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Non-viable burn eschar proteins consist of the denatured extracellular matrix components, such as collagen and elastin, that result from thermal or chemical injury to the skin [1]. This necrotic tissue, known as eschar, forms a rigid layer that prevents natural wound healing and serves as a reservoir for microbial colonization and subsequent sepsis [1, 3]. In clinical practice, these proteins are the primary target for enzymatic debridement therapies, which aim to remove devitalized tissue without the trauma of surgical excision [2]. Proteolytic enzymes, such as those derived from bromelain or Clostridium histolyticum, interact with these proteins by breaking down the cross-linked, damaged fibers into soluble fragments [2, 4]. By selectively degrading the non-viable protein matrix, these treatments prepare the wound bed for spontaneous re-epithelialization or grafting [3]. Successful removal of these proteins is a critical step in burn management to reduce inflammation and promote the formation of healthy granulation tissue [1, 2].
Enzymatic proteolysis and hydrolysis of denatured extracellular matrix proteins, specifically targeting damaged collagen and elastin within necrotic tissue while sparing viable dermis [2, 4].
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