Preparation, characterization and in vitro stability of iron-chelating peptides from mung beans

Mung bean protein was enzymatically hydrolyzed with either alcalase, neutral protease, or papain. The mung bean protein hydrolysates (MPH) showed good ability to chelate ferrous ions, and the chelates had high stability in vitro. The hydrolysates prepared by alcalase showed the highest degree of hydrolysis and the highest ferrous chelating rate. Single factor tests showed that the pH and the material ratio had significant effects on ferrous chelating rates. The optimal MPH to FeCl2 center dot 4H(2)O material ratio was 8:1 (w/w) and the optimal pH of the reaction was 7.0, which yielded a chelating rate of 96.19 +/- 0.94%. The fraction 3 with the highest ferrous chelating activity up to 61.25 +/- 1.02 mu g/mg was obtained from MPH by affinity chromatography. Meanwhile, the MPH-Fe complex had higher digestive stability than just MPH in both in vitro and acid-alkali tolerance assays. The characterization results showed that ferrous ions mainly combined with the amino, carboxyl, imidazole and other chelating active groups in mung bean peptides to form peptide-iron chelates. Scanning electron microscopy (SEM) analysis showed that mung bean peptide chelated ferrous ions to form polymer particles. These results provided insight into ways to develop functional foods such as iron-fortified cereals.

Automated summary

This study demonstrates that enzymatically hydrolyzed mung bean protein possesses good ability to chelate ferrous ions, with the potential for high chelation rates through adjustment of reaction conditions. Meanwhile, affinity chromatography can be utilized to obtain fractions with high chelating activity, and the synthesized chelates exhibit high digestive stability both in vitro and in acid-alkali tolerance assays.