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Year 2019, , 59 - 70, 23.04.2020
https://doi.org/10.35206/jan.679534

Abstract

References

  • Ahmad, S., Campos, M. G., Fratini, F., Altaye, S. Z., & Li, J. (2020). New Insights into the Biological and Pharmaceutical Properties of Royal Jelly. International Journal of Molecular Sciences, 21(2), 382. Akyol, E., & Baran, Y. (2015). Ari Sütünün Yapısı, İnsanlar ve Arılar İçin Önemi. Uludag Bee Journal, 15(1). Almeer, R. S., Alarifi, S., Alkahtani, S., Ibrahim, S. R., Ali, D., & Moneim, A. (2018). The potential hepatoprotective effect of royal jelly against cadmium chloride-induced hepatotoxicity in mice is mediated by suppression of oxidative stress and upregulation of Nrf2 expression. Biomedicine & Pharmacotherapy, 106, 1490-1498. Aslan, Z., & Aksoy, L. (2015). Anti-inflammatory effects of royal jelly on ethylene glycol induced renal inflammation in rats. International braz j urol, 41(5), 1008-1013. Balkanska, R., & Kashamov, B. (2011). Composition and physico-chemical properties of lyophilized Royal jelly. Bee Science, 11(4), 114-117. Balkanska, R., Zhelyazkova, I., & Ignatova, M. (2012). Physico-chemical quality characteristics of royal jelly from three regions of Bulgaria. Agricultural Science and Technology, 4(3), 302-305. Bărnuţiu, L. I., Mărghitaş, L. A., Dezmirean, D. S., Mihai, C. M., & Bobiş, O. (2011). Chemical composition and antimicrobial activity of royal jelly-review. Scientific Papers Animal Science and Biotechnologies, 44(2), 67-72. Benfenati L., Sabatini A. G., Nanetti A. (1986) Composizione in sali minerali della gelatina reale, Apicoltura, 2, 129-143. Bilikova, K., Hanes, J., Nordhoff, E., Saenger, W., Klaudiny, J., & Simuth, J. (2002). Apisimin, a new serine–valine-rich peptide from honey bee (Apis mellifera L.) royal jelly: Purification and molecular characterization. FEBS Letters, 528, 125–129. Bílikova, K., Huang, S. C., Lin, I. P., Šimuth, J., & Peng, C. C. (2015). Structure and antimicrobial activity relationship of royalisin, an antimicrobial peptide from royal jelly of Apis mellifera. Peptides, 68, 190-196. Bilikova, K., Wu, G., & Simuth, J. (2001). Isolation of a peptide fraction from honey bee royal jelly as a potential antifoulbrood factor. Apidologie, 32, 275–283. Burgess RR, Deutscher MP. (Eds.). Guide to Protein Purification (Vol. 463). Academic Press. 2009; 854. Buttstedt, A., Moritz, R. F., & Erler, S. (2014). Origin and function of the major royal jelly proteins of the honeybee (Apis mellifera) as members of the yellow gene family. Biological Reviews, 89(2), 255-269. Chen, X., Fang, F., & Wang, S. (2020). Physicochemical properties and hepatoprotective effects of glycated Snapper fish scale peptides conjugated with xylose via maillard reaction. Food and Chemical Toxicology, 111115. Chiu, H. F., Chen, B. K., Lu, Y. Y., Han, Y. C., Shen, Y. C., Venkatakrishnan, K., ... & Wang, C. K. (2017). Hypocholesterolemic efficacy of royal jelly in healthy mild hypercholesterolemic adults. Pharmaceutical Biology, 55(1), 497-502. Coskun, O. (2016). Separation techniques: chromatography. Northern Clinics of Istanbul, 3(2), 156. Coutinho, D., Karibasappa, S. N., & Mehta, D. S. (2018). Royal Jelly Antimicrobial Activity against Periodontopathic Bacteria. Journal of Interdisciplinary Dentistry, 8(1), 18. Dania, F., Bazelidze, N., Chinou, I., Melliou, E., Rallis, M., & Papaioannou, G. (2008). In vivo antidiabetic activity of Greek propolis and Royal Jelly. Planta Medica, 74(09), 43. Eshtiyaghi, M., Deldar, H., Pirsaraei, Z. A., & Shohreh, B. (2016). Royal jelly may improve the metabolism of glucose and redox state of ovine oocytes matured in vitro and embryonic development following in vitro fertilization. Theriogenology, 86(9), 2210-2221. Fontana, R., Mendes, M. A., De Souza, B. M., Konno, K., Cesar, L. M. M., Malaspina, O., & Palma, M. S. (2004). Jelleines: A family of antimicrobial peptides from the Royal Jelly of honey bees (Apis