Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material

Hu, Fangyu; Pan, Fan; Sawano, Yoriko; Makino, Tsukasa; Kakehi, Yuji; Komiyama, Makoto; Kawakami, Hiroshi; Tanokura, Masaru

doi:10.1016/j.idairyj.2008.05.003

Cited by 30 publications

(28 citation statements)

References 13 publications

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“…These results are in accordance with a report of Baker and Baker (2009). It seems that the electrostatic interactions between the LF molecule and the ferric ions for protein stability and iron release are important (Baker and Baker 2004;Hu et al 2008;Sreedhara et al 2010). …”

Section: Resultssupporting

confidence: 92%

“…The two iron (Fe) atoms are surrounded by each lobes; N1, N2 and C1 and C2. Recently Hu et al (2008) proposed a new structural model of holo bLF compared to native bLF. Based on the multiferric Fe-binding they have concluded that while native LF exists as a monomer, the holo form (70 FeLF) exists in a multimeric form, similar to casein micelle.…”

Section: Introductionmentioning

confidence: 99%

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Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins

et al. 2010

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Apo and holo forms of lactoferrin (LF) from caprine and bovine species have been characterized and compared with regard to the structural stability determined by thermal denaturation temperature values (T (m)), at pH 2.0-8.0. The bovine lactoferrin (bLF) showed highest thermal stability with a T (m) of 90 ± 1°C at pH 7.0 whereas caprine lactoferrin (cLF) showed a lower T (m) value 68 ± 1°C. The holo form was much more stable than the apo form for the bLF as compared to cLF. When pH was gradually reduced to 3.0, the T (m) values of both holo bLF and holo cLF were reduced showing T (m) values of 49 ± 1 and 40 ± 1°C, respectively. Both apo and holo forms of cLF and bLF were found to be most stable at pH 7.0. A significant loss in the iron content of both holo and apo forms of the cLF and bLF was observed when pH was decreased from 7.0 to 2.0. At the same time a gradual unfolding of the apo and holo forms of both cLF and bLF was shown by maximum exposure of hydrophobic regions at pH 3.0. This was supported with a loss in α-helix structure together with an increase in the content of unordered (aperiodic) structure, while β structure seemed unchanged at all pH values. Since LF is used today as fortifier in many products, like infant formulas and exerts many biological functions in human, the structural changes, iron binding and release affected by pH and thermal denaturation temperature are important factors to be clarified for more than the bovine species.

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Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins

et al. 2010

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“…The thermal denaturation of Lf has been well studied under many experimental conditions, including different pH values, buffers and concentrations of buffer salts (Abe et al 1991;Kawakami et al 1992). When Lf was heated near its isoelectric point (Table 3), the denaturation temperature (about 65°C) was consistent with that in the literature (Hu et al 2008). We also only observed an iron solubilization capacity in native Lf, which was lost after its thermal denaturation ( Fig.…”

supporting

confidence: 78%

“…In other words, the higher-level structure of denatured Lf could change, forming soluble aggregates. According to the structural model proposed by Hu et al (2008), the surface charge on Lf is responsible for the formation of FeLf. Considering that digested Lf still has an iron-solubilizing capacity (Kawakami et al 1993), HT-Lf could be affected by steric hindrance in the region of Lf involved in iron solubilization.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, the suppressive effects of FeLf on mental stress and menstrual pain have been reported (Yoshise et al 2010a, b). According to the structural model of FeLf, the Fe 3+ -HCO 3 − electrostatic interactions between Lf molecules stabilize the protein molecule, which may facilitate the absorption of iron molecules in vivo (Hu et al 2008). However, the mechanism underlying this iron solubilization is not well understood, although this is required if we are to develop applications for FeLf in the food industry, such as in the formulation of food products or manufacturing processes that include thermal treatments.…”

Section: Introductionmentioning

confidence: 99%

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Native, but not thermally denatured lactoferrin solubilizes iron in the presence of bicarbonate ions

Ueno

Kato

Ueda

et al. 2011

Dairy Science & Technol.

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Lactoferrin (Lf) can solubilize more than a 70-fold molar equivalent of iron in the presence of bicarbonate anions. Iron solubilized by Lf (FeLf) is a useful food product for iron fortification, preventing anaemia with no risk of toxicity. However, the mechanism underlying this iron solubilization is not yet well understood. The objective of this study was to investigate the effects of thermal treatments on the iron-solubilizing capacity of Lf in the presence of sodium bicarbonate. Lf was subjected to thermal treatment at 50-80°C for 10 min, and the Lf heated to over 70°C was precipitated by the addition of Fe(III). No precipitation was observed in FeLf-like mixtures of heated Lf when various other cations were substituted for Fe(III): Cu(II), Zn(II), Mg or Na. The precipitation was related to the degree of thermal denaturation of Lf, accompanied by the formation of high-molecular-weight aggregates as disulphide bonds were established. Transferrin, α-lactalbumin and β-lactoglobulin did not solubilize Fe(III), suggesting that the Fe(III)-solubilizing capacity is characteristic of Lf. In conclusion, native Lf is responsible for iron solubilization in the presence of bicarbonate anions. Owing to the application of native Lf to the manufacture of FeLf, FeLf can improve specific food products by supplementing their iron content.

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Methods to Supplement the Mineral-Containing Proteins

Zhou

2017

Mineral Containing Proteins

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Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material

Cited by 30 publications

References 13 publications

Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins

Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins

Native, but not thermally denatured lactoferrin solubilizes iron in the presence of bicarbonate ions

Methods to Supplement the Mineral-Containing Proteins

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