Alpha-lactalbumin: A new carrier for vitamin D3 food enrichment

Delavari, Behdad; Saboury, Ali Akbar; Atri, Maliheh Sadat; Ghasemi, Ali; Bigdeli, Bahareh; Khammari, Anahita; Maghami, Parvaneh; Moosavi-Movahedi, Ali Akbar; Haertlé, Thomas; Goliaei, Bahram

doi:10.1016/j.foodhyd.2014.10.017

Cited by 134 publications

(55 citation statements)

References 50 publications

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“…After 24 hours of complex formation, the diameter of insulin-VD3 and insulin-VE were 119 nm and 107 nm, respectively and it is much larger than the protein. A nanoparticle of homogenized whey protein and vitamin D3 with similar size (110 nm) and complex of α-lactalbumin with vitamin D3 with similar size (125 nm) were reported recently [52,53]. This change might be the result of encapsulation of α-tocopherol and vitamin D3 in human insulin and also of protein-protein interactions.…”

Section: Dynamic Light Scattering (Dls)supporting

confidence: 54%

“…This change might be the result of encapsulation of α-tocopherol and vitamin D3 in human insulin and also of protein-protein interactions. When vitamins bind with insulin, hydrophobic patches get exposed, enabling hydrophobic interactions between insulin molecules leading to larger insulin complexes [52,54]. Decreasing of insulin dimension from 5.4 nm to 5.0 nm upon interaction with αtocopherol shows that protein compactness and rigidity are increased as CD had shown.…”

Section: Dynamic Light Scattering (Dls)mentioning

confidence: 99%

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Vitamin E induces regular structure and stability of human insulin, more intense than vitamin D3

Soleymani

Saboury

Moosavi-Movahedi

et al. 2016

International Journal of Biological Macromolecules

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Changes in human environment and lifestyle over the last century have caused a dramatic increase in the occurrence of diabetes. Research of past decades illustrated that vitamin D and E have a key role in the improvement of diabetes by reducing oxidative stress, protein glycosylation, insulin resistance and also improving beta cell function. Binding properties and conformational changes of human insulin upon interaction with vitamins D and E (α-tocopherol) were investigated by spectroscopy, differential scanning calorimetry (DSC) and molecular dynamic simulation. Tyrosine fluorescence quenching studies indicates changes in the human insulin conformation in the presence of vitamins. Binding constants of vitamins D and E for human insulin were determined to be 2.7 and 1.5 (×10M) and the corresponding average numbers of binding sites were determined to be 1.3 and 1.2, respectively. Far- and near-UV circular dichroism studies showed that vitamin E can significantly change the secondary and tertiary structures of human insulin via an increase in the content of α-helix structure. Results of DSC showed that both vitamins D and E stabilize the structure of human insulin. Molecular dynamic simulation results indicated that vitamin D decreases the helical and strand structural contents of human insulin, but vitamin E stabilizes more regular secondary structures such as helical and strand structural contents as shown by experimental results.

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Section: Dynamic Light Scattering (Dls)supporting

confidence: 54%

Section: Dynamic Light Scattering (Dls)mentioning

confidence: 99%

Vitamin E induces regular structure and stability of human insulin, more intense than vitamin D3

Soleymani

Saboury

Moosavi-Movahedi

et al. 2016

International Journal of Biological Macromolecules

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“…Encapsulation of VD is needed for dispersing in beverages. Dairy proteins are frequently investigated as a matrix for encapsulation of VD, including casein micelles or sodium caseinate (Markman & Livney, 2012; Semo, Kesselman, Danino, & Livney, 2007), whey protein isolate (Abbasi, Emam‐Djomeh, Mousavi, & Davoodi, 2014), or individual whey proteins such as ß ‐lactoglobulin (Diarrassouba et al., 2015b) and α‐lactalbumin (Delavari et al., 2015). Other researchers have combined coencapsulants with dairy proteins.…”

Section: Introductionmentioning

confidence: 99%

Encapsulation of vitamin D₃ in gum arabic to enhance bioavailability and stability for beverage applications

