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  • Articles  (28)
  • Cellulase  (25)
  • Triticum aestivum
  • fish
  • Springer  (28)
  • Process Engineering, Biotechnology, Nutrition Technology  (28)
  • 1
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    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.
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  • 2
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    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
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    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
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    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
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    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
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    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
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    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
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    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
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    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
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    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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  • 11
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    Journal of industrial microbiology and biotechnology 10 (1992), S. 103-110 
    ISSN: 1476-5535
    Keywords: Cellulase ; Thermophilic ; Monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Cellobiohydrolase II was purified from aMicrobispora bispora culture filtrate and a monoclonal antibody to it was prepared. Screening aM. bispora genomic library inEscherichia coli with this antibody yielded three equivalent clones. Subcloning resulted in greater expression, and activity could be monitored using 4-methylumbelliferylcellobioside. Southern analysis provided evidence that there is a single gene coding for CBH II. The original 22-kb fragment was reduced to 4 kb and subcloned into pUC118/119 resulting in a doubling of expression CBH II. The gene was expressed via its own promoter. The optimal pH (6.5) and the optimal temperature (60°C) of the cloned enzyme are similar to that of the native CBH II.
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  • 12
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    Journal of industrial microbiology and biotechnology 2 (1987), S. 9-13 
    ISSN: 1476-5535
    Keywords: Lignocellulosic waste ; Trichoderma ; Single cell protein production ; Cellulase ; Xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Characterization of lignocellulosic wastes from three paper mills in New York State indicated that a kraft mill sludge contained substantial quantities of utilizable cellulose and hemicellulose. This residue was tested as a carbon source for seven cellulolytic fungi.Trichoderma reesei DAOM 167654 accumulated a product of over 22% crude protein, and caused a conversion of sludge to protein of almost 15% in 3 days growth in shake flasks.T. reesei also produced the highest levels of cellulase, whileT. longibrachiatum produced more xylanase (35 units/ml) than other fungi examined.
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  • 13
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    Journal of industrial microbiology and biotechnology 11 (1993), S. 151-155 
    ISSN: 1476-5535
    Keywords: Erwinia ; Lignocellulose ; Cellulose ; Ethanol ; Cellulase ; Xylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The soft-rot bacteriaErwinia carotovora SR38 andErwinia chrysanthemi EC16 have been genetically engineered to efficiently produce ethanol and carbon dioxide as primary fermentation products from cellobiose, glucose and xylose. These organisms have the native ability to secrete a battery of hydrolases and lyases to aid in the solubilization of lignocellulose. Both strains of ethanologenicErwinia fermented cellobiose at twice the rate of the cellobioseutilizing yeasts (Spindler et al., 1992. Biotechnology Letters 14: 403–407) and may be useful in simultaneous saccharification and fermentation processes.
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  • 14
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    World journal of microbiology and biotechnology 8 (1992), S. 183-186 
    ISSN: 1573-0972
    Keywords: Aspergillus niger ; Cellulase ; cellulosic waste ; co-culture ; Trichoderma reesei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A cellulase system possessing high hydrolytic and β-glucosidase activity was obtained by co-culturingTrichoderma reesei andAspergillus niger by a new approach using semi-solid fermentation of lignocellulosic materials. Various types of pretreatments were used for making the cellulose easily accessible to enzymatic attack. The optimal water content for maximum activity of the mixed fermentation was investigated. A more concentrated enzyme preparation could be obtained by semi-solid state fermentation than by conventional submerged fermentation.
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  • 15
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    World journal of microbiology and biotechnology 8 (1992), S. 534-535 
    ISSN: 1573-0972
    Keywords: Cellulase ; cellulose hydrolysis ; Penicillium janthinellum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The maximal carboxymethyl cellulase, filter paper (FP) cellulase and β-glucosidase activities achieved byPenicillium janthinellum grown in a fermenter were 60, 5 and 9 U/ml, respectively. Enzymic hydrolysis of 5m NaOH-pre-treated straw, cotton and FP was 57 to 58% in 48 h at 50°C, with glucose as the major product.
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  • 16
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    World journal of microbiology and biotechnology 9 (1993), S. 120-121 
    ISSN: 1573-0972
    Keywords: Cellulase ; pre-treatment ; wheat straw
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Wheat straw, pre-treated with either alkali or steam, or both together, was used 46% more efficiently byTrichoderma reesei than untreated straw. Carboxymethyl cellulase and filter paper cellulase were higher by 52% and 74%, respectively, in the treated substrate compared with the untreated one.
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  • 17
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    World journal of microbiology and biotechnology 10 (1994), S. 487-487 
    ISSN: 1573-0972
    Keywords: Cellulase ; Fusarium ; Trichoderma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Fusarium lini, F. lycopersici, F. pallidoroseum and F. semitectum grown in shake flasks produced, respectively, 0.19, 0.33, 0.13 and 0.09 units filter-paper cellulase/ml. Trichoderma reesei, in comparison, produced 0.8 U/ml.
