Fig. 3.

Fig. 3. Schematic diagram of the autoprocessing maturation of TSS and its degradation on type I collagen at high temperatures. TSS is synthesized as a precursor (pre-TSS) within Brevibacillus sp. WF146 and then secreted outside the host by a signal peptide. After being cleaved by a specific signal peptidase, the precursor folds into a proprotein (pro-TSS), which subsequently converts into an intermediate (iTSS) by removing the N-terminal propeptide. Finally, it becomes a mature enzyme (mTSS) by removing the PPC domain. At room temperature, collagens exist in a naturally triple-helical state. However, under high-temperature conditions, their molecular structure becomes loosely packed, resulting in the dissolution of some collagens into the solution. In solution, mTSS can bind to the surface of soluble collagens and degrade them. Additionally, when mTSS is adsorbed onto insoluble substrates, it degrades both insoluble and soluble collagen. The small degradation products can be absorbed and utilized by the host for metabolism.

© J. Microbiol. Biotechnol.