Recombinant Human Lysozyme

Recombinant Human Lysozyme: A High-Purity, Animal-Free Solution

The antimicrobial enzyme lysozyme catalyzes the hydrolysis of glycosidic bonds in polymeric peptidoglycans, which are the major structural component within the cell walls of gram-positive bacteria. While lysozyme is naturally found in animals as part of the innate immune system, recombinant human lysozyme provides a scalable, animal-free alternative for bioprocessing, protein purification, and research applications. As a component of the innate immune defenses of animals, lysozyme is found in macrophage and neutrophil cytoplasmic granules, in mucosal secretions such as tears, saliva, milk, and airway fluids, and also in egg whites. Once compromised by lysozyme activity, the bacterial cell wall is no longer able to help regulate osmotic pressure on the bacterial membrane, leading to lysis. Research and commercial technologies take advantage of this activity in recombinant protein expression and bioprocess fermentation, using lysozyme treatment as one of the first steps toward extracting proteins for isolation and purification from the bacterial host.

Lysozyme also plays an important role as a cost-effective natural replacement for chemical antibiotics in livestock feed, and as a natural, immune-boosting alternative to chemical preservatives to prolong shelf life in fermented foods intended for human consumption.

While the most common commercial source of lysozyme is from chicken egg whites, eggs are also a common trigger of clinically significant allergic reactions. InVitria offers Lysobac®, a recombinant human lysozyme produced in a scalable, egg-free, non-mammalian expression system. It is completely free of animal or human components and egg allergens, making it ideal for demanding research and commercial applications.

Lysobac is a recombinant human lysozyme, an animal-free alternative to chicken-egg or purified human lysozyme, ideal for bioprocessing and protein purification. for the recovery of recombinant proteins expressed in bacteria such as E. coli and Micrococcus. Expressed and purified from an animal-free system, Lysobac has an identical amino acid sequence and physiochemical properties to the native human form of lysozyme. It exhibits four times the hydrolytic activity against gram-positive bacteria compared to commercially available chicken-egg lysozyme. The high activity and purity of this product make it ideal for applications in bioprocessing, diagnostics, and life sciences research.

Discover how plant-based production enhances the purity and efficacy of recombinant human lysozyme in this comprehensive review.