53 results about "ADP Glucose" patented technology

A flavin-binding glucose dehydrogenase (FAD-GDH), which in addition to having high substrate specificity and adequate desirable heat stability, is suitable for efficient production, preferably using E. coli, yeast or molds and the like as host cells. The FAD-GDH has amino acid substitutions at positions equivalent to one or more locations selected from the group consisting of position 213, position 368 and position 526 in the amino acid sequence described in SEQ ID NO: 8. The FAD-GDH is acquired from a culture by inserting a gene encoding the FAD-GDH into host cells such as E. coli. A preferable example of the FAD-GDH is FAD-GDH, in which a signal peptide region present in an N-terminal region has been deleted from the amino acid sequence of Mucor-derived FAD-GDH, and which has the aforementioned amino acid substitutions. The FAD-GDH can be preferably used in clinical diagnosis.

The invention provides a flavin-binding glucose dehydrogenase exhibiting reduced fluctuation of activity depending on temperature environment, and a method for measuring glucose concentration using the flavin-binding glucose dehydrogenase. The flavin-binding glucose dehydrogenase has the following properties (1) to (3): (1) activity: which exhibits glucose dehydrogenase activity in the presence of an electron acceptor; (2) substrate specificity: which exhibits an activity of 10% or less against maltose, D-galactose, D-fructose, sorbitol, lactose and sucrose when the activity against D-glucose is defined as 100%; and (3) temperature characteristics: which exhibits lower fluctuation of activity in a wide temperature range of 10 to 50° C.

The present invention relates to novel mutant polynucleotide molecules encoding enzymes with enhanced thermostability. When expressed in plants, these polynucleotides lead to increased yield in plants grown under conditions of heat stress. In one embodiment, the polynucleotide molecule of the present invention encodes maize endosperm ADP glucose pyrophosphorylase (AGP) and soluble starch synthase (SSS) enzyme activities. Also contemplated by the present invention are plants and plant tissues grown to contain or transformed with such mutant polynucleotides and expressing a polypeptide encoded by such polynucleotides. The invention also relates to methods for isolating polynucleotides and polypeptides within the scope of the invention. The present invention also provides methods of increasing yield in plants grown under conditions of heat stress.

The invention discloses trehalose synthase with an increased maltose conversion rate, a method for preparing the trehalose synthase and application thereof, and belongs to the field of gene engineering and enzyme engineering. The method includes mutating glutamic acid at 289 sites near trehalose synthase active centers of Thermobifida fusca YX into glycine to obtain mutants E289G; mutating histidine at 295 sites into asparagine mutants H295N; mutating methionine at 344 sites into lysine mutants M344K; mutating methionine at 367 sites into leucine mutants M367L and carrying out combined mutation on the basis of the H295N to obtain mutants H295N / E289G, H295N / M344K, H295N / M367L and H295N / M344K / M367L. The trehalose synthase, the method and the application have the advantages that by the aid of the mutants, the conversion efficiency of trehalose prepared from the trehalose synthase still can be prevented from being severely affected even if substrates contain certain glucose, and accordingly the trehalose synthase, the method and the application have high industrial values.

Cells to be used in producing antibody compositions, for example, an antibody having a high antibody-dependent cellular cytotoxic activity which is useful in various diseases, an antibody fragment or a fused protein having the Fc domain of the antibody; a process for producing an antibody composition by using these cells; antibody compositions; and uses thereof. In the above-described antibody compositions, the ratio of sugar chains, which are free from fucose bonded to N-acetylglucosamine at the sugar chain reducing end, to the total N-glycoside linkage complex sugar chains bonded to the Fc domain amounts to 20% or more. Moreover, novel GDP-mannose 4,6-dehydrogenase, GDP-keto-6-deoxymannose 3,5-epimerase 4-reductase, GDP-beta-L-fucose pyrophosphorylase, alpha-1,6-fucosyltransferase and DNAs encoding the same are provided.

The invention provides for sequencing a nucleic acid molecule based on the detection of base incorporation by the release of pyrophosphate (PPi) using a new enzyme system comprising adenosine diphosphate (ADP)-glucose pyrophosphorylase (AGPase) and its substrate ADP-glucose.

The invention relates to the field of detecting instruments, in particular to a micrometer-scale glucose sensor microelectrode. The micrometer-scale glucose sensor microelectrode comprises a substrate, a working electrode and a counter electrode, the front portion of the substrate is a working area, the working electrode and the counter electrode are located in the working area, the maximum diameter of the cross section of the working area is less than or equal to 1 millimeter, PADs in one-to-one correspondence to the electrodes are arranged at the tail of the substrate, and each of the working electrode and the counter electrode is connected with the corresponding PAD through a lead. The electrodes are reasonably distributed on the planar or columnar insulating substrate and width of each electrode or cross-sectional diameter of each columnar electrode is limited to effectively reduce size of the electrode, so that rejection reaction of receptors is reduced.

The purpose of the present invention is to provide an FAD-conjugated glucose dehydrogenase that is hard to be inhibited by the inhibitors such as 1,10-phenanthroline.The present invention relates to a modified glucose dehydrogenase (GLD), comprising an amino acid sequence of a wild-type FAD-conjugated glucose dehydrogenase (GLD) represented by SEQ ID NO: 1 having a substitution of at least one amino acid residue selected from the group consisting of amino acid residues at positions 298, 338, 340, 341, 343, 352, 354, 424, 426, 431 and 432, wherein the modified GLD has a reduced susceptibility to an inhibitor, as compared with the wild-type GLD, especially to said modified GLD, which has 40% or more of a relative activity when determined in a system wherein the inhibitor coexists at a final concentration of 1 mM based on an enzymatic activity when determined in a system wherein the inhibitor does not coexist.