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Fibrolytic activity of enzymes produced by Trametes sp. EUM1, Pleurotus ostreatus IE8 and Aspergillus niger AD96.4 in solid fermentation
Interciencia, 2007-11, Vol.32 (11), p.780-785
[Peer Reviewed Journal]
ISSN: 0378-1844
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Title:
Fibrolytic activity of enzymes produced by Trametes sp. EUM1, Pleurotus ostreatus IE8 and Aspergillus niger AD96.4 in solid fermentation
Author:
Marquez-Araque, A T
;
Martinez, GDM
;
Munoz, SSG
;
Dios, SEB
;
Corral, O L
Subjects:
Aspergillus niger
;
Pleurotus ostreatus
;
Trametes
Is Part Of:
Interciencia, 2007-11, Vol.32 (11), p.780-785
Description:
The enzymatic activity (UI times g super(-1) times dry matter) and specific activity (UI times mg super(-1) protein) of xylanases, celullases and laccases from the fungi Trametes sp. EUM1, Pleurotus ostreatus IE8 and Aspergillus niger AD96.4 was studied at 14 and 19 days of solid fermentation in sugar cane bagasse. The highest activity of xylanases and celullases (P < 0.01) was expressed by Trametes sp., with averages of 141.77UI times g super(-1) DM and 1073.8UI times mg super(-1) protein for xylanases, and 9.04UI times g super(-1) DM and 69.16UI times mg super(-1) protein for cellulases, without significant differences at 14 and 19 days. P. ostreatus and A. niger showed lower activities of these enzymes than Trametes sp., but they were similar among them and in both fermentation periods. The higher (P < 0.01) laccasse activity was expressed by P. ostreatus with averages of 15.54UI times g super(-1) DM and 128.75UI times mg super(-1) protein at 14 days, higher (P < 0.01) than at 19 days (11.75 UI times g super(-1) DM and 102.88UI times mg super(-1) protein). In Trametes sp. the laccasse activity was lower than in P. ostreatus and similar in both fermentation times. In A. niger the laccasse activity was lower (P < 0.01) than Trametes sp. and P. ostreatus. The activity of fibrolytic enzymes in Trametes sp. EUM1 indicates a potential use for biotechnological applications.
Language:
Spanish
Identifier:
ISSN: 0378-1844
Source:
Alma/SFX Local Collection
ProQuest Central
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