Ion Exchange Chromatography for Plant Protein Isolation

Protein recovery from plant by-products like rapeseed press cake using a two-step isoelectric solubilization process synergistically combined with flocculation. The method involves treating the plant material at low pH to solubilize the proteins, then flocculating and separating the protein fraction. This is followed by optionally hydrolyzing polysaccharides and repeating the solubilization at higher pH. The resulting protein product has high protein yield, low fiber, fat, and phytochemical content compared to conventional methods.

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Method for isolating and purifying protein variants from complex mixtures using continuous chromatography. The method involves contacting the mixture with two or more chromatography columns in a continuous operation mode to enrich and isolate specific protein variants. The columns are loaded with the mixture and the variants are separated while impurities are discarded. This is repeated multiple times to further purify the variants. The method reduces time compared to traditional chromatography like HPLC/FPLC by enabling higher yields in shorter periods.

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A method to produce plant-based meat substitutes with a texture and flavor similar to real meat. The method involves dividing a hydrated plant mass into two parts. One part is isolated using amino acids like cysteine to create a chicken-flavored extract. The other part is purified to remove carbohydrates. The chicken-flavored extract is then cooked with the purified part using hot air to make a spongy fibrous gel. Alternatively, the chicken extract is dehydrated and mixed with the purified part to make a fibrous cake. The method uses chromatography without solvents to isolate amino acids from plants for flavor extraction. This allows producing plant-based meat substitutes with realistic meat-like textures and flavors.

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Ion exchange chromatography purification of recombinant proteins through a novel peptide tag that enhances protein-protein interactions with ion exchange resins. The peptide tag, specifically designed for ion exchange chromatography, enables direct binding to the resin surface while maintaining the protein's native charge properties. This approach enables efficient purification of recombinant proteins through conventional ion exchange chromatography without the need for additional steps like affinity chromatography or solubilization.

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A method for protein purification that minimizes protein loss and maintains high purity through a single-step purification process. The method employs a multimodal ion exchanger with a hydrophobic and charged moiety, enabling selective binding of target proteins under high conductivity conditions. The ion exchanger selectively interacts with the target protein, facilitating its separation from aggregates and host cell components. The purification process involves a single chromatography step, eliminating the intermediate steps of conventional purification methods.

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A flow-through purification method for proteins using tandem ion exchange chromatography (AEX-CEX) that eliminates both high molecular weight (HMW) and low molecular weight (LMW) contaminants through simultaneous operation of both ion exchange and CEX chromatography in a single column. The method achieves high throughput purification by maintaining constant pH and conductivity conditions during the chromatography process, eliminating the need for in-line adjustments. The tandem approach eliminates both HMW and LMW contaminants simultaneously, enabling efficient purification of proteins with diverse isoelectric points.

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A novel method for extracting plant proteins from raw materials that addresses the conventional problems of prolonged fermentation times, high water consumption, and environmental concerns. The process involves adjusting the pH of the raw material slurry to facilitate the precipitation of starch, followed by a controlled fermentation process that selectively separates protein, starch, and fiber components. The method eliminates the need for mechanical breakdown, sieving, and multiple precipitation steps, resulting in a more efficient and environmentally friendly extraction process.

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Process for obtaining pure rapeseed protein napin and cruciferin from rapeseed meal through a multi-step purification method. The process involves digestion of rapeseed meal, recovery of desired protein fractions, adjusting the supernatant pH, and separating the mixture through ion exchange chromatography. The resulting purified protein fractions are then further purified through cation exchange chromatography to obtain pure napin and cruciferin.

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A method for extracting legume protein from raw materials using a two-step process that minimizes the use of calcium chloride. The method involves first extracting legume protein using water at a lower protein concentration (typically 0.05M CaCl2), followed by re-extraction with a lower calcium chloride concentration (typically 0.10-0.15M CaCl2) to recover the remaining protein. This approach eliminates the need for high calcium chloride concentrations typically associated with traditional extraction methods, reducing the amount of calcium chloride used while maintaining effective protein recovery.

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Single-step fractionation of highly sialylated variants of a protein using a strong ion exchange chromatography system. The method involves loading the protein mixture onto the chromatography support, and then applying a pH gradient elution at a constant salt concentration to selectively enrich the highly sialylated variants. The gradient is established by mixing a neutral and acidic pH buffer at a predetermined rate, maintaining a linear gradient between near-neutral pH and acidic pH. This single-step approach eliminates the need for multiple steps, wash steps, or additional purification steps, achieving rapid and efficient enrichment of highly sialylated protein variants.

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