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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 and cleaves a wider variety of collagens than a standard collagenase product from  C. histolyticum . Furthermore, it dissociated murine pancreata by digesting the collagens within the pancreata in a dose-dependent manner, and this dissociation facilitated isolation of pancreatic islets with masses and numbers comparable to those isolated using the standard collagenase from  C. histolyticum . Implantation of these isolated islets into five diabetic mice led to normalisation of the blood glucose concentrations of all the recipients. These findings suggest that recombinant 62-kDa collagenase from  G. hollisae  can be used as a collagenase product to isolate primary cells.

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