Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: KEGG:D03434 (Cellulase)
512 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lactose (1,4-O-beta-d-galactopyranosyl-d-glucose) is a soluble and economic carbon source for the industrial production of cellulases or recombinant proteins by Hypocrea jecorina (anamorph Trichoderma reesei). The mechanism by which lactose induces cellulase formation is not understood. Recent data showed that the galactokinase step is essential for cellulase induction by lactose, but growth on d-galactose alone does not induce cellulases. Consequently, the hypothesis was tested that d-galactose may be an inducer only at a low growth rate, which is typically observed when growing on lactose. Carbon-limited chemostat cultivations of H. jecorina were therefore performed at different dilution rates with d-galactose, lactose, galactitol and d-glucose. Cellulase gene expression was monitored by using a strain carrying a fusion between the cbh2 (encoding cellobiohydrolase 2, Cel6A) promoter region and the Aspergillus niger glucose oxidase gene and by identification of the two major cellobiohydrolases Cel7A and Cel6A. The results show that d-galactose indeed induces cbh2 gene transcription and leads to Cel7A and Cel6A accumulation at a low (D=0.015 h(-1)) but not at higher dilution rates. At the same dilution rate, growth on d-glucose did not lead to cbh2 promoter activation or Cel6A formation but a basal level, lower than that observed on d-galactose, was detected for the carbon-catabolite-derepressible Cel7A. Lactose induced significantly higher cellulase levels at 0.015 h(-1) than d-galactose and induced cellulases even at growth rates up to 0.042 h(-1). Results of chemostats with an equimolar mixture of d-galactose and d-glucose essentially mimicked the behaviour on d-galactose alone, whereas an equimolar mixture of d-galactose and galactitol, the first intermediate of a recently described second pathway of d-galactose catabolism, led to cellulase induction at D=0.030 h(-1). It is concluded that d-galactose indeed induces cellulases at low growth rate and that the operation of the alternative pathway further increases this induction. However, under those conditions lactose is still a superior inducer for which the mechanism remains to be clarified.
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PMID:D-Galactose induces cellulase gene expression in Hypocrea jecorina at low growth rates. 1662 67

Cellulase and bovine serum albumin (BSA) were added to Avicel cellulose and solids containing 56% cellulose and 28% lignin from dilute sulfuric acid pretreatment of corn stover. Little BSA was adsorbed on Avicel cellulose, while pretreated corn stover solids adsorbed considerable amounts of this protein. On the other hand, cellulase was highly adsorbed on both substrates. Adding a 1% concentration of BSA to dilute acid pretreated corn stover prior to enzyme addition at 15 FPU/g cellulose enhanced filter paper activity in solution by about a factor of 2 and beta-glucosidase activity in solution by about a factor of 14. Overall, these results suggested that BSA treatment reduced adsorption of cellulase and particularly beta-glucosidase on lignin. Of particular note, BSA treatment of pretreated corn stover solids prior to enzymatic hydrolysis increased 72 h glucose yields from about 82% to about 92% at a cellulase loading of 15 FPU/g cellulose or achieved about the same yield at a loading of 7.5 FPU/g cellulose. Similar improvements were also observed for enzymatic hydrolysis of ammonia fiber explosion (AFEX) pretreated corn stover and Douglas fir treated by SO(2) steam explosion and for simultaneous saccharification and fermentation (SSF) of BSA pretreated corn stover. In addition, BSA treatment prior to hydrolysis reduced the need for beta-glucosidase supplementation of SSF. The results are consistent with non-specific competitive, irreversible adsorption of BSA on lignin and identify promising strategies to reduce enzyme requirements for cellulose hydrolysis.
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PMID:BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates. 1667 19

Seven cellulase preparations from Penicillium and Trichoderma spp. were evaluated for their ability to hydrolyze the cellulose fraction of hardwoods (yellow poplar and red maple) pretreated by organosolv extraction, as well as model cellulosic substrates such as filter paper. There was no significant correlation among hydrolytic performance on pretreated hardwood, based on glucose release, and filter paper activity. However, performance on pretreated hardwood showed significant correlations to the levels of endogenous beta-glucosidase and xylanase activities in the cellulase preparation. Accordingly, differences in performance were reduced or eliminated following supplementation with a crude beta-glucosidase preparation containing both activities. These results complement a previous investigation using softwoods pretreated by either organosolv extraction or steam explosion. Cellulase preparations that performed best on hardwood also showed superior performance on the softwood substrates.
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PMID:Evaluation of cellulase preparations for hydrolysis of hardwood substrates. 1691 67