mellifera). Peptides, 25, 919–928. Foret, S., Kucharski, R., Pellegrini, M., Feng, S., Jacobsen, S. E., Robinson, G. E., & Maleszka, R. (2012). DNA methylation dynamics, metabolic fluxes, gene splicing, and alternative phenotypes in honey bees. Proceedings of the National Academy of Sciences, 109, 4968–4973. Fujii, A., Kobayashi, S., Kuboyama, N., Furukawa, Y., Kaneko, Y., Ishihama, S., Yamamoto, H., & Tamura, T. (1990). Augmentation of wound healing by royal jelly (RJ) in streptozotocin-diabetic rats. Japan Journal of Pharmacy, 53, 331–337. Fujiwara, S., Imai, J., Fujiwara, M., Yaeshima, T., Kawashima, T., & Kobayashi, K. (1990). A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. Journal of Biological Chemistry, 265, 11333–11337. Furakawa, S. (2008). Stimulatory effects of royal jelly on the generation of neuronal and glial cells expectation of protection against some neurological disorders. Foods and Food Ingredients Journal, 213(7), 321-328. Ghanbari, E., Nejati, V., & Azadbakht, M. (2015). Protective effect of royal jelly against renal damage in streptozotocin induced diabetic rats. Iranian Journal of Toxicology, 9(28), 1258-1263. Guo, H., Ekusa, A., Iwai, K., Yonekura, M., Takahata, Y., & Morimatsu, F. (2008). Royal jelly peptides inhibit lipid peroxidation in vitro and in vivo. Journal of Nutritional Science And Vitaminology, 54(3), 191-195. Guo, H., Saiga, A., Sato, M., Miyazawa, I., Shibata, M., Takahata, Y., & Morimatsu, F. (2007). Royal jelly supplementation improves lipoprotein metabolism in humans. Journal of Nutritional Science and Vitaminology, 53(4), 345-348. Han, S. M., Yeo, J. H., Cho, Y. H., & Pak, S. C. (2011). Royal Jelly reduces melanin synthesis through down regulation of tyrosinase expression. American Journal of Chinese Medicine, 39(6), 1253-1260. doi: org/10.1142/S0192415X11009536. Hattori, N., Nomoto, H., Fukumitsu, H., Mishima, S., & Furukawa, S. (2007). AMP N1-oxide potentiates astrogenesis by cultured neural stem/progenitor cells through STAT3 activation. Biomedical Research, 28(6), 295-299. Hu, F. L., Bíliková, K., Casabianca, H., Daniele, G., Salmen Espindola, F., Feng, M., ... & Li, L. (2019). Standard methods for Apis mellifera royal jelly research. Journal of Apicultural Research, 58(2), 1-68. Husein, M. Q., & Haddad, S. G. (2006). A new approach to enhance reproductive performance in sheep using royal jelly in comparison with equine chorionic gonadotropin. Animal Reproduction Science, 93(1-2), 24-33. Imjongjirak, C., Klinbunga, S., & Sittipraneed, S. (2005). Cloning, expression and genomic organization of genes encoding major royal jelly protein 1 and 2 of the honey bee (Apis cerana). BMB Reports, 38, 49–57. Issaq, H. J., & Veenstra, T. D. (2008). Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE): advances and perspectives. Biotechniques, 44(5), 697-700. Jamnik, P., Raspor, P., & Javornik, B. (2012). A proteomic approach for investigation of bee products: Royal jelly, propolis and honey. Food Technology and Biotechnology, 50(3), 270-274. Kamakura, M. (2011). Royalactin induces queen differentiation in honey bees. Nature, 473, 478–483. Kamakura, M., Fukuda, T., Fukushima, M., & Yonekura, M. (2001). Storage-dependent degradation of 57-kDa protein in royal jelly: A possible marker for freshness. Bioscience, Biotechnology, and Biochemistry, 65, 277–284. Kamakura, M., Moriyama, T., & Sakaki, T. (2006). Changes in hepatic gene expression associated with the hypocholesterolaemic activity of royal jelly. Journal of Pharmacy and Pharmacology, 58(12), 1683-1689. Kamakura, M., Suenobu, N., & Fukushima, M. (2001). Fifty-seven-kDa protein in royal jelly enhances proliferation of primary cultured rat hepatocytes and increases albumin production in the absence of serum. Biochemical and Biophysical Research Communications, 282, 865–874. Kanbur, M., Eraslan, G., Beyaz, L., Silici, S., Liman, B. 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Royal Jelly: Proteins and Peptides

