Agar-diffusion assay of cellulolytic ability of thermophilic fungi

Tansey, Michael R.

doi:10.1007/bf00407983

Cited by 96 publications

(28 citation statements)

References 19 publications

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“…Several species of mucor which include Mucor pusillus and Mucor michei are not cellulolytic (Tausey, 1971).…”

Section: Resultsmentioning

confidence: 99%

Screening of Some Fungi Associated with Maize Cob Degradation for Cellulase Activity

Bamigboye¹

2013

GJBS

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Fungi involved in the biodegradation of maize-cob were isolated and screened for cellulase activity using glucose and carboxylmethyl cellulose as carbon sources. The effect of the carbon sources on cellulase production was determined. Eleven fungi species were isolated which include Rhizopus oryzae, Aspergillus flavus, Mucor racemosus, Aspergillus niger, Penicillium atrovenetum, Penicillium expansum, Botryotrichum piluliferum, Penicillium chrysogenum and Penicillium restictum. Effect of carbon source on cellulase production was also reported. The highest reducing sugar production for all fungi isolate was obtained on day 14 when carboxymethyl cellulose (CMC) was used as the carbon source; while the highest reducing sugar production was obtained on day 7 when glucose was used as the carbon source. Aspergillus niger had the highest production of reducing sugar (1.68mg/ml and 0.82/m) in CMC and glucose respectively while the lowest production was recorded for Mucor racemosus (0.69mg/,ml and 0.01mg/ml). All Aspergillus species and Penicilluim species isolated had very high reducing sugar production in CMC: Aspergillus flavus 1.24 mg/ml; A oryzae 1.08mg/ml, P expansum 1.60 mg/ml, P atrovenetum 1.43mg/ml except Penicillium chrysonenum and Penicillium restrictum with 0.78mg/ml and 0.81 mg/ml, respectively.Aspergillus and Penicillum species are good cellulase producers especially those that are associated with degrading maize cob. These organisms are considered suitable to increase the nutrient of maize-cob, an agro industrial waste and consequently make them useful for animal feed production.

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“…Several species of mucor which include Mucor pusillus and Mucor michei are not cellulolytic (Tausey, 1971).…”

Section: Resultsmentioning

confidence: 99%

Screening of Some Fungi Associated with Maize Cob Degradation for Cellulase Activity

Bamigboye¹

2013

GJBS

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“…and Tansey (1971). However, as a rule these investigators employed the most resistant forms of cellulose in their selective media and enzyme assays.…”

Section: Discussionmentioning

confidence: 99%

“…However, as a rule these investigators employed the most resistant forms of cellulose in their selective media and enzyme assays. Methods such as the measurement of the depth of clearing in cellulose-agar tubes (Tansey, 1971) or the disruption of filter paper, are simply not sensitive enough to detect the activity of culture filtrates of weakly cellulolytic organisms. The selective medium employed by Fergus ( 1969) included, in addition to a cellulose derivative (CMC), components such as urea that on their own may serve as the source of carbon for Mucor pusillus (G. A .…”

Section: Discussionmentioning

confidence: 99%

Synthesis of Cellulase by Mucor pusillus and Mucor miehei

Somkuti

2000

Microbiology

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“…Fractions I, 11, 111 and IV correspond to intact CBH 11, core protein and glycopeptides as specified in the text. (A) staining with Coomassie blue; (B) staining with fluorescamine of Polybrene/glass-fiber blot [22] commercial (Avicel PH 101, FMC Corp., USA) and the amorphous form was obtained as phosphoric-acid-swollen Whatman CF 11 cellulose (Balson OTD, UK) [18].…”

Section: Methodsmentioning

confidence: 99%

Studies of the cellulolytic system of Trichoderma reesei QM 9414

Tomme¹,

Tilbeurgh²,

Pettersson³

et al. 1988

European Journal of Biochemistry

532

276

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Limited action of papain on the native forms of two cellobiohydrolases (CBH) from Trichoderma reesei (CBH I, 65 kDa, and CBH II,58 kDa) leads to the isolation of the respective core fragments (56 kDa and 45 kDa) which are fully active on small, soluble substrates, but have a strongly reduced activity (respectively 10% and 50% of the initial value) on microcrystalline cellulose (Avicel).By partial sequencing at the C terminus of the CBH I core and at the N terminus of the CBH I1 core the papain cleavage sites have been assigned in the primary structures (at about residue 431 and 82 respectively). This limited action of papain on the native enzymes indicates the presence of hinge regions linking the core to these terminal glycopeptides. The latter conserved sequences appear either at the C or N terminus of several cellulolytic enzymes from ~r~c~o d e r m a reesei [Teeri et al. (1987) Gene 51,43 -521. The specific activities of the intact enzymes and their cores on two forms of insoluble cellulose (crystalline, amorphous) differentiate the CBH I and CBH TI in terms of adsorption and catalytic properties, Distinct functions can be attributed to the terminal peptides: for intact CBH I1 the N-terminal region contributes in the binding onto both cellulose types; the homologous C-terminal peptide in CBH I, however, only affects the interaction with microcrystalline cellulose. It could be inferred that CBH I and its core bind preferentially to crystalline regions. This seems to be corroborated by the results of CBH I/CBH I1 synergism experiments.The filamentous fungus Trichoderma reesei presents an ideal system for the study of cellulose hydrolysis since it produces a variety of enzymes including endocellulase and exocellulase (cellobiohydrolases) and b-glucosidases (cellobiases) [l]. The primary structure of several of these proteins is presently known [2 -61 but no structure/function relationships have yet been established. The two cellobiohydrolases, CBH I and CBH I1 [7 -111, lack any apparent homology in their amino acid sequence except for a conserved region present at their C and N termini respectively [4].Their action is similar both with regard to their strong adsorption onto insoluble substrates and lack of carboxymethylcellulase activity. However, studies both with microcrystalline cellulose [9] and small, soluble substrates [I 21 reveal some differences in specificity. In addition, the two cellobiohydrolases interact synergistically both with each other and with endoglucanases on microcrystalline substrates In order to differentiate these enzymes further by their function and to investigate possible domain structure, proteolysis studies were performed. Preliminary results on the limited action of papain on native CBH I have been reported by us [16]. Two fragments were isolated: first, a heavily glycosylated peptide, tentatively identified with the C terminus; secondly, a core protein containing the active (hydrolytic) site. The terminal peptide was characterised as an independent structural and functional dom...

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Agar-diffusion assay of cellulolytic ability of thermophilic fungi

Cited by 96 publications

References 19 publications

Screening of Some Fungi Associated with Maize Cob Degradation for Cellulase Activity

Screening of Some Fungi Associated with Maize Cob Degradation for Cellulase Activity

Synthesis of Cellulase by Mucor pusillus and Mucor miehei

Studies of the cellulolytic system of Trichoderma reesei QM 9414

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