2018
DOI: 10.1016/j.memsci.2018.03.079
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Ultrafiltration performance and recovery of bioactive peptides after fractionation of tryptic hydrolysate generated from pressure-treated β-lactoglobulin

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Cited by 42 publications
(26 citation statements)
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“…Under pressure, the loss of solubility is mainly related to the formation of insoluble high molecular weight protein aggregates due to exposure of hydrophobic residues and/or disulfide bond formation [ 68 , 69 ]. Consequently, during the enzymatic hydrolysis of pressure-treated protein, enzymes break the protein in different ways due to modifications of protein structure since some bonds became inaccessible to the enzymes and, on the contrary, others may be exposed due to conformational changes [ 36 , 70 , 71 ]. Therefore, Alcalase ® hydrolysis of cricket meal pretreated by pressure could generate a different peptide profile that contains more hydrophobic peptides, which could negatively impact hydrolysate solubility.…”
Section: Resultsmentioning
confidence: 99%
“…Under pressure, the loss of solubility is mainly related to the formation of insoluble high molecular weight protein aggregates due to exposure of hydrophobic residues and/or disulfide bond formation [ 68 , 69 ]. Consequently, during the enzymatic hydrolysis of pressure-treated protein, enzymes break the protein in different ways due to modifications of protein structure since some bonds became inaccessible to the enzymes and, on the contrary, others may be exposed due to conformational changes [ 36 , 70 , 71 ]. Therefore, Alcalase ® hydrolysis of cricket meal pretreated by pressure could generate a different peptide profile that contains more hydrophobic peptides, which could negatively impact hydrolysate solubility.…”
Section: Resultsmentioning
confidence: 99%
“…Consequently, and specifically regarding the degree of hydrolysis, the result indicates that HHP treatment might have facilitated the mealworm protein conformational changes that are needed to increase the effectiveness of enzymatic digestion by providing Alcalase ® access to the buried cleavage site at the very beginning of hydrolysis (until 10 min). Previous studies using various enzymes demonstrated that HHP-assisted enzymatic hydrolysis induced the exposure of new cleavage sites through protein unfolding, which enhanced enzyme activity, reduced hydrolysis time [36], and improved the degree of hydrolysis and concentration of peptides generated in protein hydrolysates [37][38][39]. In addition, the DH of mealworm proteins obtained was significantly increased (p < 0.05) during HHP-assisted enzymatic hydrolysis by Alcalase ® .…”
Section: Effects Of High Hydrostatic Pressure-assisted Enzymatic Hydrmentioning
confidence: 92%
“…from rice and Soy) may find their way in the global market [69]. Food industry generally prepares the bioactive peptides with enzymatic hydrolysis using pepsin, trypsin and papain [27] or microbial fermentation [15] and some uses both methods in combination [70]. For integrated approach, most of the researchers generally combine both in vitro and in vivo studies with the in-silico approaches [71,72].…”
Section: Discussionmentioning
confidence: 99%