| Autor: |
Novik TS; Scientific Research Centre Pharmbiomed, Selskohozjajstvennaja Str., 12a, Moscow 129226, Russia., Koveshnikova EI; Scientific Research Centre Pharmbiomed, Selskohozjajstvennaja Str., 12a, Moscow 129226, Russia., Kotlobay AA; Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine, Malaya Pirogovskaya Str. 1a, Moscow 119435, Russia., Sycheva LP; Burnasyan Federal Medical Biophysical Center of Federal Medical Biological Agency, Zhivopisnaya Str., 46, Moscow 123182, Russia., Kurochkina KG; Scientific Research Centre Pharmbiomed, Selskohozjajstvennaja Str., 12a, Moscow 129226, Russia., Averina OA; A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Moscow 119991, Russia., Belopolskaya MV; Institute of Mitoengineering MSU, Leninskie Gory 1, Moscow 119991, Russia., Sergiev PV; A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Moscow 119991, Russia., Dontsova OA; A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Moscow 119991, Russia., Lazarev VN; Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine, Malaya Pirogovskaya Str. 1a, Moscow 119435, Russia., Maev IV; Department of Propaedeutics of Internal Diseases and Gastroenterology, Moscow State University of Medicine and Dentistry, Delegatskaya St. 20/1, Moscow 103473, Russia., Kostyaeva MG; Faculty of Medicine, Peoples Friendship University of Russia Named after Patrice Lumumba, Miklukho-Maklaya Str.6, Moscow 117198, Russia., Eremeev AV; Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine, Malaya Pirogovskaya Str. 1a, Moscow 119435, Russia., Chukina SI; Scientific Research Centre Pharmbiomed, Selskohozjajstvennaja Str., 12a, Moscow 129226, Russia., Lagarkova MA; Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine, Malaya Pirogovskaya Str. 1a, Moscow 119435, Russia. |
| Abstrakt: |
This article presents the results of a comprehensive toxicity assessment of brazzein and monellin, yeast-produced recombinant sweet-tasting proteins. Excessive sugar consumption is one of the leading dietary and nutritional problems in the world, resulting in health complications such as obesity, high blood pressure, and cardiovascular disease. Although artificial small-molecule sweeteners widely replace sugar in food, their safety and long-term health effects remain debatable. Many sweet-tasting proteins, including thaumatin, miraculin, pentadin, curculin, mabinlin, brazzein, and monellin have been found in tropical plants. These proteins, such as brazzein and monellin, are thousands-fold sweeter than sucrose. Multiple reports have presented preparations of recombinant sweet-tasting proteins. A thorough and comprehensive assessment of their toxicity and safety is necessary to introduce and apply sweet-tasting proteins in the food industry. We experimentally assessed acute, subchronic, and chronic toxicity effects, as well as allergenic and mutagenic properties of recombinant brazzein and monellin. Our study was performed on three mammalian species (mice, rats, and guinea pigs). Assessment of animals' physiological, biochemical, hematological, morphological, and behavioral indices allows us to assert that monellin and brazzein are safe and nontoxic for the mammalian organism, which opens vast opportunities for their application in the food industry as sugar alternatives. |
