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Daniel Otzen

Using protein-fatty acid complexes to improve vitamin D stability

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Using protein-fatty acid complexes to improve vitamin D stability. / Pedersen, Jannik Nedergaard; Frislev, Henriette Kristina Søster; Pedersen, Jan Skov et al.

In: Journal of Dairy Science, Vol. 99, No. 10, 09.2016, p. 7755–7767.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Pedersen, JN, Frislev, HKS, Pedersen, JS & Otzen, DE 2016, 'Using protein-fatty acid complexes to improve vitamin D stability', Journal of Dairy Science, vol. 99, no. 10, pp. 7755–7767. https://doi.org/10.3168/jds.2016-11343

APA

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S., & Otzen, D. E. (2016). Using protein-fatty acid complexes to improve vitamin D stability. Journal of Dairy Science, 99(10), 7755–7767. https://doi.org/10.3168/jds.2016-11343

CBE

MLA

Pedersen, Jannik Nedergaard et al. "Using protein-fatty acid complexes to improve vitamin D stability". Journal of Dairy Science. 2016, 99(10). 7755–7767. https://doi.org/10.3168/jds.2016-11343

Vancouver

Pedersen JN, Frislev HKS, Pedersen JS, Otzen DE. Using protein-fatty acid complexes to improve vitamin D stability. Journal of Dairy Science. 2016 Sep;99(10):7755–7767. Epub 2016 Jul 27. doi: 10.3168/jds.2016-11343

Author

Pedersen, Jannik Nedergaard ; Frislev, Henriette Kristina Søster ; Pedersen, Jan Skov et al. / Using protein-fatty acid complexes to improve vitamin D stability. In: Journal of Dairy Science. 2016 ; Vol. 99, No. 10. pp. 7755–7767.

Bibtex

@article{e5c964ae982446228977380d724822e8,
title = "Using protein-fatty acid complexes to improve vitamin D stability",
abstract = "Liprotides are complexes between lipids and partially denatured proteins in which the protein forms a stabilizing shell around a fatty acid micelle core. We have previously shown that liprotides stabilize small aliphatic molecules such as retinal and tocopherol by sequestering these molecules in the fatty acid core. This opens up for the use of liprotides to formulate food additives. Here we expand our investigations to the large and bulky molecule vitamin D3 (vitD), motivated by the population-wide occurrence of vitD deficiency. We prepared liprotides using different proteins and fatty acids and evaluated their ability to protect vitD upon exposure to heating or intense UV light. Additionally, the stability of liprotides toward pH, Ca(2+), and BSA was determined. The best results were obtained with liprotides made from α-lactalbumin and oleate. These liprotides were able to completely solubilize vitD, increase the stability toward UV light 9-fold and increase the long-term stability at 37°C up to 1,000-fold. Native α-lactalbumin binds Ca(2+), making Ca(2+) potentially disruptive toward liprotides. However, liprotides prepared by incubation at 80°C were stable toward Ca(2+), in contrast to those made at 20°C. Nevertheless, the fatty acid binding protein BSA reduced the ability of both liprotides to protect vitD; the amount of vitD left after 20 d at 20°C fell from 79 ± 3% in the absence of BSA to 49 ± 4 and 23 ± 3% in the presence of BSA for liprotides made at 80 and 20°C, respectively. Both classes of liprotides were able to release their vitD content, as demonstrated by the transfer of vitD encapsulated in liprotides to phospholipid vesicles. Importantly, liprotides were not stable at pH 6 and below, limiting the useful pH range of the liprotides to >pH 6. Our results indicate that vitD may be encapsulated and stabilized for enrichment of clear beverages at neutral pH to improve the intake and bioavailability of vitD.",
author = "Pedersen, {Jannik Nedergaard} and Frislev, {Henriette Kristina S{\o}ster} and Pedersen, {Jan Skov} and Otzen, {Daniel E}",
note = "Copyright {\textcopyright} 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.",
year = "2016",
month = sep,
doi = "10.3168/jds.2016-11343",
language = "English",
volume = "99",
pages = "7755–7767",
journal = "Journal of Dairy Science",
issn = "0022-0302",
publisher = "Elsevier Inc.",
number = "10",

}

RIS

TY - JOUR

T1 - Using protein-fatty acid complexes to improve vitamin D stability

AU - Pedersen, Jannik Nedergaard

AU - Frislev, Henriette Kristina Søster

AU - Pedersen, Jan Skov

AU - Otzen, Daniel E

N1 - Copyright © 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.