Year 2019, , 59 - 70, 23.04.2020
https://doi.org/10.35206/jan.679534

Abstract

Royal jelly is secreted by the hypopharyngeal and mandibular glands of 5-15 days worker honeybees (Apis mellifera). Royal jelly is a thick and milky bee product with high nutritional value. Besides the nutritional functions on queen and worker larvaes, it also has a very important role on the specific functions of queen bees. Due to its important biological properties, royal jelly has been used in the pharmaceutical, food and cosmetics industry especially for the last 50-60 years as a functional and nutraceutical food. The studies have shown that royal jelly has antioxidant, antidiabetic, antitumor, neurotrophic, antimicrobial, anti-inflammatory, hypotensive, hepatoprotective, antihypercholesterolemic, hypoglycaemic and effects on the reproductive system and fertility. These activities are attributed to the bioactive components it contains such as major royal jelly proteins (MRJPs), jelleins and royalisin peptides and 10-hydroxy-2-decenoic acid (10-HDA). Especially MRJPs are considered an important factor in the development of queen bees. The aim of this study is to summarize and update physicochemical and bioactive properties of royal jelly, characterization and functions of royal jelly proteins (RJPs) and peptides.

References

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Balkanska, R., Zhelyazkova, I., & Ignatova, M. (2012). Physico-chemical quality characteristics of royal jelly from three regions of Bulgaria. Agricultural Science and Technology, 4(3), 302-305. Bărnuţiu, L. I., Mărghitaş, L. A., Dezmirean, D. S., Mihai, C. M., & Bobiş, O. (2011). Chemical composition and antimicrobial activity of royal jelly-review. Scientific Papers Animal Science and Biotechnologies, 44(2), 67-72. Benfenati L., Sabatini A. G., Nanetti A. (1986) Composizione in sali minerali della gelatina reale, Apicoltura, 2, 129-143. Bilikova, K., Hanes, J., Nordhoff, E., Saenger, W., Klaudiny, J., & Simuth, J. (2002). Apisimin, a new serine–valine-rich peptide from honey bee (Apis mellifera L.) royal jelly: Purification and molecular characterization. FEBS Letters, 528, 125–129. Bílikova, K., Huang, S. C., Lin, I. P., Šimuth, J., & Peng, C. C. (2015). Structure and antimicrobial activity relationship of royalisin, an antimicrobial peptide from royal jelly of Apis mellifera. Peptides, 68, 190-196. Bilikova, K., Wu, G., & Simuth, J. (2001). Isolation of a peptide fraction from honey bee royal jelly as a potential antifoulbrood factor. Apidologie, 32, 275–283. Burgess RR, Deutscher MP. (Eds.). Guide to Protein Purification (Vol. 463). Academic Press. 2009; 854. Buttstedt, A., Moritz, R. F., & Erler, S. (2014). Origin and function of the major royal jelly proteins of the honeybee (Apis mellifera) as members of the yellow gene family. Biological Reviews, 89(2), 255-269. Chen, X., Fang, F., & Wang, S. (2020). Physicochemical properties and hepatoprotective effects of glycated Snapper fish scale peptides conjugated with xylose via maillard reaction. Food and Chemical Toxicology, 111115. Chiu, H. F., Chen, B. K., Lu, Y. Y., Han, Y. C., Shen, Y. C., Venkatakrishnan, K., ... & Wang, C. K. (2017). Hypocholesterolemic efficacy of royal jelly in healthy mild hypercholesterolemic adults. Pharmaceutical Biology, 55(1), 497-502. Coskun, O. (2016). Separation techniques: chromatography. Northern Clinics of Istanbul, 3(2), 156. Coutinho, D., Karibasappa, S. N., & Mehta, D. S. (2018). Royal Jelly Antimicrobial Activity against Periodontopathic Bacteria. Journal of Interdisciplinary Dentistry, 8(1), 18. Dania, F., Bazelidze, N., Chinou, I., Melliou, E., Rallis, M., & Papaioannou, G. (2008). In vivo antidiabetic activity of Greek propolis and Royal Jelly. Planta Medica, 74(09), 43. Eshtiyaghi, M., Deldar, H., Pirsaraei, Z. A., & Shohreh, B. (2016). Royal jelly may improve the metabolism of glucose and redox state of ovine oocytes matured in vitro and embryonic development following in vitro fertilization. Theriogenology, 86(9), 2210-2221. Fontana, R., Mendes, M. A., De Souza, B. M., Konno, K., Cesar, L. M. M., Malaspina, O., & Palma, M. S. (2004). Jelleines: A family of antimicrobial peptides from the Royal Jelly of honey bees (Apis mellifera). Peptides, 25, 919–928. Foret, S., Kucharski, R., Pellegrini, M., Feng, S., Jacobsen, S. E., Robinson, G. E., & Maleszka, R. (2012). DNA methylation dynamics, metabolic fluxes, gene splicing, and alternative phenotypes in honey bees. Proceedings of the National Academy of Sciences, 109, 4968–4973. Fujii, A., Kobayashi, S., Kuboyama, N., Furukawa, Y., Kaneko, Y., Ishihama, S., Yamamoto, H., & Tamura, T. (1990). Augmentation of wound healing by royal jelly (RJ) in streptozotocin-diabetic rats. Japan Journal of Pharmacy, 53, 331–337. Fujiwara, S., Imai, J., Fujiwara, M., Yaeshima, T., Kawashima, T., & Kobayashi, K. (1990). A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. Journal of Biological Chemistry, 265, 11333–11337. Furakawa, S. (2008). Stimulatory effects of royal jelly on the generation of neuronal and glial cells expectation of protection against some neurological disorders. Foods and Food Ingredients Journal, 213(7), 321-328. Ghanbari, E., Nejati, V., & Azadbakht, M. (2015). Protective effect of royal jelly against renal damage in streptozotocin induced diabetic rats. Iranian Journal of Toxicology, 9(28), 1258-1263. Guo, H., Ekusa, A., Iwai, K., Yonekura, M., Takahata, Y., & Morimatsu, F. (2008). Royal jelly peptides inhibit lipid peroxidation in vitro and in vivo. Journal of Nutritional Science And Vitaminology, 54(3), 191-195. Guo, H., Saiga, A., Sato, M., Miyazawa, I., Shibata, M., Takahata, Y., & Morimatsu, F. (2007). Royal jelly supplementation improves lipoprotein metabolism in humans. Journal of Nutritional Science and Vitaminology, 53(4), 345-348. Han, S. M., Yeo, J. H., Cho, Y. H., & Pak, S. C. (2011). Royal Jelly reduces melanin synthesis through down regulation of tyrosinase expression. American Journal of Chinese Medicine, 39(6), 1253-1260. doi: org/10.1142/S0192415X11009536. Hattori, N., Nomoto, H., Fukumitsu, H., Mishima, S., & Furukawa, S. (2007). 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Details

