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  • Articles  (25)
  • Cellulase  (25)
  • Springer  (25)
  • Process Engineering, Biotechnology, Nutrition Technology  (25)
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  • Articles  (25)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 4 (1989), S. 419-428 
    ISSN: 1476-5535
    Keywords: Bacillus ; Paper and board machines ; Starch degrading enzymes ; Cellulase ; Proteases ; Slimicides ; Food packaging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Aerobic spore-forming bacteria were found dominant in the microflora of food packaging paper and board. Twenty-five strains of bacteria belonging to the genusBacillus were isolated from these paper and board machines, papermaking chemicals, and final products of papermaking. Nineteen strains were analyzed for production of α-amylase, α-glucosidase, glucoamylase, pullulanase, β-glucanase, carboxymethyl cellulase, and caseinase, and also for resistance towards industrial biocides. pH and temperature optima for the activity of the enzymes were determined. All strains were found to produce one or more of the enzymes studied. The amylolytic enzymes of most strains had high temperature optima for activity. Vegetative cells of all strains were found very resistant towards the different commercial slimicides used in paper and board mills. This property together with the ability to survive through the dry end of the machine to the final board and paper, and the production of enzymes degrading papermaking chemicals makes these bacteria potentially harmful in paper and board mills.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 3 (1988), S. 273-280 
    ISSN: 1476-5535
    Keywords: Adsorption ; Cellulase ; Cellulose ; Lucerne fiber ; Trichoderma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Protein-extracted lucerne fibers (PELF) had a higher adsorptive capacity forTrichoderma reesei cellulases than a variety of other cellulosic substrates compared on an equal carbohydrate basis. Adsorption at room temperature reached a maximum at about 5 min; desorption was directly proportional to the extent of carbohydrate solubilization. Cellulase binding conformed to a Langmuir isotherm; the maximum cellulasebinding capacity of PELF was 111 filter paper units per g dry weight. About 85% of the cellulase was recovered in the soluble fraction after PELF hydrolysis. Soluble carbohydrates in the hydrolysate inhibited cellulase adsorption to fresh substrate (50% inhibition at a hydrolysate concentration of 7% glucose equivalents). The effect of these carbohydrates on cellulase adsorption was a complex one composed of both enhancing and inhibitory influences. Artificial hydrolysates (known sugars in proportions identical to actual hydrolysates) inhibited adsorption, but glucose, cellobiose and xylose resulted in adsorption enhancement. Acid treatment of the hydrolysate to convert oligosaccharides to monomers increased reducing sugar concentrations and eliminated its capacity for adsorption inhibition.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 7 (1991), S. 257-261 
    ISSN: 1476-5535
    Keywords: Grape waste ; Pressed apple pulp ; Single cell protein ; Cellulolytic fungi ; Cellulase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Extracted grape waster material and pressed apple pulp were tested as carbon sources forPenicillium funiculosum 515,Myrothecium verrucaria 9095 andAspergillus niger TMF-15. They were good growth substrates, especially forA. niger. When cultivated on mixed substrate in optimized nutrient medium,A. niger accumulated a product of 35% crude protein with a maximum productivity of 0.117 g protein/1/h and cellulose consumption of 90.92%.A. niger also produced the highest levels of cellulase activity. Maximum carboxymethyl cellulase and activity against filter paper were 494 units/l and 97 units/l, respectively.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 4 (1989), S. 135-144 
    ISSN: 1476-5535
    Keywords: Xanthomonas campestris ; Xanthan gum ; Secretion ; Cellulase ; Amylase ; Pathogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Mutants ofXanthomonas campestris B 1459 were isolated that are defective in secretion of both cellulase and amylase. Both enzymes accumulated in the periplasmic space. The defects in secretion of cellulase or amylase were partly overcome by introducing into the mutants specific multiple copies of DNA cloned fromX. campestris, and presumed to code for cellulase or amylase enzymes. The mutant strains also showed reduced amounts of extracellular pectinase and protease activities, as if the mutants were generally defective for secretion of extracellular enzymes. The mutants showed reduced pathogenesis for turnip seedlings. The secretion-defective mutants may allow production of xanthan gum with reduced cellulose, pectin, protein and starch-degrading enzyme activities, thereby allowing more widespread mixing of microbially produced xanthan gum with these commercially important water-soluble polymers.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 5 (1990), S. 59-64 
    ISSN: 1476-5535
    Keywords: Cellulase ; Endoglucanase ; Cellulose ; Pseudomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The recombinant plasmid, pPFC4, which carriesPseudomonas fluorescens subsp.cellulosa chromosomal DNA was previously isolated on the basis of its ability to direct the expression of endoglucanase inEscherichia coli. In the present study, some physical and chemical properties of this activity were characterized. The major portion (78.4%) of the endoglucanase activity is found in the periplasmic space ofE. coli. This plasmid-encoded endoglucanase has a pH optimum of approximately 6.0 and a temperature optimum of approximately 50°C. With carboxymethylcellulose-zymograms, after polyacrylamide gel electrophoresis, periplasmic extracts fromE. coli carrying pPFC4 show six distinct bands with endoglucanase activity. The molecular mass of the major endoglucanase band is approximately 29 kDa while the remaining bands with endoglucanase activity range from 48 to 100 kDa. Although the basis of this heterogeneity is not known, the DNA insert of pPFC4 that encodes endoglucanase activity is not large enough to contain six separate genes; hence, the observed array of endoglucanases may result from post-translational modification of one or two primary gene products.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 285-289 