Cellulase production was investigated in a culture of a strain of Acremonium cellulolyticus. The medium components were optimized for the improvement of cellulase production. The maximum production of cellulolytic enzymes was obtained in a medium containing (grams per liter) 50 Solka Floc, 5 (NH4)2SO4, 24 KH2PO4, 4.7 potassium tartrate hemihydrate, 1.2 MgSO4.7H2O, 1 Tween 80, 4 urea, 0.01 ZnSO4.7H2O, 0.01 MnSO4.6H2O, and 0.01 CuSO4.7H2O, with a pH of 4.0. In the flask culture, 15.5 filter paper units (FPU)/mL of maximum cellulase activity was obtained, 17.42 FPU/mL in a 7-L bioreactor, and 13.08 FPU/mL in a 50-L scale bioreactor for 4-8 d at 30 degrees C. Average production rates were 1.94 FPU/mL.d in flasks, 2.86 FPU/mL.d in the 7-L bioreactor, and 2.56 FPU/mL.d in the 50-L bioreactor. Cellulase production on a small scale was successfully reproduced in the 50-L pilot scale bioreactor. Saccharification activity from A. cellulolyticus was compared with cellulolytic enzymes produced by other strains. The A. cellulolyticus culture broth had a comparable saccharification yield in comparison with those of other Trichoderma enzymes (GC220 or Cellulosin T2) under the same total cellulase activity. Its saccharification yield (percent of released reducing sugar to used dried substrate) was 60%, and its glucose content was 83%.
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PMID:Efficient cellulase production by the filamentous fungus Acremonium cellulolyticus. 1725 23

Wheat straw (Ws)was treated in a pilot-scale continuous mixer to disrupt the lignin-hemicellulose-cellulose (LHC) complex. An efficient and practical method was desired to remove lignin and hemicellulose (pentosans)rapidly and efficiently from the lignocellulose complex and to make the cellulose accessible to enzymatic hydrolysis. Milled WS in the presence of various chemicals in aqueous solutions was extruded from the mixer under several processing conditions. Chemicals used were sodium hydroxide (NaOH) sodium sulfide (Na(2)S), anthraquinone (AQ), anthrahydroquinone (AHQ), hexamethylenediamine (HMDA), hexamethylenetetramine (HMTA) hydrogen peroxide (H(2)O(2)), and ferrous ammonium sulfate (FAS), which were used alone and in selected combinations. Concomitantly, WS was treated in laboratory batches using similar reaction conditions, except for mixing and shearing. In extrusion treatments of WS at 20% concentration at 97 degrees C for 5.5 min with NaOH (15.7%, dry WS basis), NaOH (15.7%) + AHQ (0.3%), and NaOH (12.7%) + Na(2)S (5.0%), 64-72% of the WS lignin and 36-43% of the pentosans were removed from aqueously washed extrudates (residues). This compares with 46-56% and 23-27%, respectively, for batch treatments. AHQ and Na(2)S enhanced delignification. Cellulase treatment of the residues, which contained about 99%of the WS cellulose, converted 90-92%of the cellulose to glucose compared with 61-69%for the batch pretreatments. Treatments of WS with amines and H(2)O(2) (alone or combined with NaOH)were less effective for LHC disruption. In all instances the relatively high-shear extrusion treatments were superior to the laboratory-batch treatments.
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PMID:Modification of wheat straw in a high-shear mixer. 1855 45

A washed carrot substrate, prepared with high yields and easy handling properties, was found to be a suitable substrate for studying cellulolytic and pectinolytic degradation processes. A cellulase from Trichoderma reesei, and Rohament P, a macerating enzyme from Aspergillus alleaceus in endopolygalacturonase, degraded the washed carrot substrate to an extent of 60%. With the combined action of both enzymes, degradation was more than 80%. Simultaneous action of both enzymes was more efficient than their sequential use. The effect of temperature, pH, incubation time, enzyme concentration, and substrate concentration on the degradation by the single enzymes and their mixture were studied. Gas chromatographic sugar analysis revealed that Rohament P liberated glucose, arabinose, and galactose in the low-molecular-weight fraction obtained by ultrafiltration, in addition to high amounts of galacturonic acid. These carbohydrates were also found in the high-molecular-weight fraction (retentate) together with rhamnose and mannose. Cellulase BC released mainly glucose, although galacturonic acid, arabinose, xylose, and mannose were also detected both in the ultrafiltrate and retentate. Morphologically, during Rohament P degradation of the washed carrot substrate, damaged tissues and disintegrated cells were seen, whereas on cellulase BC action mainly disintegrated cell walls were observed.
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PMID:Degradation of a washed carrot preparation by cellulases and pectinases. 1855 48

