Abstract
Royal jelly is a nutritious substance secreted from the hypopharyngeal and mandibular glands of worker bees that serves as the only food on which honeybee queen larvae and adults are fed and which causes them to develop into queen bees. Royal jelly is a protein-rich food and one of the most crucial factors for the growth of queen bees. In this study, we characterized the hydrolytic activity of enzymes from the homogenates of honeybee queen larvae on royal jelly proteins. Homogenates of 3-day-old queen bee larvae were capable of hydrolyzing royal jelly proteins under alkaline conditions. Following separation by cation exchange and gel filtration column chromatographies, two proteases of 38 and 28 kDa were found by SDS-PAGE. The protease of 38 kDa had a carboxypeptidase A-like activity and that of 28 kDa a chymotrypsin-like activity. These enzymes may turn out to be useful in the manufacturing of processed royal jelly.
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Acknowledgments
We thank Dr. Yokichi Hayashi of the Department of Life Science of Asahikawa Medical Collage, Dr. Tomoyuki Mishima of the Gifu University of Medical Science, and Dr. Hisashi Suzuki of the Industrial Technology Center of Gifu Prefectural Government for helpful suggestions. We also thank Kenji Ota, Suzuyo Watanabe, and Yuri Kashima of Akitaya Honten Co., Ltd. for providing the RJ and larvae samples.
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Manuscript editor: Klaus Hartfelder
Isolation et caractérisation des protéases hydrolisant les protéines de la gelée royale, obtenues à partir de larves de reines de l’abeille, Apis mellifera .
Apis mellifera / larve de reine / protéase / gelée royale
Isolierung und Charakterisierung von Proteasen aus Königinnenlarven der Honigbiene, Apis mellifera , die zur Hydrolyse von Gelée royale geeignet sind.
Apis mellifera / Königinnenlarven / Protease / Königinnenfuttersaft
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Matsuoka, T., Kawashima, T., Nakamura, T. et al. Isolation and characterization of proteases that hydrolyze royal jelly proteins from queen bee larvae of the honeybee, Apis mellifera . Apidologie 43, 685–697 (2012). https://doi.org/10.1007/s13592-012-0143-z
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DOI: https://doi.org/10.1007/s13592-012-0143-z