A. Sethuraman et al., PLANT-CELL-WALL-DEGRADING ENZYMES PRODUCED BY THE WHITE-ROT FUNGUS CERIPORIOPSIS-SUBVERMISPORA, Biotechnology and applied biochemistry, 27, 1998, pp. 37-47
The production of various plant-cell-wall-degrading enzymes by the whi
te-rot fungus Ceriporiopsis subvermispora was monitored in shake-flask
cultures, Analyses included various cellulolytic (i.e. endo-1,4-beta-
glucanase, exo-1,4-beta-glucanase, 1,4-beta-glucosidase), hemicellulol
ytic (i.e. xylanases, 1,4-beta-xylosidases, mannanases, 1,4-beta-manno
sidases), and ligninolytic (i.e. laccase and manganese peroxidase) enz
ymes, Other enzymes studied were polyendogalacturonase, proteases, amy
lases, phenolic acid esterases and lipases, Glucose, cellobiose, avice
l and Whatman cellulose were the primary carbon sources used, Other su
bstrates were birch-wood xylan, galacto-mannan and citrus pectin, Grou
nd stems of two fibrous plants, flax and kenaf, were the substrates re
presenting a complete cell-wall composition used, Endo-1,4-beta-glucan
ase and 1,4-beta-glucosidase activities were detected in certain cultu
re solutions but, interestingly, pro significant amount of exo-1,4-bet
a-glucanase activity was found in cultures of any of the carbon source
s, Avicel, in general, gave rise to higher fungal growth and enzyme pr
oduction compared to the more crystalline Whatman cellulose, Xylanase
and mannanase activities were readily detected under all culture condi
tions used, Flax and kenaf flour generally induced more enzyme product
ion over xylan, mannan and pectin, Laccase and manganese peroxidase we
re the two ligninolytic enzymes produced, Pectin, xylan and mannan ind
uced more polyendogalacturonase than other substrates, Proteases and a
mylases were also produced, but no lipase activity was detected, C. su
bvermisporo also produced phenolic acid esterases in the avicel and xy
lan cultures, Preference for a more amorphous cellulose, avicel and he
micelluloses over a more crystalline Whatman cellulose as substrates f
or active growth is most likely the reason for the lignin specificity
of C. subvermispora. Enzyme profiles suggest that C. subvermispora sho
ws a potential for various industrial applications where removal of th
e lignin components, while maintaining cellulosic fibre strength prope
rty, is important.