Group Of Plant Proteins Research Articles

Hydrogenation as an approach to study of reactions of oxidizing polyphenols with plant proteins

Coupling of oxidation products of o-diphenols with -NH2 groups of plant proteins can damage nutritional availability of lysine residues. Relevant model coupling products (before or after reductive acetylation or permethylation) are unstable to acid hydrolysis. Hydrogenation over Rh/Al2O3, at room temperature and atmospheric pressure, gave cyclohexane derivatives stable to hydrolysis and retaining, with only partial hydrogenolysis, all groups originally attached to the aromatic nucleus. Plant bulk proteins were hydrogenated with substantial conversion of their aromatic amino acids; their S-containing amino acids were desulphurized. The technique is therefore promising for study of the fate of lysine residues in “enzymically browned” proteins.

Lectins: a chemical approach to the cell surface

Abstract