Lamsen

Wang

D’Souza

et al. 2020

Journal of Food Science

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Delivery of vitamin D3 (VD3) in foods should exhibit desirable physicochemical characteristics and improves absorption. In this study, gum arabic (GA) was investigated as a VD3 carrier to encapsulate VD3. VD3 dissolved in 5 mL ethanol corresponding to 0.3 to 6.0% mass of GA, was blended in 5.0% w/v GA solution, followed by freeze drying. The encapsulation efficiency decreased while loading capacity increased with an increased amount of VD3. At the highest VD3 level, the loading capacity (3.47%) was the highest, and the encapsulation efficiency (61.24%) was satisfactory, and the treatment was further studied. The magnitude of negative zeta‐potential increased from 3.1 to 31.0 mV at pH 2.0 to 7.4. During the 100‐day storage at 3 °C of capsules reconstituted at pH 2.0 to 7.4, the hydrodynamic diameter decreased at all pH conditions, most evident for reduction to 81.3 nm at pH 7.4, and no precipitation was observed, indicating the significance of steric repulsion on capsule stability. Bioaccessibility of VD3 in capsules (95.76%) was significantly higher than the nonencapsulated VD3 (68.98%). The in vivo pharmacokinetic study in Sprague–Dawley rats after a single‐dose of 300 µg VD3 showed the area‐under‐curve of serum 25(OHD) level in 48 hr of the encapsulation treatment was 4.32‐fold of the nonencapsulated VD3 and more than twice higher than the VD3‐GA physical mixture. During 2‐week supplementation of 60 µg VD3/d, rats receiving capsules or physical mixture had 25(OH)D levels of at least 81 ng/mL higher than that of the nonencapsulated VD3 group. The studied encapsulation system holds great potential as a value‐added ingredient to supplement VD3 in beverages with a wide pH range. Practical Application The findings of this study demonstrated the improved dispersion stability and absorption of vitamin D3 after encapsulation in gum arabic. The capsules exhibited good dispersion stability across a pH range between 2.0 and 7.4, showing potential application in beverages. Furthermore, the enhanced absorption of VD3 after encapsulation highlights the nutritional benefits of the studied encapsulation system.

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“…The fraction of the denatured protein, F d , was calculated using the relation 24,39,41 : After normalizing the absorbance of the native and denatured molecules of trypsin, T m of enzyme was obtained.…”

Section: Thermal Stabilitymentioning

confidence: 99%

“…Denaturation curves of trypsin in the absence and presence of spermine are shown in Figure 7. According to this mechanism, the difference in free energy between the folded and unfolded conformation, ∆G°, can be calculated by 39,41 : Thermal denaturation of globular proteins approached a two-state mechanism 42 .…”

Section: Thermal Stabilitymentioning

confidence: 99%

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

et al. 2016

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This work studied the interaction between spermine and trypsin at pH 8.0. The thermal stability of trypsin was investigated in the presence of spermine over a temperature range (from 293 K to 353 K).Additionally, the conformational change of trypsin induced by spermine was analyzed by UV-Vis absorption and fluorescence spectra. The effect of spermine on trypsin activity was studied at 37 °C and pH 8.0, using Tris-HCl as a buffer. The fluorescence spectroscopy results indicated that the binding of spermine to trypsin was a spontaneous binding process. The fluorescence of trypsin was quenched by spermine through the static quenching mechanism. By increasing the concentration of spermine, the thermal stability of trypsin was increased. The quantitative analysis of CD spectra revealed some information regarding the changes in the content of the α-helix and the β-sheet of the trypsin upon binding to spermine. It was also found that by increasing the concentration of spermine, the activity of 2 trypsin was increased. Molecular docking results also revealed the presence of one binding site with a negative value for the Gibbs free energy of the binding of spermine to trypsin. Further, the docking and fluorescence spectroscopy study revealed that van der Waals interactions and hydrogen bonds played a major role in stabilizing the complex. As a result, spermine could be considered as an activator and stabilizer for trypsin.

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Alpha-lactalbumin: A new carrier for vitamin D3 food enrichment

Cited by 134 publications

References 50 publications

Vitamin E induces regular structure and stability of human insulin, more intense than vitamin D3

Vitamin E induces regular structure and stability of human insulin, more intense than vitamin D3

Encapsulation of vitamin D₃ in gum arabic to enhance bioavailability and stability for beverage applications

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

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Alpha-lactalbumin: A new carrier for vitamin D3 food enrichment

Cited by 134 publications

References 50 publications

Vitamin E induces regular structure and stability of human insulin, more intense than vitamin D3

Vitamin E induces regular structure and stability of human insulin, more intense than vitamin D3

Encapsulation of vitamin D3 in gum arabic to enhance bioavailability and stability for beverage applications

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

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Product

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Encapsulation of vitamin D₃ in gum arabic to enhance bioavailability and stability for beverage applications