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Journal articles on the topic 'Brazzein'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

Neiers, Fabrice, Christine Belloir, Nicolas Poirier, Christian Naumer, Michael Krohn, and Loïc Briand. "Comparison of Different Signal Peptides for the Efficient Secretion of the Sweet-Tasting Plant Protein Brazzein in Pichia pastoris." Life 11, no. 1 (2021): 46. http://dx.doi.org/10.3390/life11010046.

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Brazzein is a small sweet-tasting protein found in the red berries of a West African evergreen shrub, Pentadiplandra brazzeana Baillon. Brazzein is highly soluble and stable over a large pH range and at high temperatures, which are characteristics that suggest its use as a natural sweetener. However, Pentadiplandra brazzeana culture is difficult at a large scale, limiting the natural source of brazzein. Heterologous expression of brazzein has been established in numerous systems, including bacteria, yeast, and transgenic plants. Brazzein requires four disulfide bonds to be active in eliciting

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2

Nagata, Koji, Nobuko Hongo, Yasuhiro Kameda, et al. "Brazzein and structurally similar proteins: structural/functional comparisons." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1511. http://dx.doi.org/10.1107/s2053273314084885.

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Brazzein, a 6.5-kDa protein consisting of 54 amino acids and four disulfide bonds, is the smallest sweet-tasting protein yet isolated from the wild African plant Pentadiplandra brazzeana. Brazzein has various desirable properties for use as a low-calorie sweetener in the diets of individuals suffering from diabetes, obesity, and metabolic syndrome. For example, brazzein has a high water solubility and a high thermostability. In addition, brazzein is 2000-times sweeter than sucrose on a weight basis. Both the solution and crystal structures of brazzein have been reported. In the crystal structu

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3

Markova, Ekaterina V., Angelina V. Chirinskaite, Julia V. Sopova, and Elena I. Leonova. "The sweet protein brazzein as a promising natural sweetener." Ecological genetics 20, no. 1S (2022): 48–49. http://dx.doi.org/10.17816/ecogen112373.

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In the modern world, due to the overconsumption of sugar-containing products, the problem of obesity is relevant. Among the many sweeteners that minimize sugar intake, a group of sweet-tasting proteins is up-and-coming. Brazzein is the smallest of the sweet proteins (54 aa, 6473 Da), and it is also safe for obese and diabetic people since it does not affect blood sugar and insulin levels. Brazzein has high thermal stability over a wide pH range: from 2 to 8 [1]. To increase the level of sweetness of brazzein, mutant variants of this protein were created through site-directed mutagenesis, the s

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4

Lynch, Barry, Tina Wang, Trung Vo, Shahrzad Tafazoli, and Jason Ryder. "Safety evaluation of oubli fruit sweet protein (brazzein) derived from Komagataella phaffii, intended for use as a sweetener in food and beverages." Toxicology Research and Application 7 (January 2023): 239784732311512. http://dx.doi.org/10.1177/23978473231151258.

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Naturally sweet proteins have no glycemic effect and offer a fundamentally new approach to sweetness and health for individuals seeking to reduce their added sugar intake. However, unlike many commercial sweeteners, little research has been performed on the potential safety implications of adding these uniquely sweet proteins to food and beverages. In this study, a naturally sweet protein found in the West African Oubli plant ( Pentadiplandra brazzeana), referred to as Oubli fruit sweet protein or brazzein, was expressed in Komagataella phaffii (formerly Pichia pastoris) and produced via preci

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5

Jafari, S. Shahrbanoo, Vahab Jafarian, Khosrow Khalifeh, Parisa Ghanavatian, and S. Akram Shirdel. "The effect of charge alteration and flexibility on the function and structural stability of sweet-tasting brazzein." RSC Advances 6, no. 64 (2016): 59834–41. http://dx.doi.org/10.1039/c6ra12626j.

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To identify the structural and functional roles of Glu<sup>9</sup> located at the first loop of sweet-tasting brazzein, two different mutants (E9K and E9G) of the minor form of brazzein were designed and constructed.