Treatment of wheat straw with 1N trifluoroacetic acid (TFA) for 7 h at reflux temperature yielded 23% xylose based upon initial straw weight. This corresponds to about an 80% xylose yield based on the xylan content of the hemicellulose. The cellulose component of wheat straw was largely unaffected, as evidenced by low glucose yields. Decomposition of xylose by prolonged refluxing (23 h) was minimal in 1N TFA compared to 1N HCl. Treatment of wheat straw with refluxing 1N TFA converts about 10% of the lignin initially present in straw into water-soluble lignin fragments. Fermentation of the xylose-rich wheat straw hydrolyzate to ethanol with Pachysolen tannophilus was comparable to the fermentation of reagent grade xylose, indicating that furfural and toxic lignin by-products were not produced by 1N TFA in sufficient amounts to impair cell growth and ethanol production. Cellulase treatment of the wheat straw residue after TFA hydrolysis resulted in a 70-75% conversion of the cellulose into glucose.
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PMID:Hydrolysis of wheat straw hemicellulose with trifluoroacetic acid. Fermentation of xylose with Pachysolen tannophilus. 1855 35

Cellulase produced by fungus Trichoderma viride was immobilized on agarose beads (Sepharose 4B) activated by cyanogen bromide and also on activated agarose beads that contained spacer arm (activated CH-Sepharose 4B and Affi-Gel 15). The CMCase activity retained by immobilized cellulase on activated Sepharose containing the spacer tended to be higher than that immobilized without spacer, although the extent of protein immobilization was lower. Also, the higher substrate specificity for cellulase immobilized on beads with spacer was obtained for cellobiose, acid-swollen cellulose, or cellulose powder. The hydrolysis product from their substrates was mainly glucose.
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PMID:Properties of cellulase immobilized on agarose gel with spacer. 1855 5

The cellulose dissolution solvent used in Lyocell process for cellulose fiber preparation, N-methylmorpholine-N-oxide (NMMO) monohydrate, was demonstrated to be an effective agent for sugarcane bagasse pretreatment. Bagasse of 20wt% was readily dissolved in NMMO monohydrate at 130 degrees C within 1h. After dissolution, bagasse could be regenerated by rapid precipitation with water as a porous and amorphous mixture of its original components. The regenerated bagasse exhibited a significant enhancement on enzymatic hydrolysis kinetic. Not only the reducing sugars releasing rate but also hydrolysis yield was enhanced at least twofold as compared with that of untreated bagasse. The cellulose fraction of regenerated bagasse was nearly hydrolyzed to glucose after 72h hydrolysis with Cellulase AP3. The recycled NMMO demonstrated the same performance as the fresh one on bagasse pretreatment for hydrolysis enhancement. The regenerated bagasse was directly used in simultaneous saccharification and fermentation (SSF) for ethanol production by Zymomonas mobilis. No negative effect on ethanol fermentation was observed and ethanol yield approximately 0.15 g ethanol/g baggasse was achieved.
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PMID:Enhanced enzymatic hydrolysis of sugarcane bagasse by N-methylmorpholine-N-oxide pretreatment. 1871 63

Cellulase and beta-glucosidase production on steam pretreated spruce (SPS) with Trichoderma reesei Rut C30, Trichoderma atroviride TUB F-1505 and TUB F-1663 was investigated. The enzymes were compared in term of activity, temperature optima and hydrolytic capacity. The T. atroviride cellulases proved to have lower temperature optima for filter paper activity (FPA) assay (50 degrees C) and for hydrolysis of SPS (40 degrees C) than the Rut C30 enzymes (60 degrees C for FPA and 50 degrees C for hydrolysis). Due to high levels of extracellular beta-glucosidases, the T. atroviride enzyme supernatants hydrolyzed the washed SPS to glucose more efficiently than the enzymes produced by T. reesei. On the other hand, when the whole fermentation broths were used instead of the supernatants, thus the mycelium bound enzymes were also present, the hydrolytic capacity of T. reesei Rut C30 was enhanced by approximately 200%, while an improvement of only 15% was observed in case of the T. atroviride isolates.
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PMID:Comparative enzymatic hydrolysis of pretreated spruce by supernatants, whole fermentation broths and washed mycelia of Trichoderma reesei and Trichoderma atroviride. 1879 35


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