[Vor. 5 
276 ANNALS OF THE MISSOURI BOTANICAL GARDEN 
enzyme acts in a suspension. Oppenheimer (13) goes fur- 
ther and states that lipases are insoluble in water, glycerin, 
fats, or ethereal solvents; that the enzyme always acts in sus- 
pension. To insure lipolytic action it is therefore desirable 
either to bring the desiccated plant material containing the 
enzyme,—preferably after extraction of fats,—directly in 
contact with the substrate, as suggested by the work of Conn- 
stein, Hoyer and Wartenberg (’03) and by Wohlgemuth 
(713), or to follow the method cited by Haas and Hill (717) 
for extracting the enzyme for commercial usage. In the 
latter process the seeds or material of high oil content are 
ground with water, centrifuged, and the resulting emulsion 
of oil, protein, and enzyme allowed to ferment at a moderate 
temperature until a seum containing the enzyme rises to the 
surface. Hydrolysis is effected by allowing this scum to act 
upon fats in the presenee of water and manganese sulphate 
as a catalyser. In the present study it was not possible to 
follow either of the methods outlined above for lack of suf- 
ficient corms of the kind used in the experiment, and it was 
necessary to use in the series the enzyme dispersion in 
aqueous extract to observe a possible, rather than a probable, 
reaction. 
In the following table showing the relations of enzyme ex- 
tract to acetamid and asparagin the values presented are 
TABLE II. 
THE ACTION OF ENZYMES EXTRACTED FROM ETHERIZED AND DNETHEBEUNMD 
CORMS OF GLADIOLUS ON AMIDO AND AMINO COMPOUN 
Milligrams ammonia nitrogen 
from 
Series number Acetamid Asparagin 
n otal n 
sample substrate sample substrate 
Control........ .0474 2.370 .0396 1.980 
Жалт 1.7640 88.200 .0388 1.940 
ЖАРҒАҒЫ ықы ры ‚0476 2.380 ‚0387 1.935 
p Басра .1417 7.085 .0360 1.800 
Baud iiw .0377 1.885 .0248 240 
Og ep ae ‚0423 2.115 .0395 975 
b mp .0452 2.260 .0371 885 
|: д Sere .0376 1.880 .0313 565 
oy MEET .0406 2.030 .0249 245 
