Practical approaches to decomposition of hard-to-degrade proteins by thermoophilic enzymes.

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We studied the decomposition of hard-to-degrade proteins by thermophilic bacteria through this project. Among hard-to-degrade proteins, we, in particular, focused on collagen and keratin. The strains we isolated and used for this project are Geobacillus collagenovorans MO-1, Aneurinibacillus sp.AM-1, and Meiothermus sp.H328. First, we analyzed the collagen-binding ability of the collagenolytic protease from a G.collagenovorans MO-1 to realize how the enzyme functions for collagen degradation. In addition, two isozymes of Pz-peptidases produced by the strain were investigated how the enzymes recognized and cleaved collagen fragments produce by the collagenolytic protease in detail. Then, we indicated the utility of a Pro-specific aminopeptidase from strain AM-1 for collagen fragments. Furthermore, we found that strain H328 efficiently degrades feather keratin which is vast industrial waste. The intermediate products derived from keratin decomposition by strain H328 were observed to be potent as an anti-oxidant substance for rat neuron cells. Collaborating with a group of Kyoto University, we have started the X-ray crystallography analysis for two Pz-peptidases and Pro-specific amino peptidase.