Abstract: There are gluten-degrading enzymes found in Rothia species bacteria that are subtilisins that belonging to the S8A family of serine protease family. The Rothia sp. derived subtilisin-like enzymes have the conserved catalytic triad composed of a Ser, His, and Asp residues that is characteristic of the serine protease family. The Rothia subtilisin enzymes are potent at cleaving proline-containing proteins, cleaving the second peptide bond after proline in the XPX1 motif, where X is any amino acid, P is proline and X1 is a hydrophobic amino acid, e.g. the XPQ motif, where Q is glutamine. Embodiments herein provide isolated enzyme compositions and formulations comprising subtilisins gluten-degrading enzyme from a Rothia species bacteria. Also provided herein are methods of treatment of celiac disease or a related disorder, treatment of gluten-containing foodstuff, degrading and/or detoxifying gluten comprising the subtilisins gluten-degrading enzyme and/or compositions.

Abstract: There are gluten-degrading enzymes found in Rothia species bacteria that are subtilisins that belonging to the S8A family of serine protease family. The Rothia sp. derived subtilisin-like enzymes have the conserved catalytic triad composed of a Ser, His, and Asp residues that is characteristic of the serine protease family. The Rothia subtilisin enzymes are potent at cleaving proline-containing proteins, cleaving the second peptide bond after proline in the XPX1 motif, where X is any amino acid, P is proline and X1 is a hydrophobic amino acid, e.g. the XPQ motif, where Q is glutamine. Embodiments herein provide isolated enzyme compositions and formulations comprising subtilisins gluten-degrading enzyme from a Rothia species bacteria. Also provided herein are methods of treatment of celiac disease or a related disorder, treatment of gluten-containing foodstuff, degrading and/or detoxifying gluten comprising the subtilisins gluten-degrading enzyme and/or compositions.