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6

Novik, Tamara S., Elena I. Koveshnikova, Anatoly A. Kotlobay, et al. "Sweet-Tasting Natural Proteins Brazzein and Monellin: Safe Sugar Substitutes for the Food Industry." Foods 12, no. 22 (2023): 4065. http://dx.doi.org/10.3390/foods12224065.

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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 hav

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7

Saraiva, Ariana, Conrado Carrascosa, Fernando Ramos, et al. "Brazzein and Monellin: Chemical Analysis, Food Industry Applications, Safety and Quality Control, Nutritional Profile and Health Impacts." Foods 12, no. 10 (2023): 1943. http://dx.doi.org/10.3390/foods12101943.

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Recently, customers have been keener to buy products manufactured using all-natural ingredients with positive health properties, but without losing flavor. In this regard, the objective of the current study is to review the consumption of brazzein and monellin, their nutritional profiles and health effects, and their potential applications in the food industry. This poses challenges with sustainability and important quality and safety indicators, as well as the chemical processes used to determine them. To better understand the utilization of brazzein and monellin, the chemical analysis of the

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8

Volkov, V. N. "Sweet Protein as a Sugar Substitute." Chemistry at School, no. 3 (March 1, 2025): 5–9. https://doi.org/10.62709/0368-5632-2025-3-5-9.

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9

Zhao, Qin, Jikui Song, Zheyuan Jin, Vicktoria Danilova, Göran Hellekant, and John L. Markley. "Probing the sweet determinants of brazzein: Wild-type brazzein and a tasteless variant, brazzein-ins(R18a-I18b), exhibit different pH-dependent NMR chemical shifts." Biochemical and Biophysical Research Communications 335, no. 1 (2005): 256–63. http://dx.doi.org/10.1016/j.bbrc.2005.07.049.

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10

Nagata, Koji, Nobuko Hongo, Yasuhiro Kameda, et al. "The structure of brazzein, a sweet-tasting protein from the wild African plantPentadiplandra brazzeana." Acta Crystallographica Section D Biological Crystallography 69, no. 4 (2013): 642–47. http://dx.doi.org/10.1107/s0907444913001005.

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11

Shishkina, E. "Sweet sensation: EFKO on the use of sweet protein." Tovaroved prodovolstvennykh tovarov (Commodity specialist of food products), no. 12 (December 5, 2024): 724–26. https://doi.org/10.33920/igt-01-2412-05.

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The article discusses the use of the sweet protein brazzein in the confectionery industry. Information on the properties of the ingredient, its eff ect on health, production technology, and prospects for use is provided.

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12

Jin, Z. "Monkey Electrophysiological and Human Psychophysical Responses to Mutants of the Sweet Protein Brazzein: Delineating Brazzein Sweetness." Chemical Senses 28, no. 6 (2003): 491–98. http://dx.doi.org/10.1093/chemse/28.6.491.

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13

Han, Jong-Eun, Yun-Ji Park, Hyoshin Lee, Yoo-Jin Jeong, and So-Young Park. "Increased brazzein expression by abiotic stress and bioreactor culture system for the production of sweet protein, brazzein." Plant Biotechnology Reports 14, no. 4 (2020): 459–66. http://dx.doi.org/10.1007/s11816-020-00625-6.

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14

Markova, E. V., E. I. Leonova, and Ju V. Sopova. "Sweet protein brazzein as a promising sweetener." Problems of Nutrition 93, no. 1 (2024): 61–71. http://dx.doi.org/10.33029/0042-8833-2024-93-1-61-71.

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15

Gao, Guanghua, Jixun Dai, Ming Ding, Göran Hellekant, Jinfeng Wang, and Dacheng Wang. "Studies on solution NMR structure of brazzein." Science in China Series C: Life Sciences 42, no. 4 (1999): 409–19. http://dx.doi.org/10.1007/bf02882061.

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16

Fatemeh, Mansouri, and Hossain Modarressi Mohammad. "Production of Monoclonal Specific Antibody against Brazzein Fusion Protein." Biotechnology Journal International 18, no. 4 (2017): 1–9. https://doi.org/10.9734/BJI/2017/33505.

