PROTEOLYTIC ENZYMES II7 



The most detailed studies of the proteolytic enzymes in 

 bacterial culture filtrates are those of Maschmann [29], who 

 isolated from the culture filtrates of the invasive Clostridia 

 {CI. histolyticum, CI. welchii, CI. septicum) an enzyme that 

 attacked gelatin and collagen but had no action on casein, 

 peptone or egg albumin. Even filtrates from young cultures 



600-t 



h^SOO- 



5400- 



300- 



^lOO- 



'l8hr.) 



K 



(18 hr.) 



O 



(20 min) 



X 



-24-0 



-160 >. 



«n 

 O 



■120 o> 

 > 

 Ui 



> 

 hQO P 



/ 



cor 



(Ihr.) 



-40 



I 1 \ 



^ 0-5 I'D , 1-5 20 



ENZYME CONC. (ml. soln.) 



FIG. 8.1. — Hydrolysis of gelatin by extracellular proteinase of 

 Micrococcus lysodeikticus as a function of enzyme concentra- 

 tion. Activity measured by appearance of amino nitrogen 

 (solid line) and by changes in viscosity (broken line). Reaction 

 times shown in parentheses. (From Gorini, L. and Fromageot, 

 C. (1950), Biochim. Biophys. Acta, 5, 524; Elsevier Publishing 

 Co. Inc., New York and Amsterdam) 



contained this specific gelatinase, and it was therefore re- 

 garded as being a truly extracellular enzyme. The invasive 

 properties of certain Clostridia can be ascribed to their ability 

 to secrete this enzyme since Maschmann could not detect 

 any specific gelatinase in filtrates from the non-invasive 

 Clostridia {CI. botidinum, CI. tetani), and later workers 

 showed that the culture filtrates of the invasive Clostridia 

 digested the collagen supporting material of muscle whereas 

 an enzyme such as trypsin liquefied the muscle fibrils and 



