Produção e purificação de proteases de Aspergillus tamarii URM 4634 para aplicação no amaciamento de carnes

Abstract

Enzymatic biotechnology is one of the most promising scenarios when it comes to the production, purification and application of high value-added molecules, such as enzymes. Proteases belong to a specific group of enzymes that are capable of catalyzing hydrolytic reactions, which results in the cleavage of proteins into smaller molecular weight molecules such as amino acids and peptides. One of the sources of protease production is through the microorganisms that in the production stages involve upstream and downstream processes. Solid State Fermentation (SSF) is an intermediate operation of these processes, and can be conduceted with the use of filamentous fungi such as Aspergillus tamarii. Through these processes, together with a purification step, the collagenases can be obtained which are responsible for the hydrolysis of the bonds of the native and denatured collagen peptides. Among its main applications is the softening of meats. In view of the above, the present study had the production of proteases with collagenolytic activity by SSF, as well as its purification by ion exchange chromatography for further evaluation of its potential in the tenderization of meats. The protease obtained showed a collagenolytic activity of 296.6 U/mL and presented purification factor of 6.28 fold. The tenderization process showed the strong efficiency of the enzyme to degrade the myofibrillar proteins noticed by the high Myofibrillar Fragmentation Index (250.8) corresponding to a Relative Fragmentation of 292.0%. The results obtained demonstrate the great potentiality of the collagenase obtained from Aspergillus tamarii to be used as a meat tenderizer.