2017
DOI: 10.1016/j.foodchem.2017.03.030
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Antioxidant potential of edible mushroom ( Agaricus bisporus) protein hydrolysates and their ultrafiltration fractions

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Cited by 98 publications
(74 citation statements)
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“…The intensity of high-M w bands was reduced and the major M w bands were below 31 kDa and primarily below 20 kDa, indicating that small molecules were successfully generated during fermentation. 25 …”
Section: Sds-pagementioning
confidence: 99%
“…The intensity of high-M w bands was reduced and the major M w bands were below 31 kDa and primarily below 20 kDa, indicating that small molecules were successfully generated during fermentation. 25 …”
Section: Sds-pagementioning
confidence: 99%
“…The initial product of enzyme hydrolysis is called a protein hydrolysate because it contains several peptides that differ in chain length, amino acid sequence, and bioactive potency (Aluko, ). A common practice in refining protein hydrolysates involves the use of membrane ultrafiltration to separate the peptides into different molecular size fractions (Kimatu et al, ; Saisavoey, Sangtanoo, Reamtong, & Karnchanatat, ). These membrane‐separated peptide fractions may or may not have better bioactive properties than the original protein hydrolysate (Kimatu et al, ).…”
Section: Introductionmentioning
confidence: 99%
“…A common practice in refining protein hydrolysates involves the use of membrane ultrafiltration to separate the peptides into different molecular size fractions (Kimatu et al, ; Saisavoey, Sangtanoo, Reamtong, & Karnchanatat, ). These membrane‐separated peptide fractions may or may not have better bioactive properties than the original protein hydrolysate (Kimatu et al, ). For example, hemp seed peptide fractions had weaker antihypertensive properties than the protein hydrolysate (Girgih, Udenigwe, Li, Adebiyi, & Aluko, ).…”
Section: Introductionmentioning
confidence: 99%
“…Moreover, hydrophobic amino acids can enhance the solubility of protein hydrolysates in lipids, thus increasing their interaction with free radicals (Najafian & Babji, ). Aromatic amino acids (Tyr, Phe) have been credited to enhance the potency of radical scavenging activity by donating protons to stabilize electron‐deficient radicals while retaining their own stability through resonance structures (Kimatu et al., ). Above antioxidant‐related amino acids are rich in ACCH, suggesting that ACCH may have potential antioxidant ability.…”
Section: Resultsmentioning
confidence: 99%
“…ACCH contains hydrophobic amino acids (Ala, Leu, Lys), which confer antioxidant activity to ACCH owing to the abundance of their electrons that can be donated to quench free radicals. Met in ACCH has the ability to donate its sulfur hydrogen and therefore is considered as an efficient radical scavenger (Kimatu et al., ). In addition, EGb showed remarkable antioxidant activity because EGb can terminate the radical chain reaction by donating electrons or protons to the radicals (Li et al., ).…”
Section: Resultsmentioning
confidence: 99%