The present invention relates to a process for preparing a yeast hydrolysate comprising less than 100 ppm gluten and at least 1 ppm gluten based on salt-free yeast dry matter.

Administering an effective dose of glutenase to a Celiac or dermatitis herpetiformis patient reduces levels of toxic gluten oligopeptides, thereby attenuating or eliminating the damaging effects of gluten.

The present invention relates to a polypeptide having proline-specific endoprotease activity, selected from the group consisting of i. a polypeptide comprising a mature polypeptide sequence of SEQ ID NO: 2; ii. a polypeptide that has least 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to the mature polypeptide sequence of SEQ ID NO: 2; iii. a polypeptide encoded by a nucleic acid that hybridizes under medium stringency, preferably under high stringency conditions to the complementary strand of the mature polypeptide coding sequence of SEQ ID NO:1; iv. a polypeptide encoded by a nucleic acid that has at least 70%, 75% 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the mature polypeptide coding sequence of SEQ ID NO: 1.
The invention further relates to a method of producing the polypeptide and a process for the preparation of a food or feed product wherein the polypeptide is used.

The present invention relates to compositions and methods comprising genes and peptides associated with cyclic peptides and cyclic peptide production in mushrooms. In particular, the present invention relates to using genes and proteins from Galerina species encoding peptides specifically relating to amatoxins in addition to proteins involved with processing cyclic peptide toxins. In a preferred embodiment, the present invention also relates to methods for making small peptides and small cyclic peptides including peptides similar to amanitin. Further, the present inventions relate to providing kits for making small peptides.

A method for modifying a gliadin and an application thereof are provided. The method includes the following steps: dissolving the gliadin in a solvent to obtain gliadin solution; and adding a proline endoprotease to the gliadin solution for a reaction, and adjusting the pH value of solution to neutral according to a gradient, to obtain a modified gliadin. The modified gliadin obtained by the present invention may be uniformly dispersed in water, and may still maintain a uniform dispersion state in the water after high-temperature thermal sterilization and long-term storage, or even in the presence of sodium chloride, it has good thermal stability, salt resistance, and storage stability.

The present invention relates to a composition comprising hydrogels from functionalized hyaluronic acid derivatives, said hydrogels loaded with exogenous enzymes selected in the group consisting of prolyl endopeptidase (PEP) and endoprotease (EP) intended for the oral treatment of celiac disease. Specifically, this invention concerns a one-pot methodology useful to prepare methacrylic derivatives of hyaluronic acid, through the formation of a specific active group on hydroxyl groups of hyaluronic acid, the subsequent substitution of the inserted active group with ethylenediamine and finally, the reaction with methacrylic anhydride. The obtained methacrylic hyaluronic acid derivatives are used to prepare hydrogels through irradiation and loaded with exogenous enzymes selected in the group consisting of prolyl endopeptidase (PEP) and endoprotease (EP). The ability of prepared hydrogels to allow the enzyme release, as active form in simulated gastrointestinal fluids is proved.

A method for modifying a gliadin and an application thereof are provided. The method includes the following steps: dissolving the gliadin in a solvent to obtain gliadin solution; and adding a proline endoprotease to the gliadin solution for a reaction, and adjusting the pH value of solution to neutral according to a gradient, to obtain a modified gliadin. The modified gliadin obtained by the present invention may be uniformly dispersed in water, and may still maintain a uniform dispersion state in the water after high-temperature thermal sterilization and long-term storage, or even in the presence of sodium chloride, it has good thermal stability, salt resistance, and storage stability.

Provide are full human anti-FAP antibodies and variants thereof with further optimized CDR sequences. The new antibodies exhibited high affinity to the FAP protein and can be used to treat cancers and inflammatory conditions.

Disclosed herein are designed ankyrin repeat domain specifically binding to fibroblast activation protein (FAP). Such designed ankyrin repeat domains can be used in recombinant adapter molecules that are displayed on adenoviruses. Adenoviruses armed with such adapters efficiently transduce human fibroblasts and significantly broaden treatment opportunities through paracrine delivery of cargo to the tumor microenvironment (TME).

The present invention is directed to a method for manufacturing an enzyme preparation, comprising at least one recombinant Actinoallomurus endopeptidase with glutenase activity, at high yields and suitable for human use. The invention is further directed to a recombinant expression vector for expressing the recombinant endopeptidase(s) of interest, and to a S. lividans host cell comprising said vector. Moreover, the present invention is directed the enzyme preparation obtained by said method, to formulations of the same and to clinical uses thereof.