Isolating .beta.-lactoglobulin and .alpha.-lactalbumin by eluting from a cation exchanger without sodium chloride
US5986063A · kind A · utility
Assignee
Inventor
Key dates
| Filing date | Jul 31, 1998 |
| Grant date | Nov 16, 1999 |
| Priority date | — |
| Expiry date | Jul 31, 2018 |
Classification
- Technology area (CPC A)Human Necessities
- CPC primaryA23V2002/00
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
A method is provided for isolating the proteins, .beta.-lactoglobulin and .alpha.-lactalbumin, from whey with a single cation exchanger, and using different pH values for eluting the proteins as separate fractions without using salt elution. A whey protein solution is adjusted to a pH of less than about 4.5. The solution is contacted with a cation exchanger to obtain a bound fraction containing .alpha.-lactalbumin and .beta.-lactoglobulin. The bound fraction is adjusted to a pH of about 4.0 to 6.0 and a .beta.-lactoglobulin fraction is eluted at this pH in the absence of sodium chloride. The pH of an remaining bound fraction is adjusted to about 6.5 or greater and an .alpha.-lactalbumin fraction is eluted. The method is advantageously conducted at elevated temperatures ranging from 35.degree. C. to 50.degree. C. The ion exchanger may be cross-linked polymeric beads made of cellulose, agarose or dextran, or a microporous polymeric membrane made of regenerated cellulose, polysulfone or cellulose acetate, and may contain charged immobilized molecules such as carboxymethyl or sulfopropyl moieties.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.