2010
DOI: 10.1016/j.foodchem.2009.12.016
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Physicochemical and structural characterisation of globulin and albumin from common buckwheat (Fagopyrum esculentum Moench) seeds

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Cited by 35 publications
(36 citation statements)
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References 34 publications
(43 reference statements)
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“…Therefore, the high solubility of albumin suggests that the carbohydrate component may have enhanced protein interactions with water. However, the high PS of the albumin at the acidic pH range may also be due to its high isoelectric point and is similar to data reported for buckwheat albumins (Tang & Wang, 2010).…”
Section: Yield and Protein Solubility (Ps)supporting
confidence: 86%
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“…Therefore, the high solubility of albumin suggests that the carbohydrate component may have enhanced protein interactions with water. However, the high PS of the albumin at the acidic pH range may also be due to its high isoelectric point and is similar to data reported for buckwheat albumins (Tang & Wang, 2010).…”
Section: Yield and Protein Solubility (Ps)supporting
confidence: 86%
“…Since protein-protein interactions are required during gelation, the presence of high levels of hydrophilic sugar moieties encouraging protein-water interactions in the albumin fraction may have contributed to reduced ability to form gels. However, the reduced gelling ability of the albumin may also be due to lower numbers of hydrophobic clusters as previously shown for buckwheat albumin (Tang & Wang, 2010), which could also limit protein-protein interactions.…”
Section: Gelation Capacitymentioning
confidence: 89%
“…Appearance of the 55 kDa polypeptide in the reduced albumin (MMA) suggests the presence of a high molecular weight disulfide-bonded protein that was insoluble in the SDS-only buffer and hence was not detected under the non-reducing condition. The results are similar to those reported for buckwheat albumin where the polypeptides were <20 kDa under non-reducing conditions but resolved as bigger 34 kDa polypeptide under reducing conditions [2]. Table 1 shows that Glx (glutamic acid + glutamine) was the most abundant amino acid in the M. myristica products, which is typical of previous reports for plant seed proteins [2,[23][24][25].…”
Section: Gel Electrophoresissupporting
confidence: 88%
“…In contrast, the albumin (MMA) was composed mainly of low molecular weight polypeptides (<35 kDa). Similar results showing dominance of high molecular weight polypeptides in globulins and low molecular weights in albumins have been reported for African yam bean seed [6], red kidney bean [3], buckwheat [2], and pea [1]. The results suggest that the major proteins in M. myristica are globulins because the polypeptide composition of MMG mirrors those obtained for MMF and MMI.…”
Section: Gel Electrophoresissupporting
confidence: 84%
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