A hybrid vegetable protein is described, comprising a guest protein having the structure of prolamine and glutelin, and a host protein having the structure of globulin and albumin, obtained from vegetable grains, such as corn and soybean, respectively. Likewise, a method for obtaining said hybrid vegetable protein is described, which comprises the steps of extracting the guest and host proteins, carrying out an acidification thereof, and further applying a magnetic field to provoke their attachment, and finally adding an alkali to the attached proteins to obtain a hybrid vegetable protein at its isoelectric point. The protein thus produced has a value higher than 0.97 according to the PDCAAS rating.

An object of the present invention is to suppress the variation of the elution position of a compound having a charged portion by a preservation liquid, in the purification of the compound, without carrying out the substitution step of the preservation liquid attached to the adsorbent used for the purification and the keeping step. A method for purifying a compound having a charged portion, the method comprising the steps of: preparing a composition containing a compound having a charged portion; preparing a buffer solution comprising a buffering agent and an alcohol, the buffer containing a calcium phosphate compound at least partially, having a buffer capacity in a range of pH 6.0 to pH 8.0, and being soluble in a polar solvent and insoluble in a non-polar solvent; preserving an adsorbent in the buffer solution; adsorbing the compound on the adsorbent by bringing the composition into contact with the adsorbent preserved in the buffer solution; and separating the compound from the adsorbent by gradient elution.

Disclosed is a method of producing high-concentration collagen for use as a medical material, including: washing tissue of a mammal; subjecting the washed tissue to crushing and immersion in ethyl alcohol; subjecting the tissue to enzymatic treatment with stirring in purified water containing phosphoric acid and pepsin; adding sodium chloride to the collagen subjected to enzymatic treatment, performing stirring, and aggregating collagen; dissolving the aggregated collagen in purified water to give a collagen solution, which is then filtered using a filter and concentrated by removing the pepsin, low-molecular-weight material, and sodium chloride from the collagen solution using a tangential flow filtration device; subjecting the concentrated collagen to sterile filtration, aggregating the collagen using a pH solution in a neutralization tank, and concentrating the collagen by removing a non-aggregated solution; and concentrating the concentrated collagen using a centrifuge and stirring the concentrated collagen using a mixer.

The disclosure relates to systems and methods for improving the manufacturing of silk solutions and powders containing silk fibroin obtained from silkworm cocoons. The solutions and powders can be used to improve the post-harvest preservation of perishables and to improve the performance of packaging, including biodegradable packaging.

Methods for production of multiple biofuels through thermal fractionation of biomass feedstocks are described. The products of said methods are also described.

Disclosed is a chromatographic method for separating and purifying a recombinant human fibronectin from a genetically engineered rice seed that expresses the human fibronectin. In the method, the genetically engineered rice seed is milled, mixed with an extraction buffer, and then filtered to obtain a crude extract comprising the recombinant human fibronectin; the crude extract comprising the recombinant human fibronectin is subjected to cation exchange chromatography, so as to perform primary separation and purification, thereby obtaining a primary product comprising the recombinant human fibronectin; and the primary product is subjected to anion exchange chromatography so as to perform final separation and purification to obtain the recombinant human fibronectin as a target substance. The method is low cost and easily utilized on an industrial scale. The obtained OsrhFn target substance has a SEC-HPLC purity greater than 95% with excellent bioactivity.

Disclosed are a conotoxin polypeptide κ-CPTx-bt101, a method for preparation thereof, and an application thereof. The conotoxin polypeptide of the present invention consists of 18 amino acids, has a molecular weight of 1872.72 daltons, and has the full sequence KCCTMSVCQPPPVCTCCA (SEQ. ID NO. 1).

A series of multi-dimensional acoustic standing waves is set up inside a growth volume of a bioreactor. The acoustic standing waves are used to hold a cell culture in place as a nutrient fluid stream flows through the cell culture. The nutrient fluid stream dislodges some cells from the cell culture, which can then be recovered for cell therapy applications. The cell culture continues to expand and reproduce, permitting continuous recovery of cells from the bioreactor.

Provided is an ionic compound, which can be formulated into an ionic solution for extracting hydrophobic proteins. The ionic solution is free of alcohol and thus advantageous for later examinations. Also provided is an anti-nonspecific protein adsorption zwitterionic compound, which can be coated on a substrate to form an anti-nonspecific protein adsorption element.

The present invention relates to a method of producing a recombinant protein in a host cell comprising adding Polyethyleneimine (PEI) during cell culture. Addition of PEI to the cell culture as a fermentation enhancer can result in reducing the viscosity of the cell culture, and/or increasing the extracellular concentration of the recombinant protein, and/or reducing the duration of cell culture to the point of harvest or protein recovery.