Edward L. Rickes

The isolotion and biological properties of a β-glucanase from B. subtilis

Abstract A purified fraction has been isolated from a crude concentrate obtained from Bacillus subtilis fermentation which was highly active as a β-glucanase in vitro . In chicks on a Washington state barley basal diet, it also produced a significant growth response when fed at a level of 0.000001% of the diet. A comparison of chick growth and β-glucanase activities over a wide range of potencies shows a correlation which indicates that both the in vitro and in vivo activities are due to a single entity. The fraction prepared by extraction, dialysis, ammonium sulfate precipitation and DEAE-cellulose chromatography showed essentially a single peak when examined by free-boundary electrophoresis at pH 6.5. Although the physical-chemical data are insufficient for us to state that the enzyme has been obtained in homogeneous form, the purest sample represents a 2600-fold purification of the β-glucanase activity from the starting concentrate.