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Solvay Protease

In the course of our development work it turned out that Optimase M 440 was no longer available [39]. Since it was known from another project that the liquid enzyme formulations exhibit a less pronounced emulsifying behavior (cf. [37]), the different commercial bulk preparations, now Alcalases and Solvay Proteases, were re-evaluated. All yielded very good results with respect to chemical purity and enantiomeric excess (>99% each). However, Solvay Protease L 660 (the successor of Optimase L 660) was clearly the most active enzyme, thus requiring the smallest amount of enzyme for the reaction. The clearly higher price of this enzyme [40] should be of no consequence because of the expected simpler work-up and, hence, lower manpower costs. [Pg.392]

After some orientating experiments employing the newly selected liquid enzyme preparation a simple extraction procedure comprising three extractions at pH 8.5 and two at pH 2 could be developed. On comparison of the solid enzyme preparation Optimase M 440 with Solvay Protease L 660, it turned out that the removal of... [Pg.393]

As Subtilisin Carlsberg was, and still is, one of the cheapest enzymes available on the market, no further proteases were tested. Four Subtilisin Carlsberg preparations from Solvay Enzymes [9] and Novo Nordisk [10] were tested successfully Solvay-Protease M 440 (solid form) and L 660 (liquid form) as well as the Novo enzymes Alcalase 2.0 T (solid) and Alcalase 2.5 L (liquid). [Pg.404]

Owing to experience previously gained concerning work-up with the solid enzyme formulations [22] only the liquid enzyme preparations of Novo and Solvay, Alkalase 2.5 L and Protease L 660, respectively, were used in the following studies. Both preparations exhibited nearly the same specific activity in the present reaction. An enzyme concentration of <5% (v/w) with respect to 9 (s/e> 20 [24]) was used in the subsequent experiments of this section. [Pg.405]


See other pages where Solvay Protease is mentioned: [Pg.398]    [Pg.398]    [Pg.398]    [Pg.398]    [Pg.402]    [Pg.10]    [Pg.10]   
See also in sourсe #XX -- [ Pg.392 ]




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