Food & Supplements : Processing

Food & Supplements Portfolios


Concentrating Dairy Proteins

UW–Madison researchers have developed negatively charged ultrafiltration membranes for improved concentration of milk casein, whey and serum dairy proteins.

The membranes are fabricated from commercial membranes having pore sizes traditionally thought to be too large. The surface of the membrane is modified to permanently attach a negative charge that repels proteins. Taken together, the increased pore size allows higher permeability of liquid through the membrane while the negative charge helps prevent protein loss. The negative surface also is antifouling, making cleaning easier and more sustainable.

Production of Milk Protein Concentrate with Energy and Environmental Savings and Reduced Equipment Needs

UW–Madison researchers have developed a novel approach for removing lactose from skim milk and other dried milk-derived products that reduces energy use and environmental impact. First, milk is concentrated under conditions that encourage the growth of large lactose crystals. The mixture is spray dried to form a powder, which contains small aggregates of proteins mixed with small molecules and large lactose crystals. The mixture then is sorted by particle size in a high speed air classifier, which uses an air stream and centrifugal forces to separate particles by shape, size and density. This method will produce a product with the same chemical and physical characteristics as moderately fortified milk protein concentrate, as well as a co-product with increased lactose content.

Improved Methods for Producing Low-Cost Protein-Polysaccharide Conjugates for Use in Foods and Beverages

UW–Madison researchers have developed novel methods of producing protein-polysaccharide complexes using a wet heat treatment.  The process involves heating aqueous solutions containing protein in the presence of a polysaccharide with a reducing sugar.  High concentrations of a stabilizing polysaccharide, such as dextran, are used to prevent unwanted protein denaturation. The resulting PPCs exhibit improved thermal stability, more desirable color and excellent emulsifying properties.  They are superior to both unmodified protein and gum Arabic.

Simple, Rapid and Inexpensive Process for Making Glue from Slaughterhouse Animal Blood

UW-Madison researchers have developed a novel and simple process for making glue from whole animal blood. The process starts by adding an anticoagulant and a preservative to fresh, whole blood. Then lime and sodium hydroxide are added, and the pH of the mixture is adjusted until it is between about 9 and 11. To yield the final adhesive, a curing agent and ammonia are added to the mixture. The resulting glue bonds well to surfaces, including paper, cardboard and wood.

Improved Low-Fat and Fat-Free Cheese

UW-Madison researchers have developed a method for producing low-fat and fat-free processed cheese with improved texture, color and baking properties. One key to this method is to acidify, with calcium chelating acids, the fat-free or skim milk source used in the cheese manufacturing process to a pH of about 5.4 to 5.8 to obtain the cheese base curd. This improves melt and reduces curd stickiness. It also eliminates the need to add phosphate- or citrate-based salts during cheese making because the calcium content is sufficiently lowered in this cheese base. The other key is to add glycerides, including monoglycerides and diglycerides, to the cheese base during the manufacturing process. The glycerides are emulsifiers with low water solubility. They change the way the milk proteins interact, leading to improvements in the textural and functional properties of the cheese.

Purification of Beta Casein from Milk

UW-Madison researchers have developed a novel, low-cost separation protocol for removing functional beta-casein from milk without adding unwanted by-products. This process allows a significant amount of highly soluble beta-casein to be extracted from milk, while also improving the cheese-making properties of the milk. Beta-casein is separated from other milk serum components using non-ceramic, cross-flow polymeric microfiltration membranes to form a permeate enriched in beta-casein. Milk may be cooled prior to microfiltration to enhance the separation. Beta-casein is then easily purified from this enriched permeate through demineralization. Cheese formed using the milk partially depleted of beta-casein has enhanced meltability and reduced bitterness, while the purified beta-casein exhibits improved yield, purity and solubility; excellent foaming and emulsification properties; and is suitable for use as a food product additive.

Methods and Compositions Involving Whey Protein Isolates

UW-Madison researchers have developed a superior method for isolating whey proteins in their native form through ion exchange chromatography. The technique prevents whey proteins from denaturing during isolation, so that they remain soluble over a wide pH range.

The method uses the normal ion exchange process in which the whey proteins are bound to a cation exchange support and unbound impurities are washed off the column. Next, the proteins are eluted with a modified buffer solution that maintains the correct pH and optimal ionic strength.

Method for Heat-Stabilizing Proteins to Protect Their Specific Binding Activities

UW-Madison researchers have developed a method for stabilizing proteins that protects the proteins’ specific binding activities from the effects of heat. A protein is mixed with a saccharide compound in a liquid suspension, and the suspension is dried. In the dried suspension, the saccharide compound openly associates with the protein molecules to protect the protein’s specific binding activity from the destructive effects of heat. The protein can be readily released from its association with the saccharide when the protein reaches a target site, allowing it to achieve its biological activity.

Fractionation of Whey Proteins by Complex Formation

UW-Madison researchers have developed an efficient and cost-effective method of separating whey proteins from solutions of whey protein concentrate by complexing them with polysaccharides. The process yields at least a 95 percent pure alpha-lactalbumin fraction and a 90 percent pure beta-lactoglobulin fraction.

Method for Increasing Yield During Cheese Making

A UW-Madison researcher has developed a method for recovering fine particles of curd and reincorporating them into a batch of cheese. A vibrating sieve is used to collect the fine particles from the whey and the wash water during the whey removal process. The particles are mixed into a subsequent lot of milk and reincorporated into the matrix of the resulting cheese curd.

Production of Substantially Pure Kappa Casein Macropeptide

A UW-Madison researcher has developed a whey-adsorbing process that produces a substantially pure cow milk protein, kappa-casein macropeptide (CMP), for nutraceutical purposes. CMP is produced as an effluent. Then, by depleting the product of the aromatic amino acids tyrosine, phenylalanine, and tryptophan through hydrolysis, CMP is freed from its characteristic bitter taste.

Continuous Crystallization System with Controlled Nucleation for Milk Fat Fractionation

UW–Madison researchers have developed a method of overcoming these limitations by more precisely controlling the triglyceride fractionation process. Specifically, the method allows separation of the nucleation and crystal growth steps. This makes it possible to use separate, specialized components that provide a continuous process for the fractionation of triglycerides.

Production of K-Casein Macropeptide for Nutraceutical Uses

A UW-Madison researcher has developed a whey-absorbing process that produces a pure cow milk protein, kappa-casein macropeptide (CMP), for nutraceutical purposes.  This process uses two opposite polarity ion exchangers in a series. The adsorbed product is hydrolyzed and reacted with water, depleting it of the aromatic amino acids tyrosine, phenylalanine and tryptophan, which usually cause its bitter taste.