Hydrophobicity exerts different effects on bioavailability and stability of antioxidant peptide fractions from casein during simulated gastrointestinal digestion and Caco-2 cell absorption

Xie, Na; Wang, Bo; Jiang, Liangping; Liu, Congcong; Лі, Бо

doi:10.1016/j.foodres.2015.06.025

Cited by 78 publications

(51 citation statements)

References 36 publications

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“…Using three enzymes, the resulting product was a polymer with high MW, which was in agreement with previous studies and showed that the treatment of peanut proteins with tyrosinase/caffeic acid and TG led to the formation of cross‐linked proteins of high MW . Our findings were similar to many studies on cross‐linked dietary products and showed that materials of high MW could be obtained, which further influenced their allergenicity .…”

Section: Discussionsupporting

confidence: 91%

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Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Fei

Liu

Chen

et al. 2016

Molecular Nutrition Food Res

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Section: Discussionsupporting

confidence: 91%

“…The difference in digestibility of CL‐pAK may be caused by the formation of the polymer. In two recently published studies, a positive correlation was found between hydrophobicity and digestion . CL‐pAK was noted to be more hydrophobic than AK.…”

Section: Discussionmentioning

confidence: 88%

Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Fei

Liu

Chen

et al. 2016

Molecular Nutrition Food Res

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“…In addition, charge is another factor affecting the bioavailability. Negative and hydrophobic casein‐derived peptides showed a higher bioavailability (Xie et al ., ; Wang & Li, ).…”

Section: Factors That Influence the Bioavailability Of Dbpsmentioning

confidence: 99%

Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Yan

Zhang

et al. 2018

Int J of Food Sci Tech

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Summary Dairy protein‐derived bioactive peptides (DBPs) have potential benefits for human health. However, their transport mechanisms and bioavailability from intestinal lumen to bloodstream are not well understood. This review summarises current understanding of their transport mechanisms across the intestinal membrane (peptide transport 1, paracellular route, transcytosis and passive transcellular diffusion) and the bioavailability of DBPs in animal and human studies. Some DBPs can escape the degradation of peptidase and reach the bloodstream at concentrations of micromolar range, and keep intact for several minutes to hours. The presences of brush‐border peptidases at the site of absorption and other peptidases in the blood, along with the peptide properties, such as molecular size and weight, stability to proteases, hydrophobicity and charge, determine their bioavailability. Developing novel analytical tools for accurate measurement and study of the transport, metabolism, and bioavailability of DBPs in vivo are expected.

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“…(). In addition, Caco‐2 cells have been used to investigate the signal transduction pathways of peptides across the plasma membrane (Mine et al ., ; Xie et al ., ).…”

Section: Introductionmentioning

confidence: 97%

“…The relationship between the permeability of Caco-2 cell monolayer and the absorption in animal intestines was discussed by Artursson et al (2012). In addition, Caco-2 cells have been used to investigate the signal transduction pathways of peptides across the plasma membrane (Mine et al, 2015;Xie et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

The antioxidant activity and transcellular pathway of Asp‐Leu‐Glu‐Glu in a Caco‑2 cell monolayer

Xing

Tang

et al. 2018

Int J of Food Sci Tech

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Summary Asp‐Leu‐Glu‐Glu (DLEE) is one of the antioxidant peptides purified from Chinese dry‐cured Xuanwei ham in our previous study. In the current work, the stability in a simulated digestion system, the transportation pathway and the antioxidant ability of DLEE were further investigated in a Caco‐2 cell monolayer. In the simulated gastrointestinal digestion system, no oligopeptides were generated. In the transport trial, the inhibitors cytochalasin D increased the transport of DLEE across the Caco‐2 cell monolayer, with Papp values of 3.22 × 10−6 cm s−1. A decreased expression occludin was observed with the DLEE incubation in the cell monolayer, and the antioxidant activity showed to be increased gradually in basolateral side. This study indicates that the absorption of DLEE could mainly occur via paracellular transport and provides information about its antioxidant activity after being absorbed across a cell monolayer.

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Hydrophobicity exerts different effects on bioavailability and stability of antioxidant peptide fractions from casein during simulated gastrointestinal digestion and Caco-2 cell absorption

Cited by 78 publications

References 36 publications

Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

The antioxidant activity and transcellular pathway of Asp‐Leu‐Glu‐Glu in a Caco‑2 cell monolayer

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