Properties, biological activity, technology, and application of proteins and protein-derived products
Main Research Areas and Activities of the Laboratory
Investigating the composition, properties, and biological activity of protein raw materials derived from animals, plants, and microorganisms to establish scientific knowledge for the development of protein- and peptide-based products for medicine, food, light industry, and agriculture;
Isolating and purifying biologically active proteins and peptides from animal, plant, and microbiological sources; determining their molecular structures and properties;
Establishing theoretical and technological bases for the comprehensive utilization of protein raw materials, together with the enhancement of innovative technologies;
Studying and modifying the biological activity of protein- and peptide-based products for healthcare, food, and cosmetics;
Developing the production of biologically active organo-preparations from animal sources in Mongolia;
Exploring the expression, activity, and application potential of recombinant proteins;
Completed and Ongoing Projects
Basic Research Projects:
"Comprehensive biochemical-technological study of enzymatic hydrolysis products of protein raw materials" (2017–2020). Shuss-2018/13. Lead: M.Bayarjargal
"Biochemical-technological study of the deep processing of protein-rich secondary raw materials from food and light industries" /2015–2017/. SSI021/2015. Lead: T.Gan-Erdene
"Biochemical-technological study of biologically active protein-peptides" /2011–2013/. SSA021/2011. Lead: T.Gan-Erdene
"Chemistry and technology of biologically active substances and preparations" under the sub-topic "Theoretical and practical issues of the properties of regulatory and food additives and preparations" /2008–2010/. Lead: P.Odonmajig
“Structure and properties of biologically active compounds, theoretical and practical issues of their use in the production of biopreparations and regulated foods” /2005–2007/. Lead: P.Odonmajig
"Research on the properties of protein-degrading enzymes and their practical application" /2002-2004/. №2005-00026. Lead: D.Regdel
"Biochemical and technological basis for processing certain protein raw materials into biopreparations" /1986–1990/. Lead: O.Batmunkh
Science and technology custom project:
"Technological study on processing protein waste from leather production using biotechnological methods to create high-value-added products" /2022–2024/. ShUZZ-2022/311. Lead: M. Bayarjargal
"Technology for producing animal- and plant-derived feed additives" /2018–2020. ShUZZ-2018/7. Lead: T. Gan-Erdene
"Study of regulatory products from Mongolian animal, plant, and microorganism sources" /2016–2018/. ShUTT_010/2015. Lead: T. Gan-Erdene
Academy Grants:
"Products with regulatory effects on carbohydrate and fat metabolism" /2022–2023/. Lead: Ts. Ariunsaihan
"Zeolite-based detoxification preparation" /2014–2015/. №201500094. Lead: M. Bayarjargal
"Using cryogels to stabilize degraded soils and create perennial plant covers" (2011–2012). №201200063. Lead: T. Gan-Erdene
Innovation Projects:
"Technology for processing collagen raw materials from livestock for healthcare, food, and cosmetics purposes" /2015–2017/. In-16/2015. Lead: M. Bayarjargal
"Obtaining biologically active preparations from secondary raw materials" /2010–2012/. IN_419_04/2010. Lead: D. Regdel
"Production of pancreatin preparations from the pancreas of Mongolian grazing livestock" /2008–2010/. B.1.4.3. Lead: T. Gan-Erdene
International Collaborative Projects:
(Mongolia-South Korea) "To express disulfide bond-containing protein in coli" /2024/. KIST School Partnership project Plus. Principal Investigator of the Project: E.Erdenedolgor
(Mongolia-Taiwan) "Isolation and Characterization of Camel Milk Proteins" /2011–2013/. NTS-MECS 2011003. Principal Investigator of the Project from Mongolian side: T.Gan-Erdene
(Mongolia-Russia) "Study on the effect of enzyme degradation of carbamide on the rheological properties of Mongolian crude oil" /2009–2010/. RUS_09/003. Lead: T. Gan-Erdene
Laboratory Capacity and Competency
The laboratory of Protein Chemistry and Technology has 10 research staff members (2 academicians, doctors of science, 2 doctors of philosophy, 5 master’s degree holders, and 1 bachelor’s degree holder).
