Elastase & Hyaluronidase

esterase and amidase activity. Nevertheless, Elastases possess a unique ability among proteases to digest native elastin, a substrate untouched by trypsin, chymotrypsin, or pepsin.

Given that elastin predominates in elastic fibres within connective tissues such as skin, blood vessels, and lungs, Elastase finds significant application in dissociating tissues with extensive intercellular fibre networks. Typically, it is used in combination with other enzymes like collagenase, trypsin, and chymotrypsin. As such, Elastase stands as the enzyme of choice for isolating Type II cells from the lung.

The Soybean Trypsin Inhibitor suppresses the proteolytic but not elastolytic activity of Elastase. The Soybean Trypsin Inhibitor is animal free.

Hyaluronidase

Hyaluronidase, a hydrolase, is an enzyme that catalyses the degradation of hyaluronic acid, a key component of the extracellular matrix in connective tissues and synovial fluid in joints.

In medicine, Hyaluronidases are sometimes used as adjuvants to enhance the absorption and dispersion of drugs injected into the body, as they can temporarily increase tissue permeability.

Hyaluronidase treatment can improve the penetration of other enzymes used in tissue dissociation protocols, such as collagenase and trypsin. By breaking down the hyaluronic acid-rich ECM, Hyaluronidase facilitates the access of these enzymes to their respective substrates, thereby increasing the efficiency of tissue dissociation.