FREE SHIPPING over $40
OVER 10000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Journal of dairy science1995; 78(5); 978-988; doi: 10.3168/jds.S0022-0302(95)76713-3

Interaction of beta-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review.

Abstract: beta-Lactoglobulin is the major whey protein in the milk of ruminants and some nonruminants, such as pigs and horses. Although beta-lactoglobulin was first isolated 60 yr ago, no function has been definitely ascribed to beta-lactoglobulin. Recent x-ray crystallographic studies have advanced knowledge of the structure of beta-lactoglobulin, which is homologous with that of retinol-binding protein and lipocalycins; the function of these proteins seems to be participation in the transport of small hydrophobic substances. By analogy, this protein has been suggested as having a role as a transporter of fatty acids and retinol. This review reassesses the function of beta-lactoglobulin in light of the large amount of information that has accrued in the last few years. In particular, this review concentrates upon studies of the binding of retinol and fatty acids to beta-lactoglobulin, including the binding constants and number of binding sites, the location of the binding sites, and the influence of chemical modifications in the interaction of the protein with both ligands. This study also describes studies of the influence of beta-lactoglobulin on several biological processes that may be relevant to the possible biological role of this protein.
Get Full Text
Publication Date: 1995-05-01 PubMed ID: 7622732DOI: 10.3168/jds.S0022-0302(95)76713-3Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Review

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research study reviews the role of beta-lactoglobulin, a major whey protein found in ruminants’ milk and some non-ruminants like pigs and horses. It explores the protein’s potential function as a transporter of retinol and fatty acids, focusing on how it binds with these substances and its possible influence on biological processes.

Background on Beta-Lactoglobulin

  • Beta-lactoglobulin is a significant whey protein found in ruminants’ milk, such as cows, and some non-ruminants, like pigs and horses.
  • Despite its discovery over six decades ago, there is still no definitive function assigned to this protein, making it an active subject of study in the scientific community.
  • The structure of beta-lactoglobulin, as revealed through recent x-ray crystallographic studies, correlates with that of retinol-binding protein and lipocalycins, giving rise to hypotheses about its purpose.

Function as a Transporter of Retinol and Fatty Acids

  • Considering its structural similarity with other proteins like retinol-binding protein and lipocalycins, beta-lactoglobulin is believed to have a role as a transporter of smaller hydrophobic substances.
  • Through this analogy, researchers propose that beta-lactoglobulin might contribute to the transportation of retinol and fatty acids.
  • This review reassesses this potential role of beta-lactoglobulin as a transporter by compiling and examining the vast amount of information obtained over the past few years.

Binding of Retinol and Fatty Acids to Beta-Lactoglobulin

  • One critical focus of the review is to study the relation of beta-lactoglobulin with retinol and fatty acids, particularly in how it attaches to these substances.
  • It analyses the binding constants and the number of binding sites, as well as the physical locations of these binding sites on the protein molecule.
  • The review further examines how chemical modifications can alter the interaction of the protein with both ligands.

Impact on Biological Processes

  • Apart from being a possible transporter, this review explores how beta-lactoglobulin might influence various biological processes.
  • These potential influences could offer more insights into the biological role of this protein, further enhancing our understanding of its functions within the body.

Cite This Article

APA
Pérez MD, Calvo M. (1995). Interaction of beta-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J Dairy Sci, 78(5), 978-988. https://doi.org/10.3168/jds.S0022-0302(95)76713-3

Publication

Journal of dairy science
ISSN: 0022-0302
NlmUniqueID: 2985126R
Country: United States
Language: English
Volume: 78
Issue: 5
Pages: 978-988

Researcher Affiliations

Pérez, M D
  • Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Zaragoza, Spain.
Calvo, M

    MeSH Terms

    • Animals
    • Fatty Acids / metabolism
    • Lactoglobulins / physiology
    • Ruminants
    • Vitamin A / metabolism

