The present invention relates to use of probiotic compositions and/or histamine degrading enzymes for the control of histamine in a farm production animal, companion animal, aquaculture, or a human, to reduce or eliminate the incidence of necrotizing enterocolitis and/or related inflammatory conditions in the gastrointestinal tract or skin, and behavioral conditions. The invention also relates to the probiotic compositions and/or histamine degrading enzymes.

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.

A mutant glycine oxidase is obtained by substituting at least one wild-type amino acid sequence derived from thermophilic bacteria belonging to the family Bacillus with another amino acid, and has the following enzyme properties. Molecular weight: 40,000±2,000 daltons by SDS-PAGE. Optimum temperature: 45° C. under the condition of pH 8.5 in presence of pyrophosphate. Optimum pH: pH 8.0 under the condition of 37° C. in presence of pyrophosphate. Thermal stability: Stable up to 70° C. under the condition of pH 8.5 while retaining for 1 hour in presence of pyrophosphate. pH Stability: Stable in the range of pH 5.5 to 10.0 under the condition of 4° C. while retaining for 24 hours in presence of pyrophosphate. Specific activity: 1.2 units/mg or more. Kinetic constant K.sub.m: 0.2 mM or less.

A novel method of producing high-purity hydroxy-L-pipecolic acids in an efficient and inexpensive manner while suppressing the production of hydroxy-L-proline is provided. The method includes allowing an L-pipecolic acid hydroxylase, a microorganism or cell having the ability to produce the enzyme, a processed product of the microorganism or cell, and/or a culture liquid comprising the enzyme and obtained by culturing the microorganism or cell, to act on L-pipecolic acid as a substrate in the presence of 2-oxoglutaric acid and ferrous ion, wherein the L-pipecolic acid hydroxylase has the properties: (1) the enzyme can act on L-pipecolic acid in the presence of 2-oxoglutaric acid and ferrous ion to add a hydroxy group to the carbon atom at positions 3, 4, and/or 5 of L-pipecolic acid; and (2) the enzyme has a catalytic efficiency (kcat/Km) with L-proline that is equal to or less than 7 times the catalytic efficiency (kcat/Km) with L-pipecolic acid.

A method and a mineral wool product include a multiple of lamellae, such as a sandwich panel core. The product includes a plurality of lamellae cut from a mineral wool web, and bonded together by applying an adhesive on the surfaces of two adjacent lamellae to form a web-like product, wherein the adhesive comprises at least one hydrocolloid.

MPO1 and MPO2 can be regulated for either decreasing or increasing alkaloid levels in plants, in particular in Nicotiana plants. In particular, suppressing or overexpressing one or more of MPO1 and MPO2 may be used to decrease or increase nicotine and nicotinic alkaloid levels in tobacco plants. Suppression or overexpression of one or more of MPO1 and MPO2 may be used in combination with modification of expression of other genes encoding enzymes on the nicotinic alkaloid biosynthetic pathway such as A622, NBB1, PMT, and QPT.

An embodiment of the present invention provides a tobacco plant having a low alkaloid content. In the tobacco plant, a function of a gene encoding aspartate oxidase AO2 is suppressed.

A system for the production of high value chemicals includes (a) an input selected from the group consisting of ethylene glycol, glycerol, ethanol methanol or a combination thereof. In addition, the system includes (b) an oxidation biocatalyst including an alcohol oxidase, a copper radical oxidase, a glycerol oxidase, an alditol oxidase or a combination thereof. Further, the system includes (c) an oxidized intermediate. The system also includes (d) a finishing catalyst including a supported metal catalyst, a carboligating catalyst, an amine oxidase, a glyoxalase, an acid catalyst, a base catalyst, an isomerization catalyst or a combination thereof. Still further, the system includes (e) an output.

The present invention refers to Amadoriase enzyme protein variants having de-glycating activity and improved thermostability compared to the wild type Amadoriase. The present invention refers also to the use of the thermostabilized Amadoriase as deglycating agent, preferably in the food industry. Moreover, the present invention refers to the use of the thermostabilized Amadoriase as diagnostic and/or therapeutic tools. Preferably, the Amadoriase enzyme protein variants of the invention can be used for determining the level of glycated haemoglobin in a biological sample and therefore for monitoring diabetes.

The present invention provides an alternative L-glutamate oxidase that allows for measurement of L-glutamate. More specifically, the present invention provides the following L-glutamate oxidase mutant (a) or (b) and the like: (a) an L-glutamate oxidase mutant including an amino acid sequence that has 90% or more identity to an amino acid sequence of SEQ ID NO: 3 and exhibits an activity of oxidizing L-glutamate, except an L-glutamate oxidase including an amino acid sequence of SEQ ID NO: 1; or (b) an L-glutamate oxidase mutant comprising a peptide linker consisting of 1 to 20 amino acid residues which is inserted into one or more sites selected from the group consisting of (1) a site in a region proximity to a boundary between α1 and α2 regions, (2) a site in a region proximity to a boundary between α2 and γ regions and (3) a site in a region proximity to a boundary between γ and β regions in the L-glutamate oxidase mutant (a), and having the activity of oxidizing L-glutamate.