    ISSN: 1476-5535
    Keywords: Cellulase ; Endoglucanase ; Gene sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The DNA of two previously isolated recombinant clones, one fromPseudomonas sp. NCIB 8634 (=Cellvibrio mixtus) (pPC71) and another fromPseudomonas fluorescens subsp.cellulosa (pPFC4) that express endoglucanase activity inE. coli was sequenced. Plasmid pPC71 had three open reading frames, two of which include portions of plasmid pBR322. The third open reading frame occurs entirely within thePseudomonas DNA insert and encodes a protein with a molecular mass of 5845 Da. The DNA insert in pPFC4 was found to contain an open reading frame (PFC-ORF) that encodes a protein of 32189 Da. The major endoglucanase produced inE. coli cells carrying pPFC4 is about 30000 Da [26]. It is concluded that PFC-ORF encodes this endoglucanase. Both ribosome and catabolite gene activator protein binding sites lie upstream from the initiating codon of PFC-ORF. An interesting feature of the PFC-ORF protein is the presence of amino acid motifs Val-Ser-Ser-Ser-Ser and Val-Val-Ser-Ser-Ser-Ser-Ser that occur within a 25 amino acid span.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 1 (1986), S. 259-264 
    ISSN: 1476-5535
    Keywords: Monoclonal antibody ; Cellobiohydrolase I ; Affinity purification ; Cellulase ; Trichoderma reesei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The several components of the fungal cellulase system present practical problems in devising facile and efficient schemes for their purification. We report on a new single-step affinity chromatographic method for purification of cellobiohydrolase I ofTrichoderma reesei based on its selective absorption and elution using an immunomatrix constructed with CnBr-activated Sepharose 4B and monoclonal antibody specific for the enzyme. Isoenzymes of cellobiohydrolase I were purified directly from crude culture filtrate. The method is fast, simple, and of high resolution.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 10 (1992), S. 123-133 
    ISSN: 1476-5535
    Keywords: Clostridia ; Maintenance energy ; Enzyme secretion ; Cellulase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Secretion of cellulolytic activity by the mesophilClostridium strain C7 was studied while the bacterium underwent progressive carbon/energy starvation and the ensuing continuous decline in growth rate. In the slowest range of growth rates studied the organism was in full response to the global regulation imposed by guanosine 5′, 3′-bispyrophosphate (ppGpp). The exoenzymes of the cellulase complex were produced at the same volumetric rate whether or not the response was active. However, the volumetric rate of biomass synthesis was reduced 45% or more by the response. Energy necessary to maintain the ppGpp-regulated state (i.e., maintenance energy) was, therefore, diverted from energy going to synthesis of biomass but not from that going to exoenzyme synthesis, making the yield of cellulase activity per mole of carbon-energy substrate independent of growth rate and the exoenzyme complex produced from the substrate with equal efficiency at all growth rates. The primary consideration in improving exoenzyme productivity by bacteria with this type of energy distribution between secretion, growth, and maintenance is simply increasing yield per mole of carbon-energy substrate, with growth rate effects on yield a secondary and minimum concern.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 35-42 
    ISSN: 1476-5535
    Keywords: Amylase ; Bagasse ; Cellulase ; Pectinase ; Thermomonospora ; Xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Extracellular enzyme production by the actinomycete,Thermomonospora curvata, was characterized during growth at 55°C on bagasse as sole carbon source. Mycelia adhered to the bagasse fibers during early growth and were released in mature cultures. Extracellular protein reached a maximum on 4% (w/v) bagasse and yielded an electrophoretic profile similar to those produced on purified cellulose. Cellulase production on bagasse exceeded that observed forT. curvata on any previously employed substrate. Amylase and pectinase, which were diminished by their instability in culture fluid at growth temperature and by the lack of inducing substrate, were readily inducible by addition of starch or pectin, respectively. Extracellular activities of β-glucosidase and β-xylosidase remained insignificant throughout growth. Xylanase production equaled or exceeded that observed on a variety of other substrates. The combined activity of extracellular enzymes from bagasse-grownT. curvata caused a 27% solubilization of the fiber, yielding a mixture of cellooligosaccharides, cellobiose, xylobiose, glucose, xylose, fructose, arabinose and mannitol. Fractionation of concentrated extracellular proteins by size exclusion chromatography yielded single peaks for amylase and pectinase (estimated molecular weights of 58 K and 34 K respectively), while cellulase and xylanase activities were distributed throughout a series of multiple unresolved peaks spanning a molecular weight range of 26–180 K.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 1 (1986), S. 149-156 
    ISSN: 1476-5535
    Keywords: Optimization ; Cellulase ; Thermostable enzymes ; Cellulolytic fungi ; Thielavia ; Fermentation ; Production
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Of the eighteen different carbon sources, solka floc was optimal for the induction of cellulases by the thermophilic fungusThielavia terrestris. The temperature optimum for growth was between 44–52°C. The effect of initial and controlled pH on fungal growth and cellulase production was investigated and the results obtained showed that the maximum volumetric productivity (6.07 I.U./1 per h) of filter paper activity was achieved when the pH was controlled at 4.5–5.0.
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