Abstract: We describe a method for purifying chymosin comprising providing an aqueous liquid sample containing chymosin and a separation medium comprising a base matrix and a plurality of firmly attached ligands that are capable of binding to chymosin, contacting the matrix with the sample under conditions permitting binding of chymosin to the matrix, and desorbing chymosin from the matrix. The characterizing feature is that the matrix is hydrophilic and that the ligands in the plurality of ligands are hydrocarbon groups in which all carbon atoms are sp3-hybridised, possibly with an ether oxygen or a thioether sulphur inserted between two carbon atoms at one or more positions in at least one of the hydrocarbon groups, and possibly a hydroxy group replacing a hydrogen atom at one or more positions in at least one of the hydrocarbon groups.

Abstract: The invention relates to a method for the inactivation of amylase in a solution comprising Rhizomucor miehei aspartic protease by keeping the solution at a pH between 2.1 and 2.8 and at a temperature between 20° C. and 40° C. for a period of time sufficient to inactivate amylase for at least 95%. With this method the level of residual Rhizomucor miehei aspartic protease activity in the solution at the end of the heating time is at least 90%, preferably at least 95%, and the residual amylase activity is 0.05 RAU/g or lower, more preferably 0.001 RAU/g or lower, i.e. more than 99% of the amylase activity has been inactivated.

Abstract: The present invention provides a liquid composition comprising: (i) an aspartic protease; and (ii) an inorganic salt and/or a polyalcohol; in which composition; the sum concentration of sorbate, benzoate and alkyl esters of para-hydroxybenzoate is less than 0.010 mol/l; the standard plate count <100 in 1 ml; yeast count <10 in 1 ml; and mould count <10 in 1 ml. The composition can be used as a coagulant in the production of cheese.

Abstract: The invention relates to a method for the inactivation of amylase in a solution comprising Rhizomucor miehei aspartic protease by keeping the solution at a pH between 2.1 and 2.8 and at a temperature between 20° C. and 40° C. for a period of time sufficient to inactivate amylase for at least 95%. With this method the level of residual Rhizomucor miehei aspartic protease activity in the solution at the end of the heating time is at least 90%, preferably at least 95%, and the residual amylase activity is 0.05 RAU/g or lower, more preferably 0.001 RAU/g or lower, i.e. more than 99% of the amylase activity has been inactivated.

Abstract: A method for purifying chymosin comprising the steps of: providing an aqueous liquid sample containing chymosin and a separation medium comprising a base matrix and a plurality of firmly attached ligands that are capable of binding to chymosin; contacting the matrix with the sample under conditions permitting binding of chymosin to the matrix; and desorbing chymosin from the matrix. The characterizing feature is that the matrix is hydrophilic and that the ligands in the plurality of ligands are hydrocarbon groups in which all carbon atoms are sp3-hybridised, possibly with an ether oxygen or a thioether sulphur inserted between two carbon atoms at one or more positions in at least one of the hydrocarbon groups, and possibly a hydroxy group replacing a hydrogen atom at one or more positions in at least one of the hydrocarbon groups.