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<strong>Background: </strong>The use of a natural sweet protein is important as an attractive alternative to sucrose in the human diet. Rigorous research has identified the use of the artificial sweetener that leads to various diseases, cancer and heart disease. Many functional studies are necessary for examining the structure and biological activity of natural sweeteners such as Brazzein and its receptor targeting. In this report, we produced a panel of monoclonal antibodies against the recombinant brazzein which can be used for functional studies. <strong>Methods:</strong> Hybridomas cell fu

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17

Jin, Zheyuan, Vicktoria Danilova, Fariba M. Assadi-Porter, David J. Aceti, John L. Markley, and Göran Hellekant. "Critical regions for the sweetness of brazzein 1." FEBS Letters 544, no. 1-3 (2003): 33–37. http://dx.doi.org/10.1016/s0014-5793(03)00383-1.

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18

Izawa, Hiroyuki, Masafumi Ota, Masanori Kohmura, and Yasuo Ariyoshi. "Synthesis and characterization of the sweet protein brazzein." Biopolymers 39, no. 1 (1998): 95–101. http://dx.doi.org/10.1002/(sici)1097-0282(199607)39:1<95::aid-bip10>3.0.co;2-b.

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19

Kazemi-Nasab, Akram, and Azar Shahpiri. "Expression of Brazzein, a Small Sweet-Tasting Protein in Saccharomyces cerevisiae: An Introduction for Production of Sweet Yeasts." Protein & Peptide Letters 27, no. 10 (2020): 945–52. http://dx.doi.org/10.2174/0929866527666200331134431.

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Background: The replacement of carbohydrate sweeteners with protein sweeteners from plants has attracted the interest of researchers because these proteins don’t trigger the insulin response and are more nutritive for consumption in food. Brazzein (Braz) is a small and heat- stable sweet protein that has been originally derived from African plant Pentadiplandra brazzeana. In the present work the solubility, sweetness and yield of recombinant forms of Braz in two expression hosts, E. coli and S. cerevisiae were comprised. Methods: The codon-optimized gene of Braz was cloned in expression vector

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20

Hellekant, G. "Brazzein a Small, Sweet Protein: Discovery and Physiological Overview." Chemical Senses 30, Supplement 1 (2005): i88—i89. http://dx.doi.org/10.1093/chemse/bjh127.

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21

Mansouri, Fatemeh, and Mohammad Modarressi. "Production of Monoclonal Specific Antibody against Brazzein Fusion Protein." Biotechnology Journal International 18, no. 4 (2017): 1–9. http://dx.doi.org/10.9734/bji/2017/33505.

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22

Caldwell, Jane E., Frits Abildgaard, Željko Džakula, Ding Ming, Göran Hellekant, and John L. Markley. "Solution structure of the thermostable sweet-tasting protein brazzein." Nature Structural Biology 5, no. 6 (1998): 427–31. http://dx.doi.org/10.1038/nsb0698-427.

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23

Ming, Ding, and Göran Hellekant. "Brazzein, a new high-potency thermostable sweet protein fromPentadiplandra brazzeanaB." FEBS Letters 355, no. 1 (1994): 106–8. http://dx.doi.org/10.1016/0014-5793(94)01184-2.

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24

Kohmura, Masanori, Masafumi Ota, Hiroyuki Izawa, Ding Göran Ming Hellekant, and Yasuo Ariyoshi. "Assignment of the disulfide bonds in the sweet protein brazzein." Biopolymers 38, no. 4 (1998): 553–56. http://dx.doi.org/10.1002/(sici)1097-0282(199604)38:4<553::aid-bip10>3.0.co;2-b.

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25

Lee, Yoo-Won, Kwan-Young Kim, Sang-Hyun Han, Chang-Ho Kang, and Jae-Seong So. "Expression of the sweet-tasting protein brazzein in Lactobacillus spp." Food Science and Biotechnology 21, no. 3 (2012): 895–98. http://dx.doi.org/10.1007/s10068-012-0116-z.

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26

Kazlouski, I. S., I. V. Belskaya, and А. I. Zinchenko. "Biosynthesis of brazzein using the bacterial cell-free protein synthesis system." Doklady of the National Academy of Sciences of Belarus 64, no. 1 (2020): 71–77. http://dx.doi.org/10.29235/1561-8323-2020-64-1-71-77.

