Superficially porous particles are disclosed, each including a solid core and a layered porous shell. The layered porous shell includes a porous inner layer and at least one porous outer layer, a shell skeleton thickness greater than 1 nm, and constitutes from 10 vol % to 90 vol % of the plurality of superficially porous particles. The porous inner layer includes an inner layer thickness of less than 300 nm. The at least one porous outer layer includes a cumulative outer layer thickness ranging from 1 to 100 times the inner layer thickness, a predominately radial pore orientation, and an outer layer pore structure which is more organized than the inner layer pore structure. A layer-by-layer process for forming a plurality of superficially porous particles with layered structure is disclosed. A post-modification process for preparing a plurality of chromatographically enhanced superficially porous properties is also disclosed.

Superficially porous particles are disclosed, each including a solid core and a layered porous shell. The layered porous shell includes a porous inner layer and at least one porous outer layer, a shell skeleton thickness greater than 1 nm, and constitutes from 10 vol % to 90 vol % of the plurality of superficially porous particles. The porous inner layer includes an inner layer thickness of less than 300 nm. The at least one porous outer layer includes a cumulative outer layer thickness ranging from 1 to 100 times the inner layer thickness, a predominately radial pore orientation, and an outer layer pore structure which is more organized than the inner layer pore structure. A layer-by-layer process for forming a plurality of superficially porous particles with layered structure is disclosed. A post-modification process for preparing a plurality of chromatographically enhanced superficially porous properties is also disclosed.

The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R.sub.1-L.sub.1-N(R.sub.3)-L.sub.2-R, immobilized on a support, wherein R.sub.1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L.sub.1 is either a methylene group or a covalent bond; R.sub.2 is a five-or six-membered, substituted or non-substituted ring structure; L.sub.2 is either a methylene group or a covalent bond; R.sub.3 is a methyl group; and wherein if R.sub.1 is a hydroxyethyl group and L.sub.1 is a covalent bond, R.sub.2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R.sub.1-L.sub.1-N(R.sub.3)-L.sub.2-R, immobilized on a support, wherein R.sub.1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L.sub.1 is either a methylene group or a covalent bond; R.sub.2 is a five-or six-membered, substituted or non-substituted ring structure; L.sub.2 is either a methylene group or a covalent bond; R.sub.3 is a methyl group; and wherein if R.sub.1 is a hydroxyethyl group and L.sub.1 is a covalent bond, R.sub.2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

A first Fab region-binding peptide includes an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5 with substitution of one or more amino acid residues at the 17.sup.th position and the 36.sup.th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second Fab region-binding peptide further includes deletion, substitution and/or addition of one or more amino acid residues at positions other than the 17.sup.th position and the 36.sup.th position. A third Fab region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first Fab region-binding peptide.

A first Fab region-binding peptide includes an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5 with substitution of one or more amino acid residues at the 17.sup.th position and the 36.sup.th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second Fab region-binding peptide further includes deletion, substitution and/or addition of one or more amino acid residues at positions other than the 17.sup.th position and the 36.sup.th position. A third Fab region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first Fab region-binding peptide.

Porous hybrid inorganic/organic materials comprising ordered domains are disclosed wherein the ordered domains are ordered radially, and having the formula (A).sub.x(B).sub.y(C).sub.z (Formula I) or the formula [A].sub.y[B].sub.x (Formula III), wherein A, B, C, x, y and z in Formula I and A, B, x and y in Formula III are further defined herein, and wherein diffraction peak maxima observed for the material exhibit a 2 position that excludes diffraction peaks resulting from atomic-range order that are associated with amorphous material. Methods of making the materials and use of the materials for chromatographic applications are also disclosed.

To provide an affinity support in which a binding property of a ligand to a target substance is improved. The affinity support contains a solid phase support and a protein ligand, wherein the protein ligand is represented by formula (1): RR.sup.1 (1) wherein R represents a linker binding to the solid phase support, which contains a polyproline, and R.sup.1 represents a protein showing an affinity to immunoglobulin, and the R is bound to a C terminal or an N terminal of an amino acid sequence in R.sup.1.

To provide an affinity support in which a binding property of a ligand to a target substance is improved. The affinity support contains a solid phase support and a protein ligand, wherein the protein ligand is represented by formula (1): RR.sup.1 (1) wherein R represents a linker binding to the solid phase support, which contains a polyproline, and R.sup.1 represents a protein showing an affinity to immunoglobulin, and the R is bound to a C terminal or an N terminal of an amino acid sequence in R.sup.1.

The invention relates to a novel biomimetic affinity purification material and its application in the purification of chitosanase, which belongs to the field of industrial biotechnology. The affinity ligand for the biomimetic affinity material is chitodisaccharides, the connecting arm is cyanuric chloride, and the base medium is epoxy-activated Sepharose 6B. The desorption constant (K.sub.d) and the theoretical maximum adsorption capacity (Q.sub.max) of the biomimetic affinity material are 24.2 g/mL and 24.1 mg/g, respectively. Using the above biomimetic affinity material, a chitosanase biomimetic affinity purification method is established, which can produce high-purity chitosanase with high efficiency and low cost, and has good industrial application potential.