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LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS

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Author(s): NEVES Valdir A. | LOURENÇO Euclides J.

Journal: Ciência e Tecnologia de Alimentos
ISSN 0101-2061

Volume: 18;
Issue: 3;
Start page: 346;
Date: 1998;
Original page

Keywords: Lens culinaris | lentil | tannin | globulin | in vitro hydrolysis

ABSTRACT
Protein fractions were isolated from lentil cotyledons and tannins were isolated and purified from lentil seed coats. The globulin fraction corresponded to 42.7% of the total lentil flour nitrogen, representing the major protein fraction. Acetone:water (7:3) was the best extractant for seed coat tannins compared to methanol or methanol-HCl 1%. Native and heated (99oC/15 min.) isolated lentil globulin and casein were hydrolyzed with trypsin and pepsin in the absence of tannins and at 1:40, 1:20, 1:10, 1:5 and 1:2.5 tannin-to-protein ratios. The tryptic and peptic hydrolysis of the unheated proteins were reduced with increasing tannin-to-protein ratios. Unheated casein showed to be more susceptible to trypsin than globulin and the opposite effect was observed with pepsin. Heating followed by tannin interaction and hydrolysis had a more pronounced effect on tryptic than peptic digestion for both proteins.
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