Browsing by Subject "ELLA"

Faba bean (Vicia faba L.) is a healthy and ecological pulse crop. Nevertheless, it contains antinutritive compounds, including lectins. Lectins are proteins or glycoproteins that bind to carbohydrates. Faba bean lectin is called favin and it binds specifically to mannose- and glucose-like carbohydrates. Agglutinatination assays have been traditionally used for the determination of lectins. These assays are, however, often inaccurate. The aim of this study was to adapt and optimize a method for the quantification of faba bean lectin and analyze lectin levels in untreated and treated faba beans. Enzyme-Linked Lectin Assay (ELLA), which is based on the ability of lectins to bind to specific carbohydrates, was adapted in the study. The hypothesis was that the method is suitable for the quantification of faba bean lectin. The commercial lectin standard did not react in the assay and thus the quantification of lectins was not possible. The faba bean samples, however, reacted and the absorbance values of varying samples were compared. The protein-rich faba bean fractions gave the highest absorbance values. Particle size affected the determination of lectins. Heating was efficient in lowering the absorbance values. Long-time roasting and boiling were the most efficient methods to reduce the binding capability of lectins.