Daicel Corporation

Kyoto Institute of Technology

Kagoshima University

National University Corporation Kyoto Institute of Technology

Hiromichi Okura

Toru Shibata

Seiichi Uchimura

Yoichi Kumada

Yuki Hirabayashi

Yuji Ito

Provided are porous cellulose particles containing chitosan and having predetermined pores on a surface and a predetermined particle diameter, and a method for producing the porous cellulose particles. Porous cellulose particles including unsubstituted cellulose and chitosan, wherein a content of the chitosan is not greater than 20 mass % in a total of 100 mass % of the unsubstituted cellulose and the chitosan, pores having a diameter from 0.05 to 5 μm are observed in an image of surfaces of the porous cellulose particles observed by a scanning electron microscope, and a proportion of porous cellulose particles having a particle diameter from 10 to 200 μm is not less than 90 mass %.

Porous cellulose particles and method for producing same

Provided is novel porous cellulose having functionality that is not imparted to porous cellulose composed of unsubstituted cellulose, and a method for producing the same. Porous cellulose containing: unsubstituted cellulose; and a glucose unit-containing polymer excluding unsubstituted cellulose, wherein a content of the polymer is not more than 20 mass % in 100 mass % of a total of the polymer and the unsubstituted cellulose.

Porous cellulose and method for producing same

Provided is a novel porous cellulose medium that can efficiently separate a large target molecule in a calibration standard. A porous cellulose medium including a porous cellulose particle having a particle size from 1 to 600 μm, wherein, in sieving the porous cellulose medium for classification and using a fraction corresponding to aperture openings between 53 μm and 106 μm as a support for size exclusion chromatography, a polyethylene oxide standard is run through size exclusion chromatography with pure water as a mobile phase, and a weight average molecular weight Mw and a gel partition coefficient Kof the polyethylene oxide standard satisfy Relationships (A) and (B) above:in a case where 4.80≤log≤5.50,>−0.445×log+2.55  (A)in a case where 5.75≤log,0≤<0.19  (B).

Porous cellulose medium

Provided is a separating agent that does not have a significantly reduced dynamic binding capacity (DBC) to a target substance even when the separating agent is continually CIP-treated under alkaline pH conditions. The separating agent includes a carrier and a protein, wherein the protein is a given protein, and a surface of the carrier and a lysine residue in the protein are bound by a chemical bond.

Separating agent

Provided is a novel method for producing cellulose beads, the method being capable of suitably producing spherical cellulose beads. The method for producing cellulose beads includes: (Step 1) preparing a coagulating bath having a first liquid medium phase and a second liquid medium phase; (Step 2) forming a particulate cellulose solution in the first liquid medium phase by supplying a cellulose solution to the first liquid medium phase of the coagulating bath; and (Step 3) coagulating the particulate cellulose solution by supplying the particulate cellulose solution in the first liquid medium phase to the second liquid medium phase.

Method for producing cellulose beads

Provided is a separating agent with an improved dynamic binding capacity (DBC) to a target substance. The separating agent includes a carrier and a protein, wherein the protein is a given protein, and a surface of the carrier and added lysine residues in the protein are bound by chemical bonds.

An object of the present invention is to provide a method by which a peptide having a specific binding capability that can be used for purification of a target molecule can be produced at a low cost, and specifically relates to a peptide fusion protein including one or more peptides having specific binding capability and a scaffold protein, the peptide being inserted into the amino acid sequence of the scaffold protein directly or via a peptide linker, and/or being linked to the N-terminal and/or C-terminal of the scaffold protein.

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Tokyo, Japan

Hiromichi Okura