Comparative effects of limited tryptic hydrolysis on physicochemical and structural features of seed 11S globulins

Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro

“…This conclusion was definitely confirmed by the X-ray determination of the 3D structure of A 1a B 1b and A 3 B 4 subunits of glycinin (Adachi, Takenaka, Gidamis, Mikami, & Utsumi, 2001;Adachi et al, 2003). Due to high content of basic amino acid residues, A-chains and especially their disordered C-terminal segment, located in the outer part of macromolecules, are especially susceptible to trypsin action (Braudo et al, 2006). The results in this study were consistent with those reports.…”

“…This might ensure the premise of hydrolysis. Trypsin has a well-defined specificity, cleaving next to the hydrophilic amino acids (Barrett, Rawlings, & Woessner, 2004) or basic amino acid residues (Braudo et al, 2006) at the P 1 position. Based on the prediction of the secondary structure of polypeptide chains (Bassüner & Finkelstein, 1986) and the data of the small-angle X-ray analysis (Plietz, Drescher, & Damaschun, 1987), it was suggested that the B-chains are buried in the interior, while the A-chains and especially their disordered segment are located in the outer part of macromolecules.…”

Functionalisation of pea protein by tryptic hydrolysis – Characterisation of interfacial and functional properties

“…As the convicilin peak (SDS-PAGE) fully disappeared, it is concluded that convicilin was fully digested to small peptides. Tryptic attack on pea legumin starts at the Cterminus of the α-chain, (Braudo, et al 2006) and thus exposes the hydrophobic β-chain and generates a variety of small peptides carrying a high density of charged side chains. It is also known that with limited hydrolysis legumin-T, a very ordered structure (M=200±50 kDa (Plumb, Carr, Newby, & Lambert, 1989)) with a nearly intact tertiary structure and improved techno-functional properties (Krause & Schwenke, 1995;Ochiai et al 1982) remains.…”

“…In the present study it is concluded, that the fractions involved in the aggregation and decrease of solubility at pH-values away from the isoelectric point must consist of more basic than acidic amino acids. Trypsin hydrolysis was carried out at pH 8 and cleavage occurred at the C-terminus of basic amino acids (Braudo et al 2006). Therefore, it is likely that small, mainly basic peptides from legumin may be close to their isoelectric points and aggregate.…”

“…Both, hydrophobic and electrostatic interactions can influence film formation. Assuming an increasing hydrophobicity after hydrolysis (Braudo et al 2006), especially at pH 7, the ratio between charge and hydrophobicity will shift. In PPC at pH 7, electrostatic repulsion was strong but hydrophobic attraction would have been low, changing to low electrostatic repulsion with low hydrophobicity at pH 5 and higher hydrophobicity and strong electrostatic repulsion at pH 4.…”