    Citations

    This article has been cited 22 times.
    1. Reiter AS, Reed SA. Lactation in horses. Anim Front 2023 Jun;13(3):96-100.
      doi: 10.1093/af/vfad003pubmed: 37324210google scholar: lookup
    2. Zhuo X, Margrethe Brekstad Kjellin M, Schaal Z, Zhang T, Löbmann K, Leng D. A Comparative Study between A Protein Based Amorphous Formulation and Other Dissolution Rate Enhancing Approaches: A Case Study with Rifaximin. Pharmaceutics 2022 Dec 30;15(1).
      doi: 10.3390/pharmaceutics15010126pubmed: 36678757google scholar: lookup
    3. Stobiecka M, Król J, Brodziak A. Antioxidant Activity of Milk and Dairy Products. Animals (Basel) 2022 Jan 20;12(3).
      doi: 10.3390/ani12030245pubmed: 35158569google scholar: lookup
    4. Puppel K, Staniszewska P, Gołębiewski M, Slósarz J, Grodkowski G, Solarczyk P, Kunowska-Slósarz M, Kostusiak P, Kuczyńska B, Przysucha T. Using the Relationship between Concentrations of Selected Whey Proteins and BHBA to Characterize the Metabolism of Dairy Cows in Early Lactation. Animals (Basel) 2021 Aug 4;11(8).
      doi: 10.3390/ani11082298pubmed: 34438755google scholar: lookup
    5. Sawyer L. β-Lactoglobulin and Glycodelin: Two Sides of the Same Coin?. Front Physiol 2021;12:678080.
      doi: 10.3389/fphys.2021.678080pubmed: 34093238google scholar: lookup
    6. Gutiérrez-Peña R, Avilés C, Galán-Soldevilla H, Polvillo O, Ruiz Pérez-Cacho P, Guzmán JL, Horcada A, Delgado-Pertíñez M. Physicochemical Composition, Antioxidant Status, Fatty Acid Profile, and Volatile Compounds of Milk and Fresh and Ripened Ewes' Cheese from a Sustainable Part-Time Grazing System. Foods 2021 Jan 3;10(1).
      doi: 10.3390/foods10010080pubmed: 33401637google scholar: lookup
    7. Çakır B, Okuyan B, Şener G, Tunali-Akbay T. Investigation of beta-lactoglobulin derived bioactive peptides against SARS-CoV-2 (COVID-19): In silico analysis. Eur J Pharmacol 2021 Jan 15;891:173781.
      doi: 10.1016/j.ejphar.2020.173781pubmed: 33271151google scholar: lookup
    8. Crowther JM, Broadhurst M, Laue TM, Jameson GB, Hodgkinson AJ, Dobson RCJ. On the utility of fluorescence-detection analytical ultracentrifugation in probing biomolecular interactions in complex solutions: a case study in milk. Eur Biophys J 2020 Dec;49(8):677-685.
      doi: 10.1007/s00249-020-01468-3pubmed: 33052462google scholar: lookup
    9. Morammazi S, Masoudi AA, Vaez Torshizi R, Pakdel A. Differential Expression of the Alpha S1 Casein and Beta-Lactoglobulin Genes in Different Physiological Stages of the Adani Goats Mammary Glands. Iran J Biotechnol 2016 Dec;14(4):278-285.
      doi: 10.15171/ijb.1171pubmed: 28959346google scholar: lookup
    10. Tai CS, Chen YY, Chen WL. β-Lactoglobulin Influences Human Immunity and Promotes Cell Proliferation. Biomed Res Int 2016;2016:7123587.
      doi: 10.1155/2016/7123587pubmed: 27957499google scholar: lookup
    11. Villa TG, Feijoo-Siota L, Rama JLR, Ageitos JM. Antivirals against animal viruses. Biochem Pharmacol 2017 Jun 1;133:97-116.
      doi: 10.1016/j.bcp.2016.09.029pubmed: 27697545google scholar: lookup
