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  • 1
    Electronic Resource
    Electronic Resource
    Indian symposium (1984)
    [s.l.] : Nature Publishing Group
    Nature 309 (1984), S. 108-108 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR ? We have read the news item in Nature (1 March p.6) regarding the inability of Israeli scientists to attend the VIIth International Biotechnology Symposium. To put the record straight, the organizers did everything possible to help the scientists from Israel to attend the symposium. In fact, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/309108b0
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of Bacterial Sulphate-Reduction in Presence of Short Chain Fatty Acids (1955)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 8 (1955), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1955.tb08965.x
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  • 3
    Electronic Resource
    Electronic Resource
    Stimulation of Bacterial Sulphate-Reduction by (+)-Biotin (1954)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 7 (1954), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1954.tb07732.x
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  • 4
    Electronic Resource
    Electronic Resource
    An analysis of the relative activities of a number of promoter constructs from genes which are expressed during late pollen development as determined by particle bombardment (1995)
    Springer
    Plant cell reports 15 (1995), S. 154-158 
    Details
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The promoters of a tobacco actin gene, a tobacco pectate lyase, a tobacco and maize polygalacturonase and aBrassica S-locus related gene have been fused to theβ-glucuronidase reporter gene and their activities determined by biolistic transient assay in tobacco pollen. In stably transformed tobacco all the transgenes with the exception of Cauliflower Mosaic Virus-35S-β-glucuronidase appear to express efficiently in maturing pollen. Transient assay analysis showed that the tobacco pectate lyase and the polygalacturonase constructs were 8x more active than the tobacco actin construct, and that the tobacco polygalacturonase construct was some 33x more active than the maize polygalacturonase construct. Constructional manipulations that altered the lengths of the 5′-untranslated leaders including one which resulted in the removal of a 490 bp leader intron had little effect on the observed level of expression. However, the alteration of the context of the ATG from A/TnnATGG to CnnATGT resulting in a 70% reduction in the observed levels of activity, was obtained with the pectate lyase and polygalacturonase promoters. An identical reductional was also observed in transgenic plant populations transformed with the polygalacturonase transgenes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01690275
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  • 5
    Electronic Resource
    Electronic Resource
    Response from New Delhi (1985)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 3 (1985), S. 591-591 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] To the editor: This is a response to the letter from MIT's Arnold Demain (Sept. 1984) concerning inability on the part of some bioscientists from Israel to participate in the VIIth International Biotechnology Symposium held in New Delhi in February 1984. A key point seems to be missing from Dr. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0785-591e
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  • 6
    Electronic Resource
    Electronic Resource
    Studies on the symbiosis of mixed culture ofAzotobacter and yeast (1975)
    Springer
    Applied microbiology and biotechnology 1 (1975), S. 95-119 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Azotobacter culture has been investigated in the physiological state in which it fixed molecular nitrogen. A chemically defined medium was formulated that would support the growth ofAzotobacter vinelandii, but not the growth ofSaccharomyces cerevisiae in pure culture, unless a nitrogen source was added. The yeast culture was allowed to grow in mixed culture with the bacterium. Transient and steady-state populations of each organism in mixed culture at various dilution rates were enumerated with hemocytometer under a microscope. The difference in size of the organisms permitted easy resolution. The essential nutrilite, nitrogen, which is fixed by the bacteria and required by yeast caused the yeast to be dependent on the growth of the bacterium. At low dilution rates the yeast population reflected changes in the numbers ofAzotobacter. The numbers ofAzotobacter were identical in pure culture or in mixed culture; thus the interaction can be termed competitive commensalism. In batch culture, yeast had no effect on the rate of nitrogen fixation byAzotobacter. E. Coli ML-30 had a slight inhibitory effect whileC1. pasteurianum exhibited a stimulating effect. In continuous culture at low dilution rates, yeast was found to increase the rate of nitrogen fixation byAzotobacter vinelandii by 4.5%. Differential equations characterizing commensalism in the chemostat have been proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00942208
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  • 7
    Electronic Resource
    Electronic Resource
    Fibril formation from cellulose by a novel protein from Trichoderma reesei: A non-hydrolytic cellulolytic component? (1998)
    Springer
    World journal of microbiology and biotechnology 14 (1998), S. 551-558 
    Details
    ISSN: 1573-0972
    Keywords: Cellulose degradation ; Trichoderma reesei cellulase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A low molecular weight protein, named fibril-forming protein (FFP), was isolated from the culture supernatant of Avicel-grown Trichoderma reesei. The protein was purified to homogeneity and it exhibited a molecular weight of 11,400Da. Low amounts of this protein caused apparently non-hydrolytic disruption of filter paper, releasing fibrils without any detectable release of reducing sugars. It displayed no hydrolytic activity on carboxymethylcellulose (CMC), p-nitrophenyl-β-d-glucoside (pNPG) or 4-methylumbelliferyl cellobioside. The pH optimum of the protein was between 4 and 5. The temperature optimum was 40°C and the computed activation energy (Ea) for the filter paper disruption process was 4.18kcal/mol, suggesting disruption of non-covalent bonds. It had no immunological cross reactivity with reported cellulase components of T. reesei.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008888331936
