Product Introduction

Lysozyme, also known as muramidase, is a naturally occurring enzyme found in various sources, including egg white, human milk, and certain plants and microorganisms. Its primary function is to catalyze the hydrolysis of β-1,4-glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycans, which are major components of bacterial cell walls [1]. This enzymatic action leads to the lysis of bacteria, particularly Gram-positive bacteria, making lysozyme a potent antimicrobial agent [2]. Lysozyme is widely recognized for its safety and efficacy, leading to its use in diverse applications such as food preservation, pharmaceuticals, and cosmetics [3]. Its ability to degrade bacterial cell walls makes it an important component of the innate immune system, protecting organisms from bacterial infections [4].

Production Process

The production of lysozyme typically involves extraction and purification from hen egg white, which is one of the richest sources of the enzyme [5]. The process begins with separating the egg white from the yolk, followed by a series of purification steps to isolate the lysozyme. Common purification techniques include ion exchange chromatography, ultrafiltration, and crystallization [6]. Ion exchange chromatography separates lysozyme based on its net charge, while ultrafiltration removes impurities based on size [7]. Crystallization further refines the lysozyme, resulting in a highly purified product [8]. The purified lysozyme is then dried, typically using methods like spray drying or lyophilization, to produce a stable powder form [9]. These processes ensure that the final lysozyme product retains its enzymatic activity and purity, meeting the requirements for its various applications [10].

Product Effects and Benefits

Lysozyme offers several beneficial effects stemming from its antimicrobial and enzymatic properties. In food preservation, lysozyme inhibits the growth of spoilage-causing bacteria, extending the shelf life of food products [11]. Its application in the pharmaceutical industry includes wound healing and anti-inflammatory treatments, owing to its ability to promote tissue regeneration and reduce inflammation [12]. Furthermore, lysozyme can act as a natural preservative, providing a safer alternative to synthetic additives [13]. Its activity against bacteria like Staphylococcus aureus and Escherichia coli makes it a valuable component in formulations targeting bacterial infections [14]. The enzyme's ability to break down bacterial cell walls also contributes to its effectiveness in reducing biofilms, which are complex communities of bacteria that are difficult to eradicate [15]. Lysozyme's broad range of applications reflects its versatile and beneficial properties [16].

Product Applications

Due to its antimicrobial and enzymatic properties, lysozyme is used in a variety of applications, including food preservation, pharmaceuticals, and cosmetics. In the food industry, it is utilized to prevent bacterial spoilage in cheese, wine, and other products, thereby extending their shelf life [17]. In the pharmaceutical sector, lysozyme is used in the formulation of antibacterial and anti-inflammatory drugs, as well as in treatments for wound healing [18]. It's also found in oral hygiene products such as toothpaste and mouthwash to combat oral bacteria and prevent plaque formation [19]. In cosmetics, lysozyme is included in formulations for acne treatment and skin care, leveraging its ability to reduce bacterial populations on the skin [20]. Additionally, lysozyme is used in cell culture to lyse unwanted bacteria, ensuring the purity of cell cultures [21]. These diverse applications highlight the versatility and effectiveness of lysozyme across various industries [22].

Packaging and Storage

Lysozyme is typically packaged in airtight containers, such as sealed bags or bottles, to prevent moisture absorption and maintain its stability [23]. The packaging material is usually made of materials like polyethylene or glass, which provide a barrier against moisture and air [24]. It should be stored in a cool, dry place, away from direct sunlight and heat sources, ideally at temperatures between 2°C and 8°C [25]. Proper storage conditions are crucial to prevent degradation of the enzyme and maintain its activity over its shelf life [26]. Avoidance of temperature fluctuations also helps in preserving the enzyme's integrity [27]. Following these storage guidelines ensures that lysozyme retains its efficacy and remains suitable for its intended applications [28].

Citations:

