2017
DOI: 10.1016/j.lwt.2017.06.021
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In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments

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Cited by 64 publications
(38 citation statements)
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“…This kind of resistance could be explained by the low hydrophobicity of pea globulins at their native state (Gueguen, ), which makes them inaccessible to pepsin. The same trend has been encountered by Laguna et al (), who observed persistence of vicilin and convicilin bands during the gastric phase for more than 120 min in pea protein‐fortified fruit puree. The FSC gel pattern (Figure b) also shows the characteristic pea protein bands at t = 0.…”
Section: Resultssupporting
confidence: 84%
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“…This kind of resistance could be explained by the low hydrophobicity of pea globulins at their native state (Gueguen, ), which makes them inaccessible to pepsin. The same trend has been encountered by Laguna et al (), who observed persistence of vicilin and convicilin bands during the gastric phase for more than 120 min in pea protein‐fortified fruit puree. The FSC gel pattern (Figure b) also shows the characteristic pea protein bands at t = 0.…”
Section: Resultssupporting
confidence: 84%
“…Contrary to what is observed for PP, vicilin bands seem to resist the gastric digestion and disappear only at the end of the intestinal phase. The persistence of vicilin bands after heat treatment had been previously reported (Laguna et al, ), but they disappeared almost instantaneously after applying a high‐pressure treatment, causing the denaturation of the proteins, which resisted thermal treatment. In fact, it is generally agreed that protein denaturation improves the enzymatic hydrolysis of amino acids (Fennema, ).…”
Section: Resultsmentioning
confidence: 51%
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“…It is known that proteins' digestion kinetics may be influenced by different factors including processing conditions, pH during processing and interactions with other components present in the food matrix. Recently, the influence of pH and processing conditions on the digestibility of pea protein isolate have been investigated (Laguna, Picouet, Guàrdia, Renard, & Sarkar, 2017). These authors found that HHP processing enhanced the degree and rate of proteolysis, which can be attributed to globular pea protein subunits unfolding.…”
Section: Digestibilitymentioning
confidence: 99%
“…The increased of smaller peptides during gastric digestion also was found by Laguna et al (2017). Reduced SDS-PAGE showed that during gastric digestion the molecules smaller than 15 kDa increased.…”
Section: Size-exclusion Chromatography (Hpsec) Analysismentioning
confidence: 69%