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27

Walters, D. E., T. Cragin, Z. Jin, J. N. Rumbley, and G. Hellekant. "Design and Evaluation of New Analogs of the Sweet Protein Brazzein." Chemical Senses 34, no. 8 (2009): 679–83. http://dx.doi.org/10.1093/chemse/bjp048.

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28

Walters, D. Eric, and Göran Hellekant. "Interactions of the Sweet Protein Brazzein with the Sweet Taste Receptor." Journal of Agricultural and Food Chemistry 54, no. 26 (2006): 10129–33. http://dx.doi.org/10.1021/jf062359y.

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29

Chung, Hyun-Jung, Hyun-Young Cho, and Kwang-Hoon Kong. "Site-direct mutagenesis of critical regions for the sweetness of brazzein." Journal of Biotechnology 136 (October 2008): S400. http://dx.doi.org/10.1016/j.jbiotec.2008.07.926.

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30

Cornilescu, Claudia C., Gabriel Cornilescu, Hongyu Rao, et al. "Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein." Proteins: Structure, Function, and Bioinformatics 81, no. 6 (2013): 919–25. http://dx.doi.org/10.1002/prot.24259.

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31

Park, Se-Woong, Byung-Ha Kang, Hyeong-Min Lee, et al. "Efficient brazzein production in yeast (Kluyveromyces lactis) using a chemically defined medium." Bioprocess and Biosystems Engineering 44, no. 4 (2021): 913–25. http://dx.doi.org/10.1007/s00449-020-02499-y.

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32

Han, Jong-Eun, Hyoshin Lee, Thanh-Tam Ho, and So-Young Park. "Brazzein protein production in transgenic carrot cells using air-lift bioreactor culture." Plant Biotechnology Reports 16, no. 2 (2022): 161–71. http://dx.doi.org/10.1007/s11816-022-00743-3.

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33

Dittli, S. M., H. Rao, M. Tonelli, et al. "Structural Role of the Terminal Disulfide Bond in the Sweetness of Brazzein." Chemical Senses 36, no. 9 (2011): 821–30. http://dx.doi.org/10.1093/chemse/bjr057.

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34

Yan, Sen, Hong Song, Daxin Pang, et al. "Expression of Plant Sweet Protein Brazzein in the Milk of Transgenic Mice." PLoS ONE 8, no. 10 (2013): e76769. http://dx.doi.org/10.1371/journal.pone.0076769.

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35

Yun, Cho-Rong, Ji-Na Kong, Ju-Hee Chung, Myung-Chul Kim, and Kwang-Hoon Kong. "Improved Secretory Production of the Sweet-Tasting Protein, Brazzein, in Kluyveromyces lactis." Journal of Agricultural and Food Chemistry 64, no. 32 (2016): 6312–16. http://dx.doi.org/10.1021/acs.jafc.6b02446.

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36

Ishikawa, K., M. Ota, Y. Ariyoshi, et al. "Crystallization and preliminary X-ray analysis of brazzein, a new sweet protein." Acta Crystallographica Section D Biological Crystallography 52, no. 3 (1996): 577–78. http://dx.doi.org/10.1107/s0907444995014867.

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37

Yoon, Sug-Young, Ji-Na Kong, Dong-Hyeon Jo, and Kwang-Hoon Kong. "Residue mutations in the sweetness loops for the sweet-tasting protein brazzein." Food Chemistry 129, no. 4 (2011): 1327–30. http://dx.doi.org/10.1016/j.foodchem.2011.06.054.

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38

Assadi-Porter, Fariba M., David J. Aceti, and John L. Markley. "Sweetness Determinant Sites of Brazzein, a Small, Heat-Stable, Sweet-Tasting Protein." Archives of Biochemistry and Biophysics 376, no. 2 (2000): 259–65. http://dx.doi.org/10.1006/abbi.2000.1726.

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39

YIN, Tao, Hong-Yu LU, Shang-Long ZHANG, Jing-Mei LIU, and Da-Ming CHEN. "Fruit-specific expression of sweet protein Brazzein in transgenic tomato plants." Hereditas (Beijing) 31, no. 6 (2009): 663–67. http://dx.doi.org/10.3724/sp.j.1005.2009.00663.