Primary Language English
Subjects Food Engineering
Journal Section Review Articles
Authors

Gülşah Okumuş Yükünç

Publication Date April 23, 2020
Published in Issue Year 2019

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APA Okumuş Yükünç, G. (2020). Royal Jelly: Proteins and Peptides. Journal of Apitherapy and Nature, 2(2), 59-70. https://doi.org/10.35206/jan.679534
AMA Okumuş Yükünç G. Royal Jelly: Proteins and Peptides. J.Apit.Nat. April 2020;2(2):59-70. doi:10.35206/jan.679534
Chicago Okumuş Yükünç, Gülşah. “Royal Jelly: Proteins and Peptides”. Journal of Apitherapy and Nature 2, no. 2 (April 2020): 59-70. https://doi.org/10.35206/jan.679534.
EndNote Okumuş Yükünç G (April 1, 2020) Royal Jelly: Proteins and Peptides. Journal of Apitherapy and Nature 2 2 59–70.
IEEE G. Okumuş Yükünç, “Royal Jelly: Proteins and Peptides”, J.Apit.Nat., vol. 2, no. 2, pp. 59–70, 2020, doi: 10.35206/jan.679534.
ISNAD Okumuş Yükünç, Gülşah. “Royal Jelly: Proteins and Peptides”. Journal of Apitherapy and Nature 2/2 (April 2020), 59-70. https://doi.org/10.35206/jan.679534.
JAMA Okumuş Yükünç G. Royal Jelly: Proteins and Peptides. J.Apit.Nat. 2020;2:59–70.
MLA Okumuş Yükünç, Gülşah. “Royal Jelly: Proteins and Peptides”. Journal of Apitherapy and Nature, vol. 2, no. 2, 2020, pp. 59-70, doi:10.35206/jan.679534.
Vancouver Okumuş Yükünç G. Royal Jelly: Proteins and Peptides. J.Apit.Nat. 2020;2(2):59-70.
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