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  • 18
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    World journal of microbiology and biotechnology 7 (1991), S. 613-618 
    ISSN: 1573-0972
    Keywords: Cellulase ; β-glucosidase ; Myceliophthora thermophila ; PNPG
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The extracellular β-glucosidase has been purified from culture broth of Myceliophthora thermophila ATCC 48104 grown on crystalline cellulose. The enzyme was purified approximately 30-fold by (NH4)2SO4 precipitation and column chromatography on DEAE-Sephadex A-50, Sephadex G-200 and DEAE-Sephadex A-50. The molecular mass of the enzyme was estimated to be about 120 kD by both sodium dodecyl sulphate gel electrophoresis and gel filtration chromatography. It displayed optimal activity at pH 4.8 and 60°C. The purified enzyme in the absence of substrate was stable up to 60°C and pH between 4.5 and 5.5. The enzyme hydrolysed p-nitrophenyl-β-d-glucoside, cellobiose and salicin but not carboxymethyl cellulose or crystalline cellulose. The K m of the enzyme was 1.6mm for p-nitrophenyl-β-d-glucoside and 8.0mm for cellobiose. d-Glucose was a competitive inhibitor of the enzyme with a K of 22.5mm. Enzyme K activity was inhibited by HgCl2, FeSO4, CuSO4, EDTA, sodium dodecyl sulphate, p-chloromercurobenzoate and iodoacetamide and was stimulated by 2-mercaptoethanol, dithiothreitol and glutathione. Ethanol up to 1.7 m had no effect on the enzyme activity.
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  • 19
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    World journal of microbiology and biotechnology 8 (1992), S. 284-286 
    ISSN: 1573-0972
    Keywords: Bacillus ; budu ; fermentation ; fish ; proteases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Eight different strains ofBacillus were isolated from fermented fish (Budu) and their proteolytic enzyme activities were determined after 18 h cultivation at room temperature (35° C). Four isolates possessed high protease activities. Optimum pH for these enzymes was between 7.0 and 8.0 and the optimal temperature was 55° C. The proteases retained 40% of their original activity after 20 min at 55° C but lost all activity at 65° C. Three of the four isolates were identified asBacillus subtilis, the fourth asBacillus licheniformis.
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  • 20
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    World journal of microbiology and biotechnology 8 (1992), S. 313-315 
    ISSN: 1573-0972
    Keywords: Cellulase ; endoglucanase ; exoglucanase ; glucosidase ; Vibrio agar-liquefaciens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Vibrio agar-liquefaciens produced the component enzymes of a cellulase complex (exoglucanase, endoglucanase and β-glucosidase). Whilst complete cellulase activity occurred in three media, each containing carboxymethylcellulose as the sole carbon source, different activities of the individual enzymes resulted. The enzymes showed a temporal sequence in their activity and differed in pH and temperature optima. NaCl enhanced the enzyme activities to varying degrees at different substrate concentrations.
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  • 21
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    World journal of microbiology and biotechnology 9 (1993), S. 164-167 
    ISSN: 1573-0972
    Keywords: Cellulase ; immobilized enzymes ; Macrophomina phaseolina ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The stability of cellulolytic and hemicellulolytic enzymes from Macrophomina phaseolina improved on immobilization and was 1.5 to 2-fold more active against pre-treated wheat bran, rice bran or jute powder. The hydrolysis efficiency of the catalyst increased with a decrease in its particle size. About 80% (w/v) of the sugar obtained from wheat bran was assimilated by Saccharomyces sp., whereas the corresponding values for rice bran and jute powder were about 70 and 50% (w/v), respectively.
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  • 22
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    World journal of microbiology and biotechnology 9 (1993), S. 100-101 
    ISSN: 1573-0972
    Keywords: Cellulase ; cellulose ; Penicillium citrinum ; protein ; solid state fermentation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Penicillium citrinum, using rice husks in a solid state fermentation, produced maximum cellulase yields (37 Units/g) after 12 days with a cellulose utilization of more than 70%. Enzyme yields were three times higher than in shake-flask cultures.
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  • 23
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    World journal of microbiology and biotechnology 13 (1997), S. 367-373 
    ISSN: 1573-0972
    Keywords: Amphibian ; aquaculture ; epizootic haematopoietic necrosis virus ; fish ; frog virus 3 ; Iridoviridae ; ranavirus ; reptile
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Systemic infections of teleost fishes caused by iridoviruses have recently been recognized in Australia, Asia, Europe and the USA. These iridoviruses are different from those of the established genera Lymphocystivirus and Goldfish Virus 1-like Viruses of the family Iridoviridae. The agents exhibit similar physicochemical properties, are antigenically related and prove to be of high virulence to different teleost fishes in aquaculture. The first iridovirus, epizootic haematopoietic necrosis virus, responsible for an epizootic outbreak of haematopoietic necrosis in redfin perch, was reported in Australia. Some years later, similar iridovirus epizootics occurred in sheatfish and catfish in Europe. The Australian and the European isolates proved to be antigenically related and showed properties in common with frog virus 3, the type species of the genus Ranavirus of the Iridoviridae. Further iridovirus isolates from fish, amphibians and reptiles exhibited a close relationship with each other and with frog virus 3. It is important to note that the Australian amphibian iridovirus, Bohle iridovirus, was experimentally transmitted to teleost fish inducing high mortalities. The occurrence of similar viruses in different host species in the aquatic environment and their inter-species transmission emphasize the importance of health control in aquaculture.
