Abstract:
From a culture of E. coli the bacterial mass is flocculated by addition of an organic base or a salt thereof having an amino function and a molecular weight above 1,000. The flocculated cells are centrifuged, resuspended in water and precipitated by a water-miscible solvent, such as acetone. The cells which are simultaneously opened by the previous step are centrifuged away and again resuspended in water, whereby the enzyme is extracted from the cells. By addition of the organic base, mentioned above, to the suspension, the extracted cells, nucleic acids and ballast proteins are precipitated and are removed by centrifugation. The L-asparaginase is precipitated from the cell-free solution by addition of acetone.
Abstract:
L-asparaginase is obtained in concentrated purified form by fractional precipitation of an aqueous solution thereof with low molecular weight solvents, specifically diols of 4 to 8 carbon atoms, such as 2-methyl-pentane-diol-(2,4) and including such diols wherein one hydroxyl group is alkylated, for example 3methoxybutanol.
Abstract:
The disclosure relates to a novel process for the microbiological production of the enzyme invertase by culturing yeast strains of the variety Saccharmyces carlsbergensis Hansen under aerobic conditions in an aqueous nutrient medium.
Abstract:
Crude L-asparaginase is freed of pyrogens by contacting solutions of the same containing weak buffers with diethylaminoethyl dextran gels. The process can be carried out according to batch techniques or in a continuous manner by using a chromatographic column.
Abstract:
Polypeptide materials such as enzymes are rendered waterinsoluble by bonding to a cross-linked copolymer produced by copolymerizing of (A) about 0.1 to 30 wt. % of at least one Alpha , Beta -monoolefinically unsaturated dicarboxylic acid anhydride having about 4 to 9 carbon atoms; (B) about 35 to 90 wt % of at least one di-and/or poly(meth)acrylate of a dial and/or polyol; and (C) about 5 to 60 wt % of at least one hydrophilic monomer.
Abstract:
L-asparaginase is obtained in a highly purified, pyrogen free and stabilized form from a crude aqueous solution thereof, by adding to said solution an amino acid, such as glycine, adjusting the pH of the solution to from 7.0 to 9.2, preferably in the presence of a lower aliphatic alcohol, such as methanol, then heating the solution for a period of from 1 to 5 days at a temperature up to 65* C., preferably between 40* C. to 61* C., thereby denaturizing the inactive accompanying proteins without affecting the L-asparaginase. The precipitated, denatured proteins are then removed, as by centrifuge, the enzyme enriched solution then adjusted to a pH between 4.5 and 5.5 and fractionally precipitated with a 50 percent polyethylene glycol solution, the precipitate then washed with acetone and dried.
Abstract:
Alpha -Amylase is separated from a liquid which contains Alpha -amylase and foreign protein impurities according to a process which comprises adsorbing the Alpha -amylase from the liquid onto a carrier-bound Alpha -amylase inhibitor to form an enzyme inhibitor complex and separating the complex from the liquid. Purified Alpha -amylase substantially free from foreign protein impurities may be obtained by washing the complex and desorbing the Alpha -amylase from the carrier-bound inhibitor.
Abstract:
Peptide materials such as enzymes and enzyme inhibitors are rendered water-insoluble by binding the peptide materials to a cross-linked copolymer formed by copolymerizing the following units: (A) about 0.1 to 50 weight percent of at least one Alpha , Beta -monoolefinically unsaturated dicarboxylic acid anhydride having about 4 to 9 carbon atoms and (B) about 99.9 to 50 weight percent of at least one di- and/or poly(meth) acrylate of a diol and/or a polyol.