2019
DOI: 10.1016/j.foodchem.2018.08.137
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Release of antioxidant peptides from buffalo and bovine caseins: Influence of proteases on antioxidant capacities

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Cited by 53 publications
(32 citation statements)
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“…Furthermore, the pyrrole and hydroxyl groups of MRPs, through their redox potential of transferring electrons, have a vital role in the process of ferrous reduction. This was in line with the opinions of Shazly et al [44], who reported that there could be a higher reducing power for glucose–glycine MRPs as the heating time increased. The ferrous reducing activity of a porcine hemoglobin hydrolysate–sugar model system was about four times higher than that of individual hydrolysate [3].…”
Section: Resultssupporting
confidence: 92%
“…Furthermore, the pyrrole and hydroxyl groups of MRPs, through their redox potential of transferring electrons, have a vital role in the process of ferrous reduction. This was in line with the opinions of Shazly et al [44], who reported that there could be a higher reducing power for glucose–glycine MRPs as the heating time increased. The ferrous reducing activity of a porcine hemoglobin hydrolysate–sugar model system was about four times higher than that of individual hydrolysate [3].…”
Section: Resultssupporting
confidence: 92%
“…Hydrolysates prepared using trypsin had the highest ABTS + RSA with 267 µmol trolox eq/g sample, while flavourzyme hydrolysates showed the lowest values (167 µmol trolox eq/g sample) (Figure 3b). The similar results were observed by Shazly et al (2019) on higher ABTS + RSA of buffalo and bovine caseins hydrolysates of trypsin than alcalase, papain, and pepsin. Hydrolysates prepared using flavourzyme showed the highest OH RSA (289 µmol histidine eq/g sample), while trypsin and alcalase hydrolysates significantly had the lower activity (Figure 3c).…”
Section: Resultssupporting
confidence: 89%
“…While trypsin cleaves exclusively C‐terminal to arginine and lysine (Ambigaipalan, Al‐Khalifa, & Shahidi, 2015; Wang et al, 2019), this result indicates that alcalase is the most efficient for corn germ protein hydrolysis. Similar results were obtained for whey protein (Lin, Tian, Li, Cao, & Jiang, 2012), rapeseed protein (He et al, 2013), camel milk casein (Kumar et al, 2016), hemp seed protein (Ren et al, 2016), quinoa and amaranth proteins (Lina, Omar, Kamal, Kilari, & Maqsood, 2019), and buffalo and bovine caseins (Shazly et al, 2019). DH could be effect on functionality and bioactive properties of hydrolysate, so it is important to control DH in production of new food products (Mudgil, Omar, Kamal, Kilari, & Maqsood, 2019).…”
Section: Resultssupporting
confidence: 61%
“…The behaviour of pepsin, however, was somewhat unexpected. This enzyme is considered to be of low specificity and tends to be less effective than Alcalase (Shazly et al, 2019). In this case, the higher yield and faster hydrolysis achieved by the use of pepsin may be credited to the predominant presence of peptide bonds susceptible to hydrolysis by this enzyme (involving hydrophobic amino acids) in the most abundant egg white proteins (e.g.…”
Section: Pepsinmentioning
confidence: 99%