New ways to replace cumbersome, lengthy and expensive processes for the production of proteins such as lactoferrin/casein

The fractionation of milk proteins by means of isoelectric precipitation separates proteins based on their isoelectric point (IEP) - at a specific pH value at which they have no net charge and thus their solubility is at its lowest. By acidifying the milk to the IEP value of casein at 4.6, it precipitates and can be separated from other milk proteins, such as whey proteins, as these are water-soluble, enabling fractionation.
If protein-rich whey is present after casein precipitation, lactoferrin can be obtained by this process. The aim of this process is to significantly simplify the very complex process of obtaining lactoferrin/casein from skimmed milk/whey or other sources. Furthermore, the protein, such as lactoferrin/casein, is obtained as a precipitate in situ in high yield. The method is suitable for the production/isolation of protein from milk/whey without the use of chemicals and previous aids such as extraction and purification from skimmed milk or whey, whereby ion exchange chromatography and membrane filtration are used.
If you have ever brought casein from skimmed milk to the isoelectric point (IEP) by acidification, you know that the precipitated protein is contaminated. The solution would therefore be to reach the IEP without adding acid. This is exactly what our new process does - it is called electro-acidosis. In principle, it works for all proteins from a liquid matrix - from milk as an emulsion or whey or other solutions/sources.
Since proteins have different IEPs, which is due to different functional groups and ligands in a macromolecule, lactoferrin can also be obtained in an alkaline pH range. This is why lactoferrin does not have an exact IEP, but rather a range. For this reason, very low traces of other alkaline proteins may also be precipitated. This process is called electro-alkalysis in the basic pH-range. This method/ technology was filed by Bioway for patent recently.
Today, lactoferrin is extracted from milk using a multi-stage purification process - state of the art technology - which preserves heat-sensitive proteins, for example through cold separation, membrane filtration and ion exchange chromatography. The concentrated lactoferrin is then converted into powder form using gentle freeze-drying or spray-drying. Cow's milk contains about 60μg of iron per litre of milk. About 1g of lactoferrin can be extracted from 10 litres of milk.
The physical properties are as follows: physical state: powder, colour: pink, solubility: slightly soluble in water :1 mg/ml, odourless, pleasant taste, pH value: 5.2~7.2 at 20g/l in water. The molecular formula is given as C141H226N46O29S3; source: https://pubchem.ncbi.nlm.nih.gov. Lactoferrin has a molecular weight of approximately 80 kDa.
There is no simple structural formula for lactoferrin, as it is a large protein consisting of a chain of approximately 700 amino acids. Instead of a structural formula for the entire substance, complex representations of the 3D structure are used, such as those available in the RCSB Protein Data Bank: https://www.rcsb.org/structure/1lfg, which show the folding of the protein and its binding sites.
The steps involved in lactoferrin extraction are preparation of the raw material raw milk: Lactoferrin is usually extracted from skimmed milk, cheese whey or 'native' whey, which is obtained directly from skimmed milk. To prevent denaturation of the heat-sensitive lactoferrin, the raw milk is carefully treated, often using sterilising separators and microfiltration.
Because proteins are rather sensitive on temperature and other possible factors - to avoid denaturation, the whole process takes place under cooling conditions. To no time the protein comes in contact with foreign ions / substances or compounds - it stays in the origin matrix.
To explain the process of electrolytic extraction, we will use casein as an example. The electrolysis of water produces H+-ions. The skimmed, fat-free milk is protonated. The pH value drops from approximately 7 to 4.6. Casein. At a pH value of 4.6 at the isoelectric point, where the charge has been neutralised and solubility decreases, casein precipitates and can be separated from the liquid phase (in this case, skimmed milk). No acid or other substances are added - the milk remains in its original form and is drinkable. This process can be controlled very precisely and produces the end product, casein, in about 30 minutes. It is clear that this process must be more cost-effective than current methods - namely, less than 50% of the production costs.

Bioway Consulting SL
C./ Tirant Lo Blanc 4, office 19
E-03750 Pedreguer / Alicante - Spain
Phone: 0034065030786
Mail: contact@biowayconsulting.com
https://www.biowayconsulting.com
Mr. Norbert Pautz (Presscontact)

Bioway Consulting SL is an engineering company in the consulting business, active in research and development of new technologies in many fields often based on electrolysis technologies.
It was founded in 1989 in Germany as a sole proprietorship and later continued in Switzerland as Bioway GmbH. The main activity at that time was initially as a distributor for renowned companies from abroad (e.g. Charm Sciences / USA and Malthus Instruments Ltd / UK etc.). This was followed by own developments with production such as the IGDS (Intelligent Gravimetric Dilution System) and devices for water disinfection. Bioway did deep research working with emulsions like soluble oil and milk as well pharmaceutical formulations.
The focus on water / emulsion disinfection / water and waste water purification was intensified. In addition, a system for the inactivation of airborne germs (viruses/bacteria) was developed and manufactured (Corona Wave).
Today Bioway is active in the consulting business and co-operates with other European companies in the field of waste water purification and develops processes by testing customer waste water samples in its own laboratory.
New project is the extraction of protein with new technology.

This release was published on openPR.