Capabilities include:
Determining physical-chemical properties of protein raw materials and products, and conducting technological experiments;
Isolating protein compounds, and producing their derivatives while studying their structures and biological activities;
Expressing recombinat proteins, and studying their practical use.
Collaborations
East Siberian State University of Technology and Management, Leather and Fur Technology Department (Russia)
Korea Institute of Science and Technology, Gangneung Branch (South Korea)
Siberian Branch of the Russian Academy of Sciences, Institute of Natural Resource Utilization (Russia)
National University of Mongolia, School of Sciences
Mongolian University of Life Sciences, Institute of Veterinary Medicine
Institute of Traditional Medicine and Technology
Monos Pharmaceuticals Research Institute
Moncreаm LLC
APU Company
Highlighted Research Outcomes (Last 5 Years)
Laboratory of Protein Chemistry and Technology has successfully implemented experimental research to develop theoretical and technological foundations for comprehensive utilization of secondary protein-rich raw materials from Mongolia’s food and light industries.
Technological advancements were made in producing protein hydrolysates from raw materials such as brewery yeast waste and leather industry wastes. Relevant technical documentation was developed, leading to applications in cosmetics (haircare products) and livestock feed additives.
For example, Moncream LLC utilizes brewery yeast hydrolysates to produce hair care shampoos, conditioners, and protein-based products targeting grey hair treatment.
We successfully developed the feasibility study for a Model protein production facility that will produce high-value protein products using casein, spent brewer's yeast, and hides. The plant is designed to manufacture 4.4 tons of product annually, including three types of protein hydrolysates and sodium caseinate.
A protein hydrolysate derived from limed cattle hide splits was used to partially replace soybean protein in the feed of laying hens. A 21-day trial conducted at “Mogul Farm” LLC on 60 hens divided into three groups showed increased egg production and improved eggshell thickness. Feed efficiency analysis revealed that hens in the test group required 0.2 kg less feed to produce 10 eggs compared to the control group, demonstrating clear economic benefits.
Young researchers, in collaboration with other units, achieved a significant milestone by winning 15 million MNT for their innovation in "Collagen gel production technology" at the "Erdem Hackathon – 2021."
As an initial step toward synthesizing recombinant proteins and implementing them in practice, a collaborative project was conducted with South Korea.
Articles published in journals indexed with IF (Impact Factor), Scopus, and WoS (Web of Science)
Lebedeva S.N., Tykheev A.A., Shalbuev D.V., Tumurova T.B., Bayarjargal M., Jamsaranova S.D. (2022). Evaluation of the reparative effectiveness of collagen matrices using a thermal burn model. //Acta biomedica scientifica. 7(1): 220-231. DOI: 10.29413/ABS.2022- 7.1.25
Bayarjargal Munkhuu, Lkhagvamaa Erdene, Zolzaya Bayarsukh, Enkh-Ariun Altantulga, Oyuntuya Baltsukh, Gan-Erdene Tudev, Ariun Narmandakh (2021). Antioxidant and Antihypertensive Activity of Collagen and Elastin Hydrolysate at Different Molecular Weights. //Atlantis Highlights in Chemistry and Pharmaceutical Sciences, Vol.2. DOI: 10.2991/ahcps.k.211004. 004
