Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2

Abstract

Glycinin is one of the most abundant storage-protein molecules in soybean seeds and is composed of five subunits (A1aB1b, A1bB2, A2B1a, A3B4 and A5A4B3). A1bB2 was purified from a mutant soybean cultivar containing glycinin composed of only A5A4B3 and A1bB2. , respectively. One, six and six subunits of A1bB2 were estimated to be present in the respective asymmetric units. The threedimensional structure of the A1bB2 hexamer is currently being determined.

Changes in the structure, digestibility and immunoreactivities of glycinin induced by the cross‐linking of microbial transglutaminase following heat denaturation

“…Native glycinin is a hexamer with a molecular mass ranging from 320 kDa to 360 kDa. So far, five major subunits, namely, A1aB1b, A1bB2, A2B1a, A3B4 and A5A4B3, have been characterised, and all of them except A5A4B3 are composed of an acidic subunit (about 38 kDa) and a basic subunit (about 20 kDa) linked together via a disulfide bond (Prak et al, 2013;Li et al, 2016). Basic subunit contains considerably more hydrophobic amino acids and shows weaker allergenicity than acidic subunit does (Yuan et al, 2009).…”