C H A P 1^ i: l{ II 



Production of Enzymes 



Act iiiomycetes produce a varict.y of extra- enzymes as the actinomycetin complex pos- 

 cellular and endocellular enzymes. Some of sess only the ability to dissolve isolated l)ac- 

 these enzymes hav(> beiMi isolated from the terial cell walls; they are wrongly classified, 

 culture filtrates or {ho mycelium, concen- therefore, with lysozymc. The ability of puri- 

 trated, and purified. Others have only been fied enzymes isolated from the actinomycetin 

 demonstrated in the mycelium of the organ- complex to form amino acids sets them a.side 



from lysozyme, which forms reducing groups. 

 The assertion of Kriss that actinomycetes 

 produce "lysozyme" still requires confirma- 

 tion of the ability of these organisms to form 

 enzjmies that liberate reducing groups and 

 an amino sugar complex of the type relea.sed 



ism. 



L 



vsozvnie 



The production of lysozj^me systems by 

 actinomycetes at first aroused consideralile 

 attention. These systems were confused, 

 h()we\er, with autolytic and bacteriolytic by lysozyme as well as the peptidase type, 

 mechanisms, on the one hand, and with anti- in accordance with the requirements laid 

 biotics, on the other. down by Salt on. 



In his classical studies of the lytic agents 



of B. sKhtilis, Xicolle first suggested that 

 bacteriolytic substances produced b}" micro- 

 organisms might ha\'e properties in common 

 with enzyme systems. According to Welsch 

 (1947), the bacteriolytic system of certain 

 actinomycetes is lysozyme-like in nature and 

 is able to digest bacterial cell wall substrates. 

 However, according to (Ihu^'sen and Saltoii serum. This is true of both saprophytic and 

 and (Ihuysen, such enzyme systems, unlike pathogenic types. They vary greatly, in this 

 lysozyme, are able to liberate amino acids respect, both (jualitatively and (luantita- 



Proteases 



Miinter, Waksman, and Lieske first estab- 

 lished that various actinomycetes, mostly 

 members of the genus Streptomijccs, possess 

 strong proteolytic activities. Some cultures 

 were able to decompose very energetically 

 proteins in gelatin, egg-white, and blood 



but not reducing substances. 



Salton defined the enzymic properties of 

 lysozyme on the basis of the following de- 

 terminations: (a) turbidity reduction of iso- 

 lated cell wall structures or lysis where the 

 wall is in situ as with intact bacterial cells; 



tively, as can be simply demonstrated by the 

 process of gelatin li(iuefaction or casein de- 

 composition in ordinary plates. As a rule, 

 s{)ecies of Nocardia are poorly proteolj^tic, 

 whereas certain species of Streptomyces are 

 highly acti\'e in this respect. The degree and 



(b) liberation of reducing groups; (cj libera- rapidity of proteol^'sis also varj^ with indi- 

 tion of an ac(>tylamino sugar complex of vidual species. 



glucosamine and the acidic hexosamine. Such Slapp found that out of 477 freshly iso- 



1S3 