Erdene-Ochir E., Shin B.K., Huda M.N., Lee E.H., Song D.G., Jung C.K. and Pan C.H. (2021). Characterization of endogenous promoters of GapC1 and GS for recombinant protein expression in Phaeodactylum tricornutum. Microbiology Open, 10 (5): e1239
Liang Ming, Liyun Yuan, Li Yi1, Guohui Ding, Surong Hasi, Gangliang Chen, Tuyatsetseg Jambl, Nemat Hedayat-Evright, Mijiddorj Batmunkh, Garyaeva Khongr Badmaevna, Tudeviin Gan-Erdene, Batsukh Ts, Wenbin Zhang, Azhati Zulipikaer, Hosblig, Erdemt, Arkady Natyrov, Prmanshayev Mamay, Narenbatu, Gendalai Meng, Choijilsuren Narangere, Orgodol Khongorzul, Jing He, Le Hai, Weili Lin, Sirendalai, Sarentuya, Aiyisi, Yixue Li, Zhen Wang & Jirimutu. (2020). Whole-genome sequencing of 128 camels across Asia reveals origin and migration of domestic Bactrian camels. Biol., 3(1):1-9
Enkh-Ariun Altantulga, Lkhagvamaa Erdene, Ariun Narmandakh, Janbolat Ashim, Bayarjargal Munkhuu, Zolzaya Majigsuren, Batjargal Batdorj, Gan-Erdene Tudev (2020). Isolation of Heavy Chain Antibodies from Camelus BactrianusCent. Asian J. Med. Sci., 6(3): 159-66
Cha K.H., Yang J.S., Kim K.A., Yoon K.Y., Song D.G., Erdene-Ochir E., Kang K.S., Pan C.H. and Ko G.P. (2020). Improvement in host metabolic homeostasis and alteration in gut microbiota in mice on the high-fat diet: A comparison of calcium supplements. Food Res. Int.,136: 109495
Erdene-Ochir E., Shin B.K., Kwon B.R., Jung C.K. and Pan C.H. (2019). Identification and characterisation of the novel endogenous promoter HASP1 and its signal peptide from Phaeodactylum tricornutum. Scientific Reports, 9: 9941
Huda M.N., Erdene-Ochir E., Pan C.H. (2017). Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells. Vis. Exp., 128: e55932
Erdene-Ochir E., Shin B.K., Huda M.N., Kim D.H., Lee E.H., Song D.G., Kim Y.M., Kim S.M., Pan C.H. (2016). Cloning of a novel endogenous promoter for foreign gene expression in Phaeodactylum tricornutum. Biol. Chem., 59: 861-867
Huda M.N., Kim D.H., Erdene-Ochir E., Kim Y.S., Pan C.H. (2016). Expression, phosphorylation, localization, and microtubule binding of tau in colorectal cell lines. Biol. Chem., 59: 807-812
Erden Erdenetsogt, Nadezhda A.Golubkina, Sergei M.Nadegkin, Bayardjargal Monhoo, Jamiyan Batjargal (2014). Health risk connected with the low Selenium levels in foodstuffs of Mongolia. Nat. Resour. J., 4 (3): 192-203
Bayarjargal M., Ariunsaikhan Ts., Lkhagvamaa E., Ankhtsetseg B., Gan-Erdene T., Regdel D. (2014). Antioxidant properties of pancreatic hydrolysates from various Protein sources. J. Chem., 15 (41): 43-46.
Ganbaatar J., Tamir O., Lkhagvamaa E., Tsiiregzen A., Oyuntsetseg J., Bayarjargal M. (2014). Antioxidative activity of Silybum marianum cultivated in Mongolia. J. Chem., 15 (41): 53-55
Altunina L.K., Fufaeva M.S., Filatov D.A., Svarovskaya L.I., Gan-Erdene T. (2013). The use of cryogels for stabilizing soils prone to deflation. Cryosphere of the Earth, 17(3): 83-88.
Bayarjargal M., Munkhbat E., Ariunsaikhan Ts., Odonchimeg M., Uurzaikh T., Gan-Erdene T., Regdel D. (2011). Preparation of yeast hydrolysate using spent brewer’s yeast. J. Chem., 12(38): 88-91
Zorin S.N., Bayarjargal M. (2009). Production of enzymatic hydrolysates of food proteins using certain commercial enzyme preparations and various hydrolysis schemes. Biomedical Chemistry, 5(1): 73-80.
Bayarjargal M., Zilova I.S., Zorin S.N., Gmoshinsky I.V., Buchanova A.V., Shevyakova L.V., Makhova N.N., Mazo V.K. (2008). Comparative evaluation of the bioavailability of organic and inorganic forms of zinc in vivo. Issues of Nutrition, 77(1): 34-37.
Gmoshinsky I.V., Munkhuu B., Mazo V.K. (2006). Trace elements in human nutrition: biological indicators of zinc deficiency. Issues of Nutrition, 76(1): 10-12.