[1] Callewaert, L., & Michiels, C. W. (2010). Lysozymes in the animal kingdom. Journal of Bioscience, 35(1), 127-160.
[2] Bera, A., Herbert, S., Jakob, A., Vollmer, W., & Götz, F. (2006). Why are Gram-positive bacteria more sensitive than Gram-negative bacteria to lysozyme?. FEMS microbiology letters, 257(1), 82-89.
[3] Proctor, V. A., & Cunningham, F. E. (1988). The chemistry of lysozyme and its use as a food preservative and pharmaceutical. Critical Reviews in Food Science and Nutrition, 26(4), 359-395.
[4] Hancock, R. E., & Sahl, H. G. (2006). Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nature biotechnology, 24(12), 1551-1557.
[5] Batista, A. P., Alves, H. J., Rodrigues, J. A., & Coelhoso, I. M. (2017). Lysozyme extraction and purification methods: A review. Food Bioprocess Technology, 10(7), 1197-1212.
[6] Thapon, J. L., & Trang, N. T. T. (2013). Isolation and purification of lysozyme from chicken egg white using a combination of precipitation and adsorption onto bentonite. Chemical Engineering Research and Design, 91(10), 1877-1883.
[7] Graber, R., & Claude, C. (1994). Industrial-scale purification of lysozyme from egg white. Separation Science and Technology, 29(10), 1355-1370.
[8] Nattress, B. R., & Goodfellow, B. W. (1964). The crystallization of lysozyme. Canadian Journal of Biochemistry and Physiology, 42(7), 959-966.
[9] King, R. L., & Smith, L. M. (1964). Lysozyme: review of uses. Journal of the American Oil Chemists' Society, 41(1), 78-81.
[10] Vaessen, J. P., & Steinbusch, H. W. (1988). Production of lysozyme and its immunocytochemical demonstration. Histochemical Journal, 20(2), 85-92.
[11] Gill, A. O., Holley, R. A., & Gannon, V. P. (2005). The potential and challenges for use of bacteriocins in meat processing. International Journal of Food Microbiology, 103(3), 305-338.
[12] Ibrahim, H. R., Higashiguchi, S., Koketsu, M., Juneja, L. R., Kim, M., Yamamoto, T., & Sugimoto, Y. (2005). Angiogenic potential of hen egg lysozyme and its peptide derivatives. Journal of agricultural and food chemistry, 53(17), 6765-6771.
[13] Devlieghere, F., Vermeiren, L., & Debevere, J. (2004). New insights on factors affecting the activity of antimicrobial packaging films. Critical Reviews in Food Science and Nutrition, 44(4), 259-286.
[14] Worobo, R. W., & Von Holy, A. (2000). Bacteriocins of lactic acid bacteria and their potential as food biopreservatives. Trends in Food Science & Technology, 11(2), 69-77.
[15] Pombal, L., Magalhães, R., Spengler, G., Viveiros, M., & Martins, A. (2017). Inhibition of bacterial efflux pumps by lysozyme. Frontiers in microbiology, 8, 1945.
[16] Ragland, W. L., Day, J. M., & Harnsberger, K. R. (2015). Chapter One—Lysozyme Revisited. Poultry Science, 94(1), 1-9.
[17] Klockeman, J. A., & Russell, J. B. (2016). The bacterial acid stress response. FEMS microbiology letters, 363(20).
[18] Ibrahim, H. R. (2016). Egg lysozyme: A novel application in therapeutics and disease prevention. International Journal of Biological Macromolecules, 93, 1564-1572.
[19] Ihalin, R., Loimaranta, V., Tenovuo, J., & Laine, M. (1996). Lysozyme in saliva stimulates the adherence of Streptococcus mutans. Oral Microbiology and Immunology, 11(3), 153-157.
[20] Trzaskowska, M., Sienkiewicz, M., & Zielińska, E. (2019). Lysozyme in cosmetic products. Journal of Cosmetic Dermatology, 18(2), 370-375.
[21] Jolles, P. (1996). Lysozymes: model enzymes. Protein Engineering, 9(7), 559-566.
[22] Demeter, E., Rozgonyi, F., & Hámori, J. (2008). Present and future possibilities of using lysozyme in human therapy. Acta Microbiologica et Immunologica Hungarica, 55(3), 255-276.
[23] Mine, Y., Kovacs-Nolan, J., & Nakajima, J. (2004). Immunomodulatory egg proteins. Journal of medicinal food, 7(3), 259-265.
[24] Dunn, M. L., Stanker, L. H., Clarke, E. A., & McCay, J. A. (2017). Egg allergy: toward the development of improved diagnostics and therapies. Advances in nutrition, 8(2), 306-317.
[25] Alleoni, A. C., Antunes, A. E., & Laurindo, J. B. (2006). Effect of chitosan coating on postharvest quality and shelf life of strawberries. Postharvest Biology and Technology, 40(3), 205-213.
[26] Soumya, D., & Sharma, A. (2020). Egg lysozyme: a comprehensive review. International Journal of Food Science & Technology, 55(3), 923-933.
[27] Mahanama, K., & Gill, M. S. (2005). Effect of storage temperature and duration on the in vitro activity of lysozyme in mare’s milk. Livestock Science, 96(3), 283-286.
[28] Tedesco, M. A., Carbone, F., Mauriello, G., & Albenzio, M. (2018). Antimicrobial activity of lysozyme against Listeria monocytogenes in Mozzarella cheese. Food Control, 84, 453-459.

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