2011
DOI: 10.1016/j.foodchem.2011.05.026
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Glycosylation, amino acid analysis and kinetic properties of a major Kunitz-type trypsin inhibitor from Acacia victoriae Bentham seeds

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Cited by 9 publications
(8 citation statements)
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“…Conversely, the low antioxidant activity of PIs, including that from wattle seed, could be due to the globular nature of the seed protein where the hydrophobic side chains of aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and histidine, were not usually exposed. Furthermore, the low level of aromatic amino acids in AvTI, as reported in our previous study (Ee et al. , 2011b), was possibly another negative factor for the antioxidant properties.…”
Section: Resultssupporting
confidence: 62%
See 1 more Smart Citation
“…Conversely, the low antioxidant activity of PIs, including that from wattle seed, could be due to the globular nature of the seed protein where the hydrophobic side chains of aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and histidine, were not usually exposed. Furthermore, the low level of aromatic amino acids in AvTI, as reported in our previous study (Ee et al. , 2011b), was possibly another negative factor for the antioxidant properties.…”
Section: Resultssupporting
confidence: 62%
“…2), these biological analyses were not performed on roasted samples. The relatively low versatility of the wattle seed extracts in terms of their biological activities may be related to the low diversity of the phenolic constituents, as our previous study showed that phenolics in wattle seed were dominated by two phenolic acids, namely succinic and gallic acids (Ee et al. , 2011b).…”
Section: Resultsmentioning
confidence: 99%
“…However, there are reports of trypsin inhibitors with covalently linked carbohydrates to their structures. For example, the trypsin inhibitor from Acacia victoriae (AvTI) has a glycosylation degree of 2.06% (Ee et al, 2011). The protease inhibitors of Echinodorus paniculatus (Paiva et al, 2003) and Peltophorum dubium (Macedo et al, 2003) are all glycosylated proteins.…”
Section: Assessment Of the Glycoprotein Nature And Amino-terminal Anamentioning
confidence: 99%
“…However, the most widely studied is the serine protease inhibitors, which are grouped into 18 families based on their primary and three-dimensional structures, and mechanism of inhibition . Furthermore, plant serine protease inhibitors are divided into Kunitz, Bowman–Birk, Potato I, Potato II, and Squash families based mainly on their primary structure. , Generally, Bowman–Birk inhibitors are proteins of 8–10 kDa and have seven disulfide bonds and two independent reactive domains, one for trypsin and the other for chymotrypsin …”
mentioning
confidence: 99%