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40

Kim, Hansaem, Jaeyong Kang, Seungwoo Hong, et al. "3M-Brazzein as a Natural Sugar Substitute Attenuates Obesity, Metabolic Disorder, and Inflammation." Journal of Agricultural and Food Chemistry 68, no. 7 (2020): 2183–92. http://dx.doi.org/10.1021/acs.jafc.0c00317.

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41

Chung, Ju-Hee, Ji-Na Kong, Hyo-Eun Choi, and Kwang-Hoon Kong. "Antioxidant, anti-inflammatory, and anti-allergic activities of the sweet-tasting protein brazzein." Food Chemistry 267 (November 2018): 163–69. http://dx.doi.org/10.1016/j.foodchem.2017.06.084.

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42

Lee, Jin-Ju, Ji-Na Kong, Hyun-Dong Do, Dong-Hyeon Jo, and Kwang-Hoon Kong. "Design and Efficient Soluble Expression of a Sweet Protein, Brazzein and Minor-Form Mutant." Bulletin of the Korean Chemical Society 31, no. 12 (2010): 3830–33. http://dx.doi.org/10.5012/bkcs.2010.31.12.3830.

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43

Lee, Ye Rim, Shahina Akter, In Hye Lee, et al. "Stable expression of brazzein protein, a new type of alternative sweetener in transgenic rice." Journal of Plant Biotechnology 45, no. 1 (2018): 63–70. http://dx.doi.org/10.5010/jpb.2018.45.1.063.

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44

Amri, Ezekiel. "The Effect of Mutation in Brazzein Deduced from Mutational Sites and Sequence Carbon Content." International Journal of Genetics and Genomics 3, no. 6 (2015): 59. http://dx.doi.org/10.11648/j.ijgg.20150306.11.

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45

Hung, Chien-Ya, Lee-Hao Cheng, and Chuan-Mei Yeh. "Functional expression of recombinant sweet-tasting protein brazzein by Escherichia coli and Bacillus licheniformis." Food Biotechnology 33, no. 3 (2019): 251–71. http://dx.doi.org/10.1080/08905436.2019.1618323.

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46

Jo, Hyun-Joo, Jin-Seok Noh, and Kwang-Hoon Kong. "Efficient secretory expression of the sweet-tasting protein brazzein in the yeast Kluyveromyces lactis." Protein Expression and Purification 90, no. 2 (2013): 84–89. http://dx.doi.org/10.1016/j.pep.2013.05.001.

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47

Gao, Guang-Hua, Ji-Xun Dai, Ming Ding, Göran Hellekant, Jin-Fen Wang, and Da-Cheng Wang. "Solution conformation of brazzein by 1H nuclear magnetic resonance: resonance assignment and secondary structure." International Journal of Biological Macromolecules 24, no. 4 (1999): 351–59. http://dx.doi.org/10.1016/s0141-8130(99)00055-0.

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48

Lim, Jin-Kyung, Jin-Chul Jang, Mi-Mi Kim та Kwang-Hoon Kong. "Role of Lys5 Residue in β-Strand I of the Sweet-Tasting Protein Brazzein". Journal of Food Biochemistry 40, № 4 (2016): 446–50. http://dx.doi.org/10.1111/jfbc.12231.

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49

Lim, Jin-Kyung, Jin-Chul Jang, Ji-Na Kong, Myung-Chul Kim, and Kwang-Hoon Kong. "Importance of Glu53 in the C-terminal region of brazzein, a sweet-tasting protein." Journal of the Science of Food and Agriculture 96, no. 9 (2015): 3202–6. http://dx.doi.org/10.1002/jsfa.7501.

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50

Hong, Seungwoo, Hansaem Kim, Kwang-Hoon Kong, and Sungguan Hong. "3M-Brazzein as a natural sugar substitute rescued obesity in maternal and offspring mice." Journal of Functional Foods 115 (April 2024): 106104. http://dx.doi.org/10.1016/j.jff.2024.106104.

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