Binding of proanthocyanidins to soybean (Glycine max) seed ferritin inhibiting protein degradation by protease in vitro

Deng, Jianjun; Li, Meiliang; Zhang, Tuo; Chen, Bin; Leng, Xiaojing; Zhao, Guanghua

doi:10.1016/j.foodres.2010.11.020

Cited by 41 publications

(34 citation statements)

References 26 publications

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“…This represents the first possible mechanism on the inhibition of iron uptake from SSF by PAs. Support for this idea comes from previous studies showed that phytic acid and tannic acid significantly reduced ferrous Fe uptake by Caco-2 cells [17]. On the other hand, partially undigested ferritin may escape from the stomach and into intestine where it was absorbed by the enterocytes via a receptor-mediated mechanism [24,25].…”

Section: Discussionmentioning

confidence: 93%

“…Our recent study showed that PAs from grape seeds, as a class of naturally plant polyphenols, can bind with SSF in a dosedependent manner. Consequently, such binding significantly inhibited the degradation of SSF by the protease(s) in vitro [17]. This may represent an alternative way to improve ferritin iron bioaccessibility in vivo.…”

Section: Discussionmentioning

confidence: 96%

“…Thus, PAs did not exhibit a positive effect on iron uptake from SSF crude by rats through its binding to SSF. Based on in vitro results, it was proposed that most of the ferritin might be degraded at pH 2.0 by pepsin in the stomach [17,23], and iron released from the core is likely taken up by divalent metal transporter-1 (DMT-1) [1,11]. It is possible that the iron released from the core binds to PAs, forming insoluble compounds, and finally resulting in low iron uptake.…”

Section: Discussionmentioning

confidence: 99%

“…PAs from grape seeds were extracted and purified as reported methods [17]. Resulting samples were lyophilized, powdered, and frozen at −80°C until used.…”

Section: Methodsmentioning

confidence: 99%

“…Recently, we have found that PAs from grape seed, a class of naturally occurring active phenols [16], can bind to SSF in a dose-dependent manner [17]. Such binding exhibited a pronounced inhibitory effect for SSF degradation by pepsin at pH 4.0 as well as by trypsin at 7.5.…”

Section: Introductionmentioning

confidence: 99%

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Proanthocyanidins Inhibit Iron Absorption from Soybean (Glycine max) Seed Ferritin in Rats with Iron Deficiency Anemia

Yun

Zhang

et al. 2011

Plant Foods Hum Nutr

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The objective of this study was to evaluate the effect of proanthocyanidins (PAs) on iron uptake from soybean seed ferritin (SSF) crude by rats with iron deficiency anemia (IDA) for the first time. Six groups of Sprague-Dawley (SD) rats (n = 10) were used, which contain (1) SSF crude group; (2) SSF crude + PAs group; (3) PAs group; (4) FeSO(4) group; (5) iron deficiency control group; and (6) control group. The bioavailability of iron was examined by measuring hemoglobin (Hb) concentration value, red blood cell (RBC) numbers, and serum iron stores. After 8 weeks, Hb concentration was almost recovered to the normal level upon feeding SSF crude or FeSO(4) to rats. In contrast, Hb concentration was recovered to less extent when SSF crude plus PAs was used instead of SSF crude alone (P < 0.05). A similar profile was observed with these three sample groups when serum iron and RBC were used as parameters. All rats in PAs group died at the 8th week. Taken together, all these results demonstrated that PAs inhibited iron uptake of rats from SSF, and are toxic for rats with IDA.

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Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

“…PAs from grape seeds were extracted and purified as reported methods [17]. Resulting samples were lyophilized, powdered, and frozen at −80°C until used.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Proanthocyanidins Inhibit Iron Absorption from Soybean (Glycine max) Seed Ferritin in Rats with Iron Deficiency Anemia

Yun

Zhang

et al. 2011

Plant Foods Hum Nutr

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Leguminous ferritin, a natural protein for iron supplementation, Pickering emulsion formation and encapsulation of bioactive molecules

Hang,

Chu,

Chen

2024

J Americ Oil Chem Soc

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Ferritin is a naturally occurring iron storage protein. Leguminous ferritins exhibit unique structural features, including diverse subunit composition and an extension peptide, which contribute to superior thermal stability compared to animal ferritins. The high iron content, remarkable effectiveness, low risk of oxidative damage and thermal stability make the leguminous ferritin an attractive candidate for iron supplementation. Moreover, apoferritin is an excellent nanosized carrier for encapsulating bioactive compounds due to its inherent inner cavity, water solubility, biocompatibility, and reversible self‐assembly behavior. However, the harsh condition during encapsulation by unmodified ferritins may cause damage to sensitive bioactive compounds. Thus, different processing methods are employed to alter the leguminous ferritin structures, including chemical, enzymatic, mild heat treatments, and nonthermal processing to achieve gentler encapsulation conditions for a wide range of bioactive compounds. Another challenge is to improve the stability of leguminous ferritin to withstand gastric digestion. The degradation of ferritin by proteases may lead to premature release of bioactive compounds. Recent works demonstrated that certain phenolic compounds such as proanthocyanidin‐induced protein association, thereby enhancing digestive stability of ferritins, leading to a sustained release and a potentially greater bioavailability of bioactive compounds. Leguminous ferritin also has the potential to serve as a stabilizer for the Pickering emulsion, where the hydrophilic and hydrophobic compounds can be encapsulated in the ferritin nanocages and oil phase, respectively. The release and absorption of bioactive compounds in encapsulates and emulsions will need to be further demonstrated through in vivo studies.

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Characterization of intermolecular interaction between cyanidin‐3‐glucoside and bovine serum albumin: Spectroscopic and molecular docking methods

et al. 2013

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The intermolecular interaction between cyanidin-3-glucoside (Cy-3-G) and bovine serum albumin (BSA) was investigated using fluorescence, circular dichroism and molecular docking methods. The experimental results revealed that the fluorescence quenching of BSA at 338 nm by Cy-3-G resulted from the formation of Cy-3-G-BSA complex. The number of binding sites (n) for Cy-3-G binding on BSA was approximately equal to 1. The experimental and molecular docking results revealed that after binding Cy-3-G to BSA, Cy-3-G is closer to the Tyr residue than the Trp residue, the secondary structure of BSA almost not change, the binding process of Cy-3-G with BSA is spontaneous, and Cy-3-G can be inserted into the hydrophobic cavity of BSA (site II') in the binding process of Cy-3-G with BSA. Moreover, based on the sign and magnitude of the enthalpy and entropy changes (ΔH(0) = - 29.64 kcal/mol and ΔS(0) = - 69.51 cal/mol K) and the molecular docking results, it can be suggested that the main interaction forces of Cy-3-G with BSA are Van der Waals and hydrogen bonding interactions.

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Binding of proanthocyanidins to soybean (Glycine max) seed ferritin inhibiting protein degradation by protease in vitro

Cited by 41 publications

References 26 publications

Proanthocyanidins Inhibit Iron Absorption from Soybean (Glycine max) Seed Ferritin in Rats with Iron Deficiency Anemia

Proanthocyanidins Inhibit Iron Absorption from Soybean (Glycine max) Seed Ferritin in Rats with Iron Deficiency Anemia

Leguminous ferritin, a natural protein for iron supplementation, Pickering emulsion formation and encapsulation of bioactive molecules

Characterization of intermolecular interaction between cyanidin‐3‐glucoside and bovine serum albumin: Spectroscopic and molecular docking methods

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