An enzymatic deacidification method for partial glyceride lipase and PUFA-rich oil, comprising the following steps: 1) mixing a polyunsaturated fatty acid (PUFA)-rich oil with a non-polar organic solvent and a short-chain monohydric alcohol, adding an immobilized partial glyceride lipase to carry out an esterification reaction, wherein the partial glyceride lipase is a mutant obtained by mutating the Phe at the 278th position of Lipase SMG1 as Asn; 2) recovering the immobilized enzyme, and recovering the organic solvent and the monohydric alcohol so as to obtain a deacidified PUFA-rich oil. The partial glyceride lipase does not catalyze alcoholysis of triglyceride and like side reactions, has high deacidification efficiency, low reaction temperature, prevents high temperature oxidation of PUFAs, and the immobilized enzyme may be recovered and reused repeatedly, and thus the present invention has good application prospects in industry.

To provide a ketose 3-epimerase that can be used in the food industry and is highly safe, highly active, and heat resistant, a microorganism that produces this enzyme, and a method of producing a ketose. The present invention provides a ketose 3-epimerase that can be obtained from a microorganism belonging to the genus Arthrobacter, has a molecular mass of about 36 kDa as measured by SDS-PAGE, and has the following substrate specificities (A) and (B): (A) having an activity of epimerizing position 3 of a D- or L-ketose and preparing a D- or L-ketose corresponding thereto, and (B) having the highest epimerization activity on position 3 of D-allulose, among D- or L-ketohexoses.

To provide a ketose 3-epimerase that can be used in the food industry and is highly safe, highly active, and heat resistant, a microorganism that produces this enzyme, and a method of producing a ketose. The present invention provides a ketose 3-epimerase that can be obtained from a microorganism belonging to the genus Arthrobacter, has a molecular mass of about 36 kDa as measured by SDS-PAGE, and has the following substrate specificities (A) and (B): (A) having an activity of epimerizing position 3 of a D- or L-ketose and preparing a D- or L-ketose corresponding thereto, and (B) having the highest epimerization activity on position 3 of D-allulose, among D- or L-ketohexoses.

The present invention relates to a test element for the detection of an analyte comprising an enzyme, wherein the enzyme is incorporated in a nanocapsule.

A biological filler includes an embedding agent and an embedded complex. The embedded complex includes a scallop shell powder, 1,5-dihydroxyanthraquinone, and Thiobacillus denitrificans. The embedding agent includes a poly(vinyl alcohol)-sodium alginate blend membrane and a crosslinked composite membrane. The embedded complex is embedded by the embedded agent.

The invention provides a transaminase mutant and application thereof, wherein the amino acid sequence of the transaminase mutant is formed after mutation of the amino acid sequence as shown in SEQ ID NO: 1, and mutated amino acid sites comprise T7C+S47C sites. The transaminase mutant having the mutation sites can be further prepared into an immobilized enzyme through an immobilization technology, the immobilized enzyme has relatively high activity and high stability, can be recycled for multiple times, and is applicable to continuous flow reaction in a packed bed.

A foaming body for supporting microbes according to the present invention is superb in terms of microbial adherence to and affinity for pore areas therein, exhibits greatly improved supporting environments for microbes, and has a large surface area, thereby securing sufficient water treatment efficiency after loading microbes thereto.

A method for immobilizing in a sol-gel combined composite active or activable biological materials. The loss by leaching of the biological materials from the obtained combined composite is reduced while retaining the inherent biological activity. In addition, the composite obtained the method.

The present invention relates to an enzyme-catalyzed process for producing UDP-galactose from low-cost substrates uridine monophosphate and D-galactose in a single reaction mixture. The process can be operated (semi)continuously or in batch mode. The process can be extended to uridine as starting material instead of uridine monophosphate. Further, the process can be adapted to produce galactosylated molecules and biomolecules including saccharides, proteins, peptides, glycoproteins or glycopeptides, particularly human milk oligosaccharides (HMO) and (monoclonal) antibodies.

The present invention relates to an enzyme-catalyzed process for producing UDP-galactose from low-cost substrates uridine monophosphate and D-galactose in a single reaction mixture. The process can be operated (semi)continuously or in batch mode. The process can be extended to uridine as starting material instead of uridine monophosphate. Further, the process can be adapted to produce galactosylated molecules and biomolecules including saccharides, proteins, peptides, glycoproteins or glycopeptides, particularly human milk oligosaccharides (HMO) and (monoclonal) antibodies.