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  • 24
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    World journal of microbiology and biotechnology 13 (1997), S. 487-490 
    ISSN: 1573-0972
    Keywords: Cellulase ; filamentous fungi ; β-glucosidase ; submerged fermentation ; pretreated poplar wood
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Gliocladium sp. TUB F-498, a wild strain of a lignocellulolytic fungus with a fast growth rate and enzyme production rate was selected as a potential in situ enzyme source for the bioprocessing of pretreated poplar wood (PPW) to ethanol in a simultaneous saccharification and fermentation process. TUB F-498 produced 77 filter paper units of cellulase activity and 246 IU of β-glucosidase activity per g dry weight of substrate utilized, as compared with the highly successful mutant reference strain Trichoderma reesei Rut-C30, which produced 100 filter paper units and 92 IU per g dry weight substrate in a stirred-tank fermentation. TUB F-498 also produced more xylanase and endoglucanase activity than Rut-C30 on PPW in shake-flask fermentations.
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  • 25
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    World journal of microbiology and biotechnology 10 (1994), S. 280-284 
    ISSN: 1573-0972
    Keywords: Cellulase ; enzyme production ; β-glucosidase ; Penicillium purpurogenum ; xylanases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A cellulolytic wild-type strain of Penicillium purpurogenum was isolated from a soil sample in southern Chile. It grew best at 28°C from an inoculum of 4×107 spores/100 ml medium. Highest endoglucanase activity was with Sigmacell as carbon source and corn steep liquor as nitrogen source. Wheat bran enhanced the production of endoglucanase and β-glucosidase. The enzymes in the crude supernatants were stable up to 50°C and between pH 4.4 and 5.6 for 48 h.
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  • 26
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    World journal of microbiology and biotechnology 11 (1995), S. 347-348 
    ISSN: 1573-0972
    Keywords: Cellulase ; lignocellulose ; kallar grass straw ; thermophilic fungi ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Seven indigenous thermophilic fungi were screened for cellulase and xylanase production when grown on Leptochloa fusca (kallar grass) straw. Aspergillus fumigatus produced the highest activities of 0.4, 2.5, 3.5 and 0.14 U/ml of filter paper cellulase, CM-cellulase, xylanase and β-xylosidase, respectively. Sporotrichum thermophile produced 0.47 β-glucosidase/ml. Chaetomium thermophile, Humicola grisea and Torula thermophila had lower activities than the other thermophilic fungi.
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  • 27
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    World journal of microbiology and biotechnology 15 (1999), S. 417-423 
    ISSN: 1573-0972
    Keywords: 15N ; nitrogen mineralization ; Pseudomonas fluorescens ; rhizosphere ; Triticum aestivum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The effects of an antibiotic-producing Pseudomonas fluorescens strain (F113) carrying the marker gene cassette lacZY and a marked, non-producing strain (F113G22) on the uptake of nitrogen from 15N-enriched organic residues incorporated into a sandy soil were investigated in microcosm studies. Strain F113 produces the antibiotic 2,4-diacetylphloroglucinol (DAPG), whilst its modified derivative strain F113G22 has DAPG production deleted by Tn5 mutagenesis. Uptake of nitrogen by wheat (Triticum aestivum) from 15N-enriched organic residues was estimated using stable isotope-ratio mass spectrometry of shoot and root material of 17-day-old plants. In addition, plant growth and active microbial biomass in soil were monitored. In contrast to results obtained in our previous study on pea (Pisum sativum), it was found that in wheat, inoculation with either strain F113 or F113G22 decreased the proportion of nitrogen derived from 15N-labelled organic residues incorporated into soil as compared to non-inoculated controls. It is therefore suggested that these strains decreased mineralization of organic residues in the rhizosphere of wheat, making less inorganic N (15N) available for plant uptake. The results of this study indicate that the effects of introduced Pseudomonas fluorescens strains on nitrogen mineralization in the rhizosphere are plant-species dependent, and highlight the importance of testing microbial inocula on a range of plant species.
    Type of Medium: Electronic Resource
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  • 28
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 695-695 
    ISSN: 1573-0972
    Keywords: Cellulase ; submerged fermentation ; Volvariella diplasia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Volvariella diplasia produced cellulolytic enzymes (550 U CM-cellulase and 69 U filter-paper cellulase/l) when grown in shake culture at pH 5.4 and 28°C with 0.5% cellulose powder as carbon source. Alkali-treated as well as untreated cellulosic substrates were hydrolysed by both enzymes (sp. act. 2.75 U/mg protein), with cellobiose and glucose as the end products.
    Type of Medium: Electronic Resource
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