    12. Selvaggi M, Laudadio V, Dario C, Tufarelli V. Major proteins in goat milk: an updated overview on genetic variability. Mol Biol Rep 2014 Feb;41(2):1035-48.
      doi: 10.1007/s11033-013-2949-9pubmed: 24381104google scholar: lookup
    13. Reboul E. Absorption of vitamin A and carotenoids by the enterocyte: focus on transport proteins. Nutrients 2013 Sep 12;5(9):3563-81.
      doi: 10.3390/n傓563pubmed: 24036530google scholar: lookup
    14. Sardina MT, Rosa AJ, Davoli R, Braglia S, Portolano B. Polymorphisms of beta-lactoglobulin promoter region in three Sicilian goat breeds. Mol Biol Rep 2012 Mar;39(3):3203-10.
      doi: 10.1007/s11033-011-1087-5pubmed: 21701825google scholar: lookup
    15. Mastrangelo S, Sardina MT, Riggio V, Portolano B. Study of polymorphisms in the promoter region of ovine β-lactoglobulin gene and phylogenetic analysis among the Valle del Belice breed and other sheep breeds considered as ancestors. Mol Biol Rep 2012 Jan;39(1):745-51.
      doi: 10.1007/s11033-011-0794-2pubmed: 21567200google scholar: lookup
    16. Niavarani A, Dehghanizadeh S, Zeinali S, Karimi M, Magliano M, Rassoulzadegan M. Development of transgenic mice expressing calcitonin as a beta-lactoglobulin fusion protein in mammary gland. Transgenic Res 2005 Oct;14(5):719-27.
      doi: 10.1007/s11248-005-7217-xpubmed: 16245163google scholar: lookup
    17. Ragona L, Fogolari F, Zetta L, Pérez DM, Puyol P, De Kruif K, Löhr F, Rüterjans H, Molinari H. Bovine beta-lactoglobulin: interaction studies with palmitic acid. Protein Sci 2000 Jul;9(7):1347-56.
      doi: 10.1110/ps.9.7.1347pubmed: 10933500google scholar: lookup
    18. Uhrínová S, Uhrín D, Denton H, Smith M, Sawyer L, Barlow PN. Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form. J Biomol NMR 1998 Jul;12(1):89-107.
      doi: 10.1023/a:1008268528695pubmed: 9729790google scholar: lookup
    19. Rocha TL, Paterson G, Crimmins K, Boyd A, Sawyer L, Fothergill-Gilmore LA. Expression and secretion of recombinant ovine beta-lactoglobulin in Saccharomyces cerevisiae and Kluyveromyces lactis. Biochem J 1996 Feb 1;313 ( Pt 3)(Pt 3):927-32.
      doi: 10.1042/bj3130927pubmed: 8611177google scholar: lookup
    20. Yang X, Zhang L, Zheng Z, Langer R, Jaklenec A. Advanced Oral Delivery Systems for Nutraceuticals. Adv Healthc Mater 2025 Dec;14(31):e2500271.
      doi: 10.1002/adhm.202500271pubmed: 40500936google scholar: lookup
    21. Puppel K, Slósarz J, Solarczyk P, Grodkowski G, Kostusiak P, Kalińska A, Balcerak M, Kunowska-Slósarz M, Gołębiewski M. Assessing the Usefulness of Interleukin-8 as a Biomarker of Inflammation and Metabolic Dysregulation in Dairy Cows. Int J Mol Sci 2024 Oct 16;25(20).
      doi: 10.3390/ijms252011129pubmed: 39456911google scholar: lookup
    22. Boushaba N, Tabet-Aoul N. Allele and genotype frequencies of β-lactoglobulin gene using PCR-RFLP in Algerian local cattle populations. Mol Biol Res Commun 2024;13(1):43-49.
      doi: 10.22099/mbrc.2023.47661.1841pubmed: 38164367google scholar: lookup
    Subscribe to our newsletter
    Join 99,911 horse owners like you who receive our email updates on horse health and nutrition.