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  • 8
    Electronic Resource
    Electronic Resource
    Analysis of the gibberellin-responsive promoter of a cathepsin B-like gene from wheat (1992)
    Springer
    Plant molecular biology 20 (1992), S. 849-856 
    Details
    ISSN: 1573-5028
    Keywords: GA regulation ; thiol-protease promoter ; wheat ; aleurone ; particle gun
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A wheat gene (A121) encoding a protein with sequence similarity to mammalian cathepsin B is regulated by gibberellic acid (GA) in aleurone layers of germinating grains. To analyse the mechanism of A121 regulation, its promoter was fused to the β-glucuronidase reporter gene (GUS) and introduced by micro-projectile bombardment into aleurone layers of oat. With 2.3 kb of promoter sequence, the GUS expression was enhanced by GA treatment. This effect was reversed by abscisic acid (ABA). This result showed for A121, like the α-amylase genes, that the regulation by GA and ABA was at the level of transcription. The GA responsiveness of the promoter was retained with as little as 276 bp of promoter sequence. Sequence comparison with a GA responsive promoter of an α-amylase gene identified the conserved element GCAACGGCAACGATGG which is required intact for full expression of both promoters. However, there was no identifiable similarity in the cathepsin-like promoter with the GA-responsive element of α-amylase promoters with the consensus sequence TAACAAA, suggesting that GA affects more than one mechanism of transcriptional control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027156
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  • 9
    Electronic Resource
    Electronic Resource
    Bioconversion of cellulose into ethanol by Clostridium thermocellum - product inhibition (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1109-1126 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Direct anaerobic bioconversion of cellulosic substances into ethanol by Clostridium thermocellum ATCC 27405 has been carried out at 60°C and pH 7.0 (initial for 100 L) under continuous sparging of oxygen free nitrogen in a culture vessel. Raw bagasse, mild alkali-treated bagasse, and solka floc were used as substrates. The extent of conversion of raw bagasse (cellulose, 50%; hemicellulose, 25%; lignin, 19%) was observed as 52% (w/w) and 79% (w/w) in the case of mild alkali and steam-treated bagasse (cellulose, 72%; hemicellulose, 11%; lignin, 12%), respectively. Use of bagasse concentration above 10 g/L showed a decreased rate in ethanol production. An inoculum age between 28-30 h and cell mass content of 0.027-0.036 g/L (dry basis) were used. The results obtained with raw and pretreated bagasse have been compared with those of highly pure Solka Floc (hemicellulose, 10%). Studies on the product inhibition indicated a linear fall of the percent of survivors with time. An Arrhenius type correlation between the cell decay rate constant and the product concentration was predicted. Even at low levels, the inhibitory effects of products on cell viability, the specific growth rate, and extracellular cellulase enzyme were observed.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250418
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  • 10
    Electronic Resource
    Electronic Resource
    Cellobiose hydrolysis using Pichia etchellsii cells immobilized in calcium alginate (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 340-346 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The rate of celluose degradation, limited due to the inhibition by cellobiose, can be increased by the hydrolysis of cellobiose to glucose using immobilized β-glucosidase. Production of β-glucosidase in four yeasts was studied and a maximum activity of 1.22 IU/mg cells was obtained in cells of Pichia etchellsii when grown on 3% cellobiose as the sole carbon source. A study of the immobilization of β-glucosidase containing cells of Pichia etchellsii on various solid supports was conducted and immobilization by entrapment in calcium alginate gel beads was found to be the most simple and efficient method. A retention of 96.5% of initial activity after ten sequential batch uses of the immobilized preparation was observed. The pH and temperature optima for free and immobilized cells were the same, i.e., 6.5 (0.05M Maleate buffer) and 50°C, respectively. Even though the temperature optimum was found to be 50°C, the enzyme exhibits a better thermal stability at 45°C. Beads stored at 4°C for six months retain 80% of their activity. Kinetic studies performed on free and immobilized cells shown that glucose is a noncompetitive product inhibitor.The immobilized preparation was found to be limited by pore diffusion but exhibited no film-diffusion resistance during packed bed column indicated by a low dispersion number of 0.1348. A model for reaction with pore diffusion for a noncompetitive type of inhibited system was developed and applied to the cellobiose hydrolysis system. The rate of reaction with diffusional limitations was determined by using the model and effectiveness factors were calculated for different particle sizes. An effectiveness factor of 0.49 was obtained for a particle diameter of 2.5 mm. The modified rate expression using the effectiveness factor represented batch and packed bed reactor operation satisfactorily. The productivity in the packed bed column was found to fall rapidly with increase in conversion rate indicating that the operating conditions of the column would have to be a compromise between high conversion rates and reasonable productivity. A half-life of over seven days was obtained at the operating temperature of 45°C in continuous operation of the packed bed reactor. However, the half-life in the column was found to be greatly affected by temperature, increasing to over seventeen days at a temperature of 40°C and decreasing to less than two days at 50°C.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260408
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