The present invention relates to a mutated immunoglobulin-binding protein having increased alkaline tolerance and, more specifically, to an immunoglobulin-binding protein in which, with respect to the A-domain of Staphylococcal protein A, or a functional variant thereof, an amino acid at a specific site is mutated and thereby exhibits an increased chemical stability at an alkaline pH value in comparison to a parental molecule. The present invention can provide an antibody-purifying immunoglobulin-binding protein ligand and matrix which have enhanced alkaline tolerance and accordingly enhanced stability in multiple times of alkaline cleaning.

The present invention relates to recombinant proteins/peptides from plant and animal materials, compositions comprising the proteins/peptides and methods for making them.

This invention is intended to produce a novel functional material through solubilization and molecular weight reduction of a water-insoluble polymeric compound, such as a water-insoluble protein or water-insoluble polysaccharide, in a simple and efficient manner. This invention provides a method for producing a degradation product of a water-insoluble polymeric compound comprising the steps of: bringing a water-insoluble polymeric compound into contact with a solid acid catalyst, heating the resulting mixture, and recovering a supernatant; adding an aqueous medium to the solid acid catalyst after the supernatant is recovered, agitating and heating the resulting mixture, and recovering a supernatant; washing the solid acid catalyst with an aqueous medium and recovering a wash solution; mixing the recovered supernatant with the wash solution, so as to obtain a fraction that has not adsorbed to the solid acid catalyst; and eluting an adsorbed fraction from the solid acid catalyst and recovering an eluate, so as to obtain a fraction that has adsorbed to the solid acid catalyst.

The present invention relates to a preparation method which is performed by expressing the recombinant carrier proteins in Escherichia coli and purification thereof. More particular, the invention relates to industrially scalable process for the recovery of recombinant carrier proteins.

The present disclosure relates to the design and generation of stapled helical peptides that perturb protein-protein interactions (PPIs). The methods disclosed herein for preparing stapled peptides involve providing a peptide having a first amino acid that is functionalized with a salicylaldehyde ester side group and a second amino acid functionalized with a 1,2-hydroxyl amine side group; reacting the first and second amino acids to generate an N,O-benzylidene acetal moiety; and performing acidolysis of the resultant N,O-benzylidene acetal moiety to generate the stapled peptide. In many forms, the stapled helical peptides described herein are not hydrophobic.

This project presents a method for extracting collagen from broiler chicken feet. The process involves several steps, including raw material processing, washing, grinding, hydrolysis, centrifugation, extraction with an acetic acid solution and filtering. During hydrolysis, a 2.0-2.5% acetic acid solution is used at temperatures of 18-25 C. for 6-10 hours. Raw material extraction is performed using a 1.5-1.8% acetic acid solution at temperatures of 50-55 C. for 45-50 minutes with continuous stirring. This method aims to obtain high-yield collagen extracts from broiler chicken feet while streamlining the production process.

The subject matter of the present invention is peptide C.sup.-amides which are precursors of peptide C.sup.-thioesters, characterized in that they comprise the radical of general formula (I) in which X, R.sub.1, R.sub.2, R.sub.3, R.sub.4, R.sub.5, R.sub.6, R.sub.7, R.sub.8, R.sub.9, n and A are as defined in Claim 1. The subject matter of the present invention is also the use of these peptide C.sup.-amides for obtaining peptide C.sup.-thioesters. The subject matter of the present invention is also the use of these peptide C.sup.-amides for obtaining peptides or proteins, in particular of therapeutic interest, by direct use as a crypto-thioester partner in NCL reactions. ##STR00001##

The present disclosure relates to the design and generation of stapled helical peptides that perturb protein-protein interactions (PPIs). The methods disclosed herein for preparing stapled peptides involve providing a peptide having a first amino acid that is functionalized with a salicylaldehyde ester side group and a second amino acid functionalized with a 1,2-hydroxyl amine side group; reacting the first and second amino acids to generate an N,O-benzylidene acetal moiety; and performing acidolysis of the resultant N,O-benzylidene acetal moiety to generate the stapled peptide. In many forms, the stapled helical peptides described herein are not hydrophobic.

Disclosed herein are methods of producing peptides, including liquid phase peptide synthesis methods in which one or more cycles of peptide elongation are performed in one pot. In particular, the present disclosure provides liquid phase peptide synthesis methods employing solvent systems comprising 2-methyltetrahydrofuran for condensation reactions, as well as convergent liquid phase peptide assembly methods in which benzyl alcohol anchor groups are selectively removed from an N-protected C-protected peptide by base-catalyzed ester hydrolysis.

A method for preparing nondenatured collagen type II for alleviating joint pain includes pulverizing a cartilage raw material and defatting to obtain a total protein crude extract; adding anhydrous ethanol to the total protein crude extract, soaking, stirring, and centrifuging to obtain an anhydrous ethanol insoluble material; dissolving the anhydrous ethanol insoluble material in water, adjusting pH to acidic, stirring and centrifuging to obtain an acid-insoluble material; dissolving the acid-insoluble material in water, performing enzymatic hydrolysis and centrifuging to obtain an enzymatic hydrolysis precipitate; dissolving the enzymatic hydrolysis precipitate in water, followed by performing co-fermentation, and centrifuging to obtain a fermentation precipitate; and adding a water activity regulator to the fermentation precipitate, and then drying to obtain the nondenatured collagen type II. The content of protein, hydroxyproline and nondenatured collagen type II in the prepared nondenatured collagen type II is high, and the shelf life is prolonged.