Mazo V.K., Zorin S.N., Bayarjargal M., Gmoshinsky I.V., Burdza E.A. (2005). New food sources of essential elements. Brief communication 6: Production and physicochemical characteristics of certain new food sources of zinc, copper, manganese, chromium, and selenium. Issues of Pediatric Nutrition, 3(5): 19-21.
Keith D. Wilkinson, Tudeviin Gan-Erdene, and Nagamalleswari Kolli (2005). Derivitization of the C-terminus of Ubiquitin and Ubiquitin-like Proteins Using Intein Chemistry Methods and Uses. Methods in Enzymology, 399: 37-51
David Reverter, Kenneth Wu, Tudeviin Gan Erdene, Zhen-Oiang Pan, Keith D. Wilkinson and Christopher D. Lima (2005). Structure of a Complex between Nedd8 and the Ulp/Senp Protease Family Member Den1. Mol. Biol., 345(1): 141-151
Martin Horn, Lucie Doleckova-Maresova, Lubomir Rulisek, Martin Masa, Olga Vasiljeva, Boris Turk, Tudeviin Gan-Erdene, Miroslav Baudys and Micheal Mares (2005). Activation processing of cathepsin H impairs recognition by its propeptide. Chem., 386(9): 941-947
Hemelaar J, Borodovsky A, Kessler BM, Reverter D, Cook J, Kolli N, Gan-Erdene T, Wilkinson KD, Gill G, Lima CD, Ploegh HL, Ovaa H. (2004). Specific and Covalent Targeting of Conjugating and deconjugating Enzymes of Ubiquitin-Like Proteins. Cell Biol., 24(1): 84-95
Tudeviin Gan-Erdene, Nagamallesawari Kolli, Luming Yin, Kenneth Wu, Zhen-Quing Pan and Keith D. Wilkinson (2003). Identification and Characterization of DEN1, A Denedylase of ULP family. Biol. Chem., 278 (31): 28892-900
Kenneth Wu, Kosj Yamoah, Georgia Dolios, Tudeviin Gan-Erdene, Peilin Tan, Angus Chen, Chee-gun Lee, Ning Wei, Keith D. Wilkinson, Rong Wang and Zhen-Qiang Pan (2003). DEN1 is a dual function protease capable of processing the C-terminus Nedd8 and deconjugating hyper-neddylated CUL1. Biol. Chem., 278 (31): 28882-91
Anna Brodovsky, Huib Ovaa, Nagamalleswari Koli, Tudeviin Gan-Erdene, Keith D. Wilkinson, Hidde L. Ploegh and Benedikt M. Kessler (2002). Chemistry-Based functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family. Biol., 9(10): 1149-1159
Regdel D., Kühn H, Schewe T. (1994). On the reaction specificity of the lipoxygenase from tomato fruits. Biophys. Acta, 1210(3): 297-302
Baudys M., Meloun B., Gan-Erdene T., Fusek M., Mares M., Kostka V., Pohl J. and Blake C.C.F. (1991). S-S Bridges of Cathepsin B and H from Bovine Spleen. A basis for Cathepsin B. Model Building and Possible Functional Implications for Discriminations between Exo-and Endopeptidase Activities among Cathepsins B, H and L. Biochim. Acta, 50(4-6): 569-577
Baudys M., Meloun B., Gan-Erdene T., Pohl J. and Kostka V. (1990). Disulfide Bridges of Bovine Spleen Cathepsin B. Chem. Hoppe-Seyler,71(6): 485-491
Baudys M., Gan-Erdene T., Kostka V., Pavlik M. and Foltman B. (1988). Comparison between Prochymosin and Pepsinogen from Lamb and Calf. Biochem. Physiol., 89(2): 385-391
Regdel D., Schewe T., Rapoport S.M. (1985). Enzymatic properties of the lipoxygenase from pea seeds. Biochim. Acta, 44(10): 1411-28
Current Members:
Regdel, Academician, (Sc.D), Advisor
Gan-Erdene, Principal Researcher, Academician, (Sc.D)
