The present invention provides a new type of galacto-oligosaccharide, having a mannose residue instead of a glucose residue at the reducing end. The invention also relates to compositions comprising this galacto-oligosaccharide, its preparation and use in nutritional compositions.

The usefulness of β-galactosidases derived from Bacillus circulans is further enhanced. A modified β-galactosidase in which one or more amino acids selected from the group consisting of proline 182 (P182), tyrosine 187 (Y187), serine 188 (S188), tryptophan 405 (W405), alanine 406 (A406), glutamine 407 (Q407), tyrosine 449 (Y449), threonine 483 (T483), serine 512 (S512), serine 531 (S531), threonine 533 (T533), serine 534 (S534), asparagine 550 (N550), glutamine 551 (Q551), tryptophan 593 (W593), tyrosine 598 (Y598), proline 602 (P602), proline 604 (P604), tyrosine 609 (Y609), lysine 612 (K612), and tyrosine 615 (Y615), or an amino acid(s) corresponding thereto, has/have been substituted by other amino acid in a β-galactosidase consisting of the amino acid sequence of any of SEQ ID NOs. 1 to 4 or an amino acid sequence having 90% or more identity to the amino acid sequence set forth in any of SEQ ID NOs. 1 to 4.

Disclosed is a method for improving the productivity of 2′-fucosyllactose (2′-FL) through enzymatic treatment. Lactose used as a substrate in the stationary phase during culture is degraded by treatment with a small amount of enzyme, the resulting glucose is consumed to produce guanosine diphosphate-L-fucose as a precursor of 2′-fucosyllactose, and the use of lactose left after culture can be maximally utilized for the production of 2′-fucosyllactose. As a result, it is possible to increase the productivity of 2′-fucosyllactose in an economically efficient manner because additional glucose is not required while minimizing by-products.

The present invention relates to the use of one or more glycosidases in the process for the production and/or purification of a produced desired oligosaccharide. The process is preferably a microbial fermentation process using a host microorganism, which may also comprise nucleic acids expressing sugar catabolic pathway proteins suitable for the degradation of saccharides otherwise hindering the purification of the desired oligosaccharide.

The present invention relates to the use of one or more glycosidases in the process for the production and/or purification of a produced desired oligosaccharide. The process is preferably a microbial fermentation process using a host microorganism, which may also comprise nucleic acids expressing sugar catabolic pathway proteins suitable for the degradation of saccharides otherwise hindering the purification of the desired oligosaccharide.

There is provided a method of analyzing a biological sample component that allows easy and accurate quantification and counting of any of a plasma component and a blood cell component in a trace and unknown amount of a whole blood sample collected from a finger, for example. The method of the present invention is a method of analyzing a biological sample component in a trace amount of blood, comprising analyzing a diluent buffer into which the blood has been mixed and an internal standard substance and/or an external standard substance contained in the diluent buffer, calculating a dilution ratio, and analyzing a biological component in a plasma or serum component in the blood.

There is provided a method of analyzing a biological sample component that allows easy and accurate quantification and counting of any of a plasma component and a blood cell component in a trace and unknown amount of a whole blood sample collected from a finger, for example. The method of the present invention is a method of analyzing a biological sample component in a trace amount of blood, comprising analyzing a diluent buffer into which the blood has been mixed and an internal standard substance and/or an external standard substance contained in the diluent buffer, calculating a dilution ratio, and analyzing a biological component in a plasma or serum component in the blood.

Disclosed are compositions and formulations comprising enzymes or other biocatalyst that cleave surface-accessible DNA polymers and/or glycoprotein carbohydrate chains at galactose residues in dental calculus, and optionally further include one or more proteolytic enzymes, thereby destroying the structural integrity of the calculus, and allowing it to be readily removed without requiring special treatment by a trained dental professional. Also disclosed are methods for removing dental calculus using the disclosed compositions and formulations.

Provided is a high-accuracy analysis method utilizing an enzyme-lined immunoassay. The presence of an analyte 3 can be detected or the abundance of the analyte 3 can be analyzed by: bonding an antibody 5 that is capable of specifically bonding to the analyte 3 immobilized on a solid phase 1 and has an enzyme 7 bonded thereto; then decomposing an enzyme substrate 8, which can generate decomposition products capable of being detected easily with a mass spectrometry, with the enzyme 7 bonded to the antibody 5; and then analyzing the decomposition products 9 and 10 with a mass spectrometry.

Aspects of the disclosure relate to compositions of enzyme-binding polypeptides (EBPs) that modify the substrate specificity of an enzyme and a method for identifying an EBP that modifies substrate specificity of an enzyme binding at least one substrate, the method comprising: contacting the enzyme with a polypeptide library comprising a plurality of EBPs that bind different epitopes of the enzyme; identifying EBPs that bind to the enzyme to form an EBP-enzyme complex; assaying for the activity level and substrate specificity of the EBP-enzyme complex; and identifying EBPs that modify the substrate specificity of the enzyme by identifying EBPs that, when in an EBP-enzyme complex, have a different substrate specificity than un-complexed EBP; wherein the catalytic rate constant of the EBP-enzyme complex is ≥50% of the un-complexed enzyme for at least one substrate and/or wherein the EBP-enzyme complex retains binding to a substrate.