312 
Studies on Enzyme Acton. XI.—Hydrolysis of Raffinose by Acids 
and Enzymes. 
By H. E. Armstrona, F.R.S., and W. H. Giover, Ph.D. 
(Received and read April 2, 1908.) 
[International Catalogue of Scientific Literature. 
Authors’ title slip :—D. Q. 
Subject slips :— 
D 1820 Cane-sugar. Hydrolysis by acids and enzymes. 
D 1830 Raffinose. Hydrolysis by acids and enzymes. 
D 8014 Invertase, action of, on raffinose and sucrose compared. 
D 7095 Cane-sugar and raffinose, hydrolysis of, by acids and enzymes compared. 
@ 1240 Invertase, action of, on raffinose and sucrose compared. | 
In a previous communication of this series (vol. 74, p. 191),* it is pointed 
out that the variouss glucosides are hydrolysed by acids at very different 
rates, the relative values being approximately of the order shown in the 
following table :— 
a-Methylelucoside .................. 100 
B- ee We See ace a a ater 180 
a-Methylgalactoside ............... 540 
B- POLY Ps cnc re 880 
Salicin (a @-glucoside) ............ 600 
Milk-sugar (a 8-galactoside)...... 720 
Maltose (an e-glucoside ) ......... 740 
Cane-sugar, it is to be remembered, is hydrolysed at a rate vastly more 
rapid—at least 1000 times as rapidly as maltose, in fact. These differences, 
taking into account the peculiar specific behaviour of enzymes as hydrolytic 
agents, raise questions of interest from the chemical side and they are of no 
slight significance perhaps also from a biological point of view. 
The two stereo-isomeric methylglucosides are represented by the following 
formule :— 
ise Ouss ee OLE 
| I | | 
FON oe! a seer u 
on.o.da CZ Hepc_é_bon OEE Sh 
oe OP te OE gH.C—C—C.OH. 
\ OHH iN OH 
~4 - Be We 
Nia a 
Qa 
a-Methylelucoside B-Methylglucoside 
* All references are to these ‘ Proceedings.’ 
