Described are compositions and methods relating to the stabilization of oxidase enzymes using the amino acid glycine. The compositions and methods allow for drying oxidase-containing compositions with improved enzyme activity yield and long term storage of dried oxidase-containing compositions, in some cases without the need for refrigeration.

Described are compositions and methods relating to the stabilization of oxidase enzymes by heat (or thermal) drying under reduced partial pressure of diatomic oxygen. The compositions and methods allow for dehydration of oxidase-containing compositions with no loss of enzyme activity.

The invention relates to a recombinant Escherichia coli expressing a fusion protein of formamidase and phosphite dehydrogenase, a construction method and use thereof. The invention includes adopting engineered E. coli DH5α as a host, amplifying a cloned formamidase gene and a cloned phosphite dehydrogenase gene into a fusion gene, ligating the fusion gene to a multiple cloning site of a vector, transforming the obtained recombinant plasmid into the E. coli DH5α, extracting the plasmid and transforming into an expression strain, and performing induction culture to obtain a recombinant E. coli. The recombinant E. coli can express a fusion protein of formamidase and phosphite dehydrogenase.

The disclosed subject matter provides for genetically modified cells, e.g., fungal cells, that autonomously generates and/or secretes one or more therapeutic molecules, e.g., therapeutic peptides, therapeutic proteins or small therapeutic molecules, in situ. In certain embodiments, the present disclosure provides genetically-engineered fungal cells that generate and secrete tetracycline and analogues thereof.

An object of the present invention is to provide an evaluation system capable of detecting an extracellular purinergic receptor ligand minimally invasively, chronologically and systemically, and the present invention provides a genetically modified non-human animal expressing a first fusion protein and a second fusion protein for detecting an extracellular purinergic receptor ligand, in which the first fusion protein comprises a membrane protein that binds to a purinergic receptor ligand, and a first reporter protein, and the second fusion protein comprises a protein that binds to the membrane protein bound to the ligand, and a second reporter protein; and a cell thereof.

A DNA fragment to encode a nitrogen fixation enzyme includes a base sequence of SEQ ID NO:1 or a base sequence having not less than 50% identity with the SEQ ID NO:1.

The present disclosure relates to a microorganism expressing active D-proline reductase.

An artificial non-coding RNA (ncRNA) module constructed by a synthetic biology technique and the use of the artificial ncRNA module in the construction of an artificial nitrogen fixation system are disclosed. The RNA module can enhance the post-transcriptional stability of nifHDK mRNA by interacting with a nitrogenase coding gene nifHDK mRNA, thereby improving the nitrogen fixation ability of a chassis microorganism. A fusion expression vector carrying the artificial RNA module is constructed and transformed into different chassis nitrogen-fixing microorganisms. It is confirmed through experiments that, under nitrogen fixation conditions, the artificial RNA module of the present disclosure can significantly improve the nitrogenase activity of a recombinant engineering bacterial strain.

A nucleic acid carrier according to an embodiment of the present disclosure includes CpG-ODN-RNA conjugate and a porous silica particle carrying the conjugate inside pores thereof. In this regard, the nucleic acid carrier of the present invention can stably deliver loaded nucleic acid molecules to a body and release the same to a target, thereby increasing Type 1 interferon and exhibiting RNA-inherent functions.

The invention relates to a method for identifying compounds useful for the treatment of cancer based on assessing the ability of the compound to modulate the interaction between the AIF protein and the CHCHD4 protein.