Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds

Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase and Maillard cross-linking

“…3. A higher value of net titratable charge on a gel would indicate a higher content of acidic groups within the gels (Choi & Ma, 2006). The result indicates that the ribose-induced ''Maillard cross-linking" resulted in a more pronounced charge increase than that of MTGase incubation.…”

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

“…In IEF, all larger proteins of the 13S globulin are visible in the acidic region of the gel. While a minor fraction of the small proteins has pIs of about 6.8 (Radovic and others ), the majority shows pIs of about 8.5 (Choi and Ma ). Choi and others estimated that the secondary structure of the 13S globulin consists of 34.5% β‐sheets, 20.0% β‐turns, 16.0% α‐helices, and 14.4% random coils.…”

Promoting structure formation by high pressure in gluten-free flours

“…Choi and Ma (2006) previously stated that buckwheat globulin, accounting for 70% of total seed proteins, is a hexamer with non-identical monomers that interact non-covalently. Furthermore, each monomer is composed of disulphide-linked large acidic and small basic polypeptides with M w ranging from 32 to 57.5 and 23 to 25.8 kDa, respectively (Choi & Ma, 2006). This is in agreement with the results obtained in this study: most of the buckwheat proteins were extracted by the non-reducing buffer containing urea, which breaks non-covalent bonds.…”

“…In agreement with Funtenberger et al (1997), Schurer et al (2007) stated that the key step in the HP-induced thiol/disulphide-interchange reactions is a nucleophilic attack of a disulphide bond by a RS À e ion, and that if no free thiol groups are present, no effect of HP-treatment can be found. Low levels of free cysteine residues in buckwheat globulins might explain the minor role played by disulphide bonds, as cysteine residues in buckwheat globulin exist as disulphide linkages between the basic and acidic polypeptides rather than as free SH-groups (Choi & Ma, 2006).…”