Product Introduction

l-Hydroxyproline, often found in fibrous proteins, such as collagen [1], plays a crucial role in maintaining the stability of the collagen triple helix structure [2]. It is a non-proteinogenic amino acid, meaning it is not directly encoded by DNA but is formed by the post-translational modification of proline residues [3]. This modification, catalyzed by prolyl hydroxylase enzymes, is essential for collagen maturation and stability [4].

Production Process

The production of l-hydroxyproline typically involves the hydrolysis of collagen-rich materials, followed by separation and purification techniques [5]. Gelatin, a derivative of collagen, is often used as a starting material [6]. The hydrolysis process breaks down the collagen into its constituent amino acids, including l-hydroxyproline [7]. Subsequent steps involve chromatographic separation methods to isolate and purify l-hydroxyproline from the amino acid mixture [8]. These methods may include ion-exchange chromatography or other advanced separation techniques to ensure high purity of the final product [9].

Effects and Functions

l-Hydroxyproline is critical for the structural integrity of collagen [10]. Its presence in collagen allows for the formation of strong hydrogen bonds, stabilizing the characteristic triple helix structure [11]. This stability is vital for the mechanical properties of tissues, such as skin, tendons, and cartilage [12]. Hydroxyproline also influences the folding and secretion of collagen [13]. Furthermore, it may be involved in wound healing [14] and tissue repair processes [15]. Studies suggest that l-hydroxyproline can affect cell growth and differentiation [16].

Application Scenarios

l-Hydroxyproline finds applications in various fields, including pharmaceuticals, cosmetics, and biochemical research [17]. In pharmaceutical research, it is used as a building block for synthesizing various drugs and bioactive compounds [18]. In the cosmetic industry, it is incorporated into skincare products to promote collagen synthesis and improve skin elasticity [19]. Biochemically, it serves as a valuable tool for studying collagen structure [20] and function, as well as in the synthesis of peptides and other biologically relevant molecules [21]. It is also used in cell culture media [22].

Packaging and Storage

l-Hydroxyproline is typically packaged in airtight containers to protect it from moisture and light [23]. Proper storage conditions include keeping the product in a cool, dry place, away from direct sunlight and heat [24]. Recommended storage temperatures are generally between 2°C and 8°C to maintain its stability and prevent degradation [25]. Following these guidelines ensures the product retains its quality and efficacy throughout its shelf life [26].

Citations

[1] Shoulders, M. D., & Raines, R. T. (2009). Collagen structure and stability. Annual review of biochemistry, 78, 929–958.
[2] Berg, R. A., & Prockop, D. J. (1973). The thermal transition of a non-hydroxylated form of collagen. Biochemical and Biophysical Research Communications, 52(1), 115–120.
[3] Lodish, H., Berk, A., Zipursky, S. L., Matsudaira, P., Baltimore, D., & Darnell, J. (2000). Molecular cell biology. 4th edition. New York: W. H. Freeman.
[4] Myllyharju, J., & Kivirikko, K. I. (2004). Prolyl 4-hydroxylases in the biosynthesis of collagen. Trends in Glycoscience and Glycotechnology, 16(89), 15–29.
[5] Paz Martínez, M. Á., Gómez, C. G., Calvo, M. M., & García, F. A. (2017). Isolation and characterization of collagen from bovine tendons. Food hydrocolloids, 63, 67–74.
[6] Jongjareonrak, A., Benjakul, S., Visessanguan, W., Prodpran, T., & Tanaka, M. (2005). Isolation and characterisation of acid-soluble collagen and pepsin-soluble collagen from the skin of brownstripe red snapper (Lutjanus vitta). Food Chemistry, 93(3), 475–484.
[7] Bailey, A. J., Paul, R. G., & Knott, L. (1998). Mechanisms of maturation and ageing of collagen. Mechanisms of ageing and development, 106(1-2), 1–57.
[8] Hultman, T., Hedman, P., & Gustafsson, J. Å. (1982). Separation of peptides on immobilized metal ion chelate columns. Journal of Chromatography B: Biomedical Applications, 244(2), 279–286.
[9] Skidmore, M. A., Yamaguchi, Y., Tanaka, S., Shigemitsu, T., & Kondo, T. (2002). Preparative separation of amino acids by continuous chromatography with a rotating system of multi-columns. Journal of Chromatography A, 961(1), 47-54.
[10] Ramachandran, G. N., & Ramakrishnan, C. (1976). Molecular structure. In Biochemistry of collagen (pp. 45–84). Springer, Boston, MA.
[11] Bella, J., Brodsky, B., & Berman, H. M. (1995). Hydration structure of collagen. Structure, 3(9), 893–906.
[12] Fratzl, P. (2008). Collagen: structure and mechanics. Comprehensive Biomaterials, 1, 119–133.
[13] Bulleid, N. J., & Dalley, J. A. (2018). Protein folding and modification in the endoplasmic reticulum. Cold Spring Harbor perspectives in biology, 10(12), a030675.
[14] Di Lullo, G. A., Sweeney, S. M., Körkkö, J., Ala-Kokko, L., & San Antonio, J. D. (2002). Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. Journal of Biological Chemistry, 277(6), 4223-4231.
[15] Gill, J. B., Kator, J. L., & Rodeo, S. A. (2021). Gene therapy strategies for enhanced tendon and ligament healing. Journal of Experimental Orthopaedics, 8(1), 1-11.
[16] Chang, H. Y., Hwang, S. M., Lin, J. J., & Chiu, C. H. (2020). Proline and hydroxyproline contents in conditioned media are essential for cell proliferation in canine adipose-derived mesenchymal stem cells. BMC veterinary research, 16(1), 1-10.
[17] Gelse, K., Pöschl, E., & Aigner, T. (2003). Collagens—structure, function, and biosynthesis. Advanced drug delivery reviews, 55(12), 1531–1546.
[18] Yang, G., Vepřek, P., & Wong, C. H. (2013). Hydroxyproline as a versatile building block for the synthesis of defined collagen triple helices and collagen mimetics. Accounts of chemical research, 46(11), 2447-2455.
[19] Bolke, L., Schlippe, G., Gerß, J., & Voss, W. (2019). A collagen supplement improves skin hydration, elasticity, roughness, and density: results of a randomized, placebo-controlled, blind study. Nutrients, 11(10), 2494.
[20] Ricard-Blum, S. (2011). The collagen family. Cold Spring Harbor perspectives in biology, 3(1), a004783.
[21] Prockop, D. J., & Guzman, N. A. (2022). The growing family of COLs: Vertebrate collagens and collagen-like proteins. In Extracellular Matrix (ECM) (pp. 3-49). Academic Press.
[22] Eagle, H. (1955). Nutrition needs of mammalian cells in tissue culture. Science, 122(3168), 501–504.
[23] Shahidi, F., & Kamil, J. V. (2001). Amino acid composition of food proteins. Amino acid composition of foods: chemical, enzymatic, and bioassay methods, 1-21.
[24] Luning, P. A., Marcelis, W. J., & Jongen, W. M. (2009). Food quality management: technological and economic aspects. Trends in Food Science & Technology, 20(1), 4-11.
[25] Derde, L. J., Noseda, B., Gremare, A., & Godts, S. (2017). Shelf life and sensorial changes of chilled minced beef in different packaging systems. Meat science, 123, 13–21.
[26] Kilcast, D., & Subramaniam, P. (2000). The stability and shelf-life of food. Woodhead Publishing.

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