C. Grosswindhager et al., Endo-beta-1,4-D-mannanase is efficiently produced by Sclerotium (Athelia) rolfsii under derepressed conditions, J BIOTECH, 67(2-3), 1999, pp. 189-203
A number of wild-type isolates of Sclerotium (Athelia) rolfsii and S. coffe
icola were studied for their ability to produce endo-beta-1,4-mannanase, en
do-beta-1,4-xylanase, and endo-beta-1,4-glucanase activity when grown on ce
llulose- or glucose-based media. Whereas the presence of the inducer cellul
ose was strictly necessary for increased xylanase and endoglucanase product
ion by both S. rolfsii (208 and 599 U ml(-1), respectively) and S. coffeico
la (102 and 330 U ml(-1), respectively), elevated activities of mannanase (
up to 96.6 U ml(-1)) were formed even when employing glucose as the only ca
rbohydrate substrate. Significant production of mannanases as well as of au
xiliary mannan-degrading enzymes (beta-mannosidase, beta-glucosidase, alpha
-galactosidase, acetyl esterase) was only observed, however, under derepres
sed conditions, i.e. after glucose had been consumed from the medium. By ap
plying a fed-batch strategy, in which a glucose solution was continuously f
ed to a cultivation of S. rolfsii CBS 191.62 so that the glucose concentrat
ion in the medium never exceeded a certain low, critical value, production
of mannanase could be almost doubled as compared to a batch cultivation on
glucose (462 versus 240 U ml(-1)). Mannanase preparations produced by sever
al S. rolfsii and S. coffeicola strains under inductive and noninductive co
nditions (i.e. using cellulose or glucose as the substrates, respectively)
were further analyzed with respect to the patterns of isoformic mannanases
formed under these different growth conditions. Multiple mannanases were se
creted by all isolates investigated. Certain mannanase isoenzymes were only
formed by S. rolfsii in the presence of the inducer cellulose, indicating
a complex and separated regulation of the synthesis of mannanase isoenzymes
in this strain. (C) 1999 Elsevier Science B.V. All rights reserved.