3 



TABLE 1. Activity of purified invertase in aqueous alcohol. 



[Temperature 30 C. Concentrations: Aqueous alcohol containing cane sugar 0.2 normal, and acetic 

 acid 0.02 normal; 100 cc of this mixture were added to 10 cc of purified invertase solution.) 



The inactivation of invertase by alcohol was noticed by O'Sullivan 

 and Tompson, a and they state that the inactivation by alcohol is 

 1 'in direct proportion with the amount present. Five per cent alcohol 

 decreases the speed of the reaction by about one-half." The results 

 here given are somewhat different in detail from those quoted, 

 because we have measured the inactivation for higher strengths of 

 alcohol than were used by the previous investigators. It will be 

 noticed that our results also show almost a linear relation between 

 activity and alcohol strength for weak alcoholic solutions. 



THE DESTRUCTION OF INVERT ASE BY ALCOHOL. 



The measurements of the destruction of invertase by alcohol were 

 made by the method previously used in studying the destruction of 

 the enzym by acids and alkalis. 6 The rate of the destruction follows 

 the course of unimolecular reactions, as is shown by the following 

 experiment. The value of the velocity-coefficient of the unimolecu- 

 lar formula, & 2 , remains constant within the errors of experiment dur- 

 ing the course of the destruction. 



TABLE 2. Unimolecular order of the destruction of invertase by alcohol. 

 [Temperature 30 C. Alcohol 20 per cent by volume. Maximum activities were measured.) 



a J. Chem. Soc., 1890, 57:927. 



6 U. S. Dept. Agr., Bureau of Chemistry Cir. 65. 



[Cir. 58] 



