in monogastrics, for example pigs, is disturbed by poorly digested, phaseolin lectins, which can bind to carbohydrates in brush border membranes of the small intestinal epithelium, and trypsin inhibitors. The effect of the germination of white kidney beans on lectins, phaseolin and trypsin inhibitors was studied in order to achieve a degradation of lectins, phaseolin and trypsin inhibitors and an increase of in vitro enzymatic hydrolysis of the protein of bean flour. Therefore, whole bean extracts were examined throughout a germination period of up to seven days for their lectin and phaseolin pattern, lectin content, binding capacities of functional lectins towards brush border membranes and trypsin inhibitor content. In addition the in vitro enzymatic hydrolysis by pepsin and pancreatin of the protein from flours of (un)germinated white kidney beans was studied. SDS-PAGE demonstrated a degradation of E-lectins and a disappearance of L-lectins and phaseolin during germination. Results indicated a decrease of the lectin content by 85%, a loss of binding capacities of functional lectins towards brush border membranes by 91%, and a decrease of trypsin inhibitors by 76%, in bean flour after germination for seven days. A maximum in in vitro enzymatic hydrolysis of protein from bean flour was already established after germination for half a day.
authors.affiliation: Department of Animal Nutrition, Agricultural University, Wageningen, The Netherlands.
authors.forename: F H
authors.initials: FH
authors.lastname: Savelkoul
authors.forename: S
authors.initials: S
authors.lastname: Tamminga
authors.forename: P P
authors.initials: PP
authors.lastname: Leenaars
authors.forename: J
authors.initials: J
authors.lastname: Schering
authors.forename: D W
authors.initials: DW
authors.lastname: Ter Maat
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D004797:Enzyme-Linked Immunosorbent Assay; D007887:Fabaceae / Q000254:growth & development / Q000378:metabolism*; D006868:Hydrolysis; D037102:Lectins / Q000032:analysis / Q000378:metabolism*; D008871:Microvilli / Q000378:metabolism*; D037121:Plant Lectins; D010940:Plant Proteins / Q000378:metabolism*; D010946:Plants, Medicinal; D013552:Swine; D014361:Trypsin Inhibitors / Q000378:metabolism*
chemical_list: D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D014361:Trypsin Inhibitors; C048826:phaseolin protein, Phaseolus vulgaris