226 results about "Ethanol dehydrogenase" patented technology

The invention relates to an ADH (ethanol dehydrogenase) protein family mutant and an application thereof, and particularly provides a mutant of an ADH protein. Compared with wild type ADH proteins, the ADH protein mutant is capable of remarkably increasing expression purity, efficiency and yield of foreign proteins in a cell-free synthesis system in vitro, and / or reducing binding capacity of the mutant protein and the Ni medium.

The invention discloses an XZ-A26 bacterial strain for producing L-alanine with high yield, which has a preservation number of CGMCC (China General Microbiological Culture Collection Center) No.4036 and has the capacity of generating high-concentration L-alanine through fermentation. The XZ-A26 bacterial strain is constructed by the steps of: integrating an L-alanine dehydrogenase gene on thermophilic fatty bacillus chromosome on lactic dehydrogenase position on an escherichia coli ATCC8739 chromosome, then sequentially knocking out a pyruvate formate lyase gene, an alcohol dehydrogenase gene, an acetokinase gene, a fumaric acid reductase gene and an alanine racemase gene of the escherichia coli chromosome, and then carrying out continuous cell culture in a fermenting tank for obtaining agenetic engineering strain. The invention also relates to a construction method of the XZ-A26 bacterial strain and an application of the XZ-A26 bacterial strain in preparation of the L-alanine. According to the invention, the escherichia coli with the preservation number of CGMCC No.4036 for generating the high-concentration L-alanine through fermentation can be constructed by using a metabolic engineering method, and the yield of the L-alanine generated by using the XZ-A26 bacterial strain reaches up to 115g / L. The XZ-A26 bacterial strain is suitable for industrially producing the L-alanine.

The stabilization of biomaterials such as proteins in a nominally dry, hydrophilic glassy matrix is vastly improved by the addition of an appropriate amount of a small-molecule pasticizer such as a glycol or DMSO to the formulation, while maintaining a glass transition temperature (Tg) that is above the storage temperature. By plasticizing the glasses, their ability to preserve proteins is improved by as much as 100 times over the unplasticized glass at room temperature. The plasticizer confers the greatest beneficial effect when it is dynamically coupled into the bulk glass, and this coupling occurs over a fairly narrow range of plasticizer concentration. Methods are described in which a small-molecule plasticizer can be incorporated into a glass made of much larger molecules (e.g. a polymeric glass), with desired dynamic coupling, via a molecule that is believed to act as a dynamic linker. Protein preservation data was obtained from two enzymes, horseradish peroxidase (HRP) and alcohol dehydrogenase (ADH).

A fusion protein of pyrroloquinoline quinone glucose dehydrogenase (PQQGDH) and a cytochrome is disclosed. PQQGDH is, for example, a water-soluble PQQGDH derived from Acinetobacter calcoaceticus. The cytochrome is, for example, an electron transfer domain of quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. The fusion protein of the present invention shows intramolecular electron transfer from PQQ, a redox center, to the cytochrome, which allow construction of a direct electron transfer-type glucose sensor which requires no electron mediators.