Recombinant collagenase from Grimontia hollisae as a tissue dissociation enzyme for isolating primary cells.

ABSTRACT: Collagenase products are crucial to isolate primary cells in basic research and clinical therapies, where their stability in collagenolytic activity is required. However, currently standard collagenase products from Clostridium histolyticum lack such stability. Previously, we produced a recombinant 74-kDa collagenase from Grimontia hollisae, which spontaneously became truncated to ~60 kDa and possessed no stability. In this study, to generate G. hollisae collagenase useful as a collagenase product, we designed recombinant 62-kDa collagenase consisting only of the catalytic domain, which exhibits high production efficiency. We demonstrated that this recombinant collagenase is stable and active under physiological conditions. Moreover, it possesses higher specific activity against collagen a

SUBMITTER: Tanaka K 

PROVIDER: S-EPMC7054364 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature