Analysis of Protein Inhibitors of Trypsin in Quinoa, Amaranth and Lupine Seeds. Selection and Deep Structure-Function Characterization of the <i>Amaranthus caudatus</i> Species.

ABSTRACT: Protease inhibitors are biomolecules with growing biotechnological and biomedical relevance, including those derived from plants. This study investigated strong trypsin inhibitors in quinoa, amaranth, and lupine seeds, plant grains traditionally used in Andean South America. Amaranth seeds displayed the highest trypsin inhibitory activity, despite having the lowest content of aqueous soluble and thermostable protein material. This activity, directly identified by enzymatic assay, HPLC, intensity-fading mass spectrometry (IF-MS), and MS/MS, was attributed to a single protein of 7889.1 Da, identified as identical in Amaranthus caudatus and A. hybridus, with a K_i of 1.2 nM for the canonical bovine trypsin. This form of the inhibitor, which is highly homogeneous

SUBMITTER: Hernandez de la Torre M 

PROVIDER: S-EPMC11817793 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature