Effect of pH-shifting on the water holding capacity and gelation properties of mung bean protein isolate.

ABSTRACT

In this study, alkaline pH-shifting modified the globular structure of mung bean protein isolate (MBPI) to form flexible and stretched structures. In contrast, acidic pH-shifting increased the rigidity of MBPI. The increased flexibility (at the level of the secondary structure) and newly exposed intermolecular amino acid groups induced by alkaline pH-shifting improved the water holding capacity and gelation properties of proteins. Specifically, MBPI treated at pH 12 (MP12) showed the most flexible structure and highest water holding capacity and gel formation properties (least gelation concentration). The water-holding capacity of native MBPI increased from 1.56 g/g to 4.81 g/g, and its least gelation concentration decreased from 22 % to 15 % by pH-shifting at pH 12. Furthermore, MP12 formed stronger and more elastic heat-induced gels than native MBPI. We identified significant differences in the structural properties and water holding capacity, and gelation properties of acidic and alkaline pH-shifted MBPI and investigated the gelation properties of MP12 including rheological and morphological analyses. Our findings can facilitate the use of mung beans as a protein source in a wide range of food applications, including plant-based and processed meats.