Provided herein, among other things, is an engineered non-plant cell that produces a tropane alkaloid product, a precursor of a tropane alkaloid product, or a derivative of a tropane alkaloid product by means of a complement of biosynthetic enzymes and a complement of transporter proteins. A method for producing a tropane alkaloid, a precursor of a tropane alkaloid product, or a derivative of a tropane alkaloid product that makes use of the cell is also described.

A system for determining a concentration of hemoglobin A1C includes a first electrochemical test strip, the first electrochemical test strip providing for an HbA1C concentration; and a second electrochemical test strip, the second electrochemical test strip providing for the total amount of hemoglobin.

This invention provides an amadoriase having improved specific activity on a glycated substrate, compared with conventional amadoriase. Provided is an amadoriase comprising a substitution of the amino acid at the position corresponding to position 64 of the amino acid sequence as shown in SEQ ID NO: 1 with an amino acid selected from the group consisting of glycine, serine, methionine, leucine, threonine, valine, and isoleucine, a method for measurement of HbA1c, and a reagent kit for measurement of HbA1c using such amadoriase. Such method and kit for measurement enable rapid, simple, and accurate quantification of HbA1c.

The invention relates to recombinant microorganisms and methods for producing steviol glycosides and steviol glycoside precursors.

The present invention provides a composition that enables measurement of glycated hemoglobin in the presence of a stronger surfactant than conventional surfactants. To this end, the present invention provides an amadoriase in which one or more amino acids have been substituted at positions corresponding to positions selected from the group consisting of positions 80, 71, 175, 172, 279, 12, 9, 77, 30, 28, 13, 3, 4, 286, 204, 338, 44, 340, and 194 of the amadoriase derived from the genus Coniochaeta having the amino acid sequence as shown in SEQ ID NO: 1 as well as a composition for measurement of glycated hemoglobin comprising an amadoriase that retains activity in the presence of an anionic surfactant. The present invention can provide an enzyme and a composition for measurement of glycated hemoglobin that sufficiently remain stable even when exposed to anionic surfactants.

The fructosyl amino acid oxidase (FPOX-CE) of other species, wild-type fructosyl amino acid oxidase (PnFPOX), and the recombinant proteins (PnFPOX-SS, PnFPOX-DS, and PnFPOX-TS) were respectively dissolved in a 100 mM potassium phosphate buffer (pH value of 8.0) to achieve a concentration of 0.05 mg/ml, and after a heat treatment at 25 C. to 60 C. for 10 minutes, the oxidase activities of the above-mentioned fructosyl amino acid oxidases and recombinant proteins were measured. At the same time, thermal stability (%) was calculated based on the following formula:

thermal stability=(value of oxidase activity after heat treatment)/(value of oxidase activity without heat treatment)100%.

Object An object of the present invention is to provide a highly stable FVHO preparation and a low-hygroscopicity dried FVHO preparation. Means for achieving the object A method for producing a FVHO preparation comprising a step of allowing at least one member selected from phosphoric acid, casein peptone, D-glucosamine hydrochloride, melibiose, sorbose, lactose, fructose, melezitose, glucono-1,5-lactone, and ribitol; and a method for producing a dried FVHO preparation, comprising a step of allowing Bicine to coexist.

Fructosyl amino acid oxidase is provided, which has an amino acid sequence as shown in SEQID. No. 1 or fructosyl amino acid oxidase having a homology of more than 80% with this amino acid sequence, on a corresponding site of an amino acid selected from following (a) to (f), having one or more amino acid residues conducting a substitution, obtained fructosyl amino acid oxidase having a higher thermostability: (a) 59-site glutamic acid, (b) 98-site glutamic acid, (c) 225-site glycine, (d) 277-site lysine, (e) 285-site glutamic acid, and (f) 355-site aspartic acid. The method for preparing the above oxidase and the test kit containing the enzyme for determining glycated albumin are also provided.

The present invention provides a protein comprising an amino acid sequence in which arginine at position 61 of a protein comprising the amino acid sequence represented by SEQ ID NO: 1 is substituted to an amino acid selected from the group consisting of glycine, alanine, valine, leucine, serine, threonine, proline, cysteine, methionine, asparagine, glutamine, and aspartic acid; and a method for measuring a glycated hemoglobin in a sample, wherein the method comprises reacting a glycated hemoglobin in a sample with a protease to produce a glycated hexapeptide, then reacting the produced glycated hexapeptide with the aforementioned protein, and measuring a substance produced or consumed by the reaction.

Recombinant microorganisms, plants, and plant cells are disclosed that have been engineered to express recombinant genes encoding UDP-glycosyltransferases (UGTs). Such microorganisms, plants, or plant cells can produce steviol glycosides, e.g., Rebaudioside A and/or Rebaudioside D, which can be used as natural sweeteners in food products and dietary supplements.