172 



A. I. OPARIN 



amylase was determined in the drops with the indicated starch content. The 

 resvdts are given in Table i . 



Table i 



The effect of ^-amylase on starch in coacervate drops 



The figures in the table show that the concentration of reducing sugars, com- 

 puted for unit volume, was four times greater in the coacervates than in the 

 equihbrium fluid. Consequently, formation of the reaction products is concen- 

 trated in the coacervates due to the fact that they contain the enzyme. In this 

 case also we can regard the coacervates as systems in which the morphological 

 structure substantially influences the nature of the process. 



In order to test the alternative possibility that the increased concentration of 

 reaction products in the coacervate drops was due to absorbed sugar from the 

 surrounding solution, control experiments were made with the addition of 

 maltose to coacervate containing inactivated amylase; in this case all the added 

 maltose was recovered in the equilibrium fluid, and not in the coacervate sedi- 

 ment. Evidently, we are justified in regarding the presence of maltose in the 

 coacervate drops under the adopted experimental conditions as a result of the 

 action of /3-amylase in the coacervate drops on starch embodied in these drops. 



A good illustration of the incorporation of enzymes into coacervates are our 

 experiments on the coacervation of bacterial lysates. A solution (lysate) of 

 Micrococcus lysodeikticus cells with high catalase activity was obtained from 

 N. Gel'man. The experiments were carried out in the following way: 0-2 ml of 

 o-oi M phosphate buffer with a fixed pH, o-i ml of bacterial lysate diluted 

 I : 100, (the method of preparing the lysate is given in the following section) 

 followed by 0-25 ml of 0-67% aqueous solution of gum arable were added to 

 0-5 ml of 1-5% aqueous solution of protamine sulphate obtained from the 

 spawn of sevruga sturgeon by Kossel's method. The complete mixture with 

 pH 6-0 was maintained in a water bath for 3 minutes at temperature of + 41- 

 43°C. The formation of coacervate drops was controlled with the microscope in 

 all experiments. Then 0-2 ml of 0-64% H2O2 solution was added to the mixture. 

 Incubation with hydrogen peroxide lasted from 2 to 5 minutes. After this the 

 enzyme was inactivated by 0-4 ml of 10% (w/v) H2SO4. The activity of the 