PY - 2016/9

Y1 - 2016/9

N2 - Liprotides are complexes between lipids and partially denatured proteins in which the protein forms a stabilizing shell around a fatty acid micelle core. We have previously shown that liprotides stabilize small aliphatic molecules such as retinal and tocopherol by sequestering these molecules in the fatty acid core. This opens up for the use of liprotides to formulate food additives. Here we expand our investigations to the large and bulky molecule vitamin D3 (vitD), motivated by the population-wide occurrence of vitD deficiency. We prepared liprotides using different proteins and fatty acids and evaluated their ability to protect vitD upon exposure to heating or intense UV light. Additionally, the stability of liprotides toward pH, Ca(2+), and BSA was determined. The best results were obtained with liprotides made from α-lactalbumin and oleate. These liprotides were able to completely solubilize vitD, increase the stability toward UV light 9-fold and increase the long-term stability at 37°C up to 1,000-fold. Native α-lactalbumin binds Ca(2+), making Ca(2+) potentially disruptive toward liprotides. However, liprotides prepared by incubation at 80°C were stable toward Ca(2+), in contrast to those made at 20°C. Nevertheless, the fatty acid binding protein BSA reduced the ability of both liprotides to protect vitD; the amount of vitD left after 20 d at 20°C fell from 79 ± 3% in the absence of BSA to 49 ± 4 and 23 ± 3% in the presence of BSA for liprotides made at 80 and 20°C, respectively. Both classes of liprotides were able to release their vitD content, as demonstrated by the transfer of vitD encapsulated in liprotides to phospholipid vesicles. Importantly, liprotides were not stable at pH 6 and below, limiting the useful pH range of the liprotides to >pH 6. Our results indicate that vitD may be encapsulated and stabilized for enrichment of clear beverages at neutral pH to improve the intake and bioavailability of vitD.

AB - Liprotides are complexes between lipids and partially denatured proteins in which the protein forms a stabilizing shell around a fatty acid micelle core. We have previously shown that liprotides stabilize small aliphatic molecules such as retinal and tocopherol by sequestering these molecules in the fatty acid core. This opens up for the use of liprotides to formulate food additives. Here we expand our investigations to the large and bulky molecule vitamin D3 (vitD), motivated by the population-wide occurrence of vitD deficiency. We prepared liprotides using different proteins and fatty acids and evaluated their ability to protect vitD upon exposure to heating or intense UV light. Additionally, the stability of liprotides toward pH, Ca(2+), and BSA was determined. The best results were obtained with liprotides made from α-lactalbumin and oleate. These liprotides were able to completely solubilize vitD, increase the stability toward UV light 9-fold and increase the long-term stability at 37°C up to 1,000-fold. Native α-lactalbumin binds Ca(2+), making Ca(2+) potentially disruptive toward liprotides. However, liprotides prepared by incubation at 80°C were stable toward Ca(2+), in contrast to those made at 20°C. Nevertheless, the fatty acid binding protein BSA reduced the ability of both liprotides to protect vitD; the amount of vitD left after 20 d at 20°C fell from 79 ± 3% in the absence of BSA to 49 ± 4 and 23 ± 3% in the presence of BSA for liprotides made at 80 and 20°C, respectively. Both classes of liprotides were able to release their vitD content, as demonstrated by the transfer of vitD encapsulated in liprotides to phospholipid vesicles. Importantly, liprotides were not stable at pH 6 and below, limiting the useful pH range of the liprotides to >pH 6. Our results indicate that vitD may be encapsulated and stabilized for enrichment of clear beverages at neutral pH to improve the intake and bioavailability of vitD.

U2 - 10.3168/jds.2016-11343

DO - 10.3168/jds.2016-11343

M3 - Journal article

C2 - 27474981

VL - 99

SP - 7755

EP - 7767

JO - Journal of Dairy Science

JF - Journal of Dairy Science

SN - 0022-0302

IS - 10

ER -