ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Thermostable α-galactosidase from Thermotoga neapolitana: cloning, sequencing and expression (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 163 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A gene encoding a thermostable α-galactosidase from the hyperthermophile Thermotoga neapolitana was cloned and sequenced. Sequence analysis showed that the 552-amino acid protein is similar to Escherichia coli Raf type α-galactosidase and belongs to Family 36 of the glycosyl hydrolases. Recombinant α-galactosidase expressed in E. coli has a molecular mass of ca. 61 kDa, and an optimum activity at 93°C at pH 7.0. The enzyme is highly thermostable and retains 75% of activity after heating to 80°C for 4 h. The potential application of the enzyme to high temperature processing of soy molasses has been demonstrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13023.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Expression of an endoglucanase gene of Pseudomonas fluorescens var. cellulosa in Zymomonas mobilis (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Using a broad host-range, mobilizable plasmid vector, the endoglucanase gene eglX from Pseudomonas fluorescens var. cellulosa was cloned and expressed in the bacterial ethanologen Zymomonas mobilis. The enzyme was intracellular in this new host. It was produced throughout the growth phase and was not repressed by glucose. We postulate that transcription of the eglX gene was initiated from a promoter of the vector in Z. mobilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02758.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Growth ofZymomonas on lactose: Gene cloning in combination with mutagenesis (1989)
    Springer
    Journal of industrial microbiology and biotechnology 4 (1989), S. 19-27 
    Details
    ISSN: 1476-5535
    Keywords: Zymomonas mobilis ; Growth on lactose ; Cloning ; Mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Wild-type strains ofZymomonas mobilis have a limited substrate range of glucose, fructose and sucrose. In order to expand this substrate range, transconjugants ofZ. mobilis containing Lac+ plasmids have been constructed. Although β-galactosidase is expressed in such strains, they lack the ability to grow on lactose. We now report the development ofZ. mobilis strains capable of growth on lactose. This was achieved in two stages. First, a broad host range plasmid was constructed (pRUT102) which contained the lactose operon under the control of aZ. mobilis promoter plus genes for galactose utilization.Z. mobilis CP4.45 containing pRUT102 was then subjected to mutagenesis combined with continued selection pressure for growth on lactose. One strain,Z. mobilis SB6, produced a turbid culture that yielded 0.25% ethanol from 5% lactose (plus 2% yeast extract) in 15 days.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569689
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cloning of an endoglucanase gene fromPseudomonas fluorescens var.cellulosa intoEscherichia coli andPseudomonas fluorescens (1986)
    Springer
    Journal of industrial microbiology and biotechnology 1 (1986), S. 79-86 
    Details
    ISSN: 1476-5535
    Keywords: Cloning ; Expression ; Endoglucanase ; Pseudomonas fluorescens ; Restriction mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An endoglucanase chromosomal gene from the cellulolyticPseudomonas fluorescens var.cellulosa (NCIB 10462) was cloned inEscherichia coli. Chromosomal DNA was partially digested with the restriction enzymeEcoRI and ligated into the broad host-range, mobilizable plasmid pSUP104 that had been linearized with the same enzyme. After transformation ofEscherichia coli, and endoglucanase-positive clone was detected in situ by use of the Congo-red assay procedure. The endoglucanase gene on the recombinant plasmid pRUCL 100 was expressed in the non-cellulolyticPseudomonas fluorescens PF41. The DNA fragment carrying the gene was transferred to the plasmid pBR322, generating plasmids pRUCL150 and pRUCL151, and its restriction map was derived.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569315
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Growth ofZymomonas mobilis CP4 on mannitol (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 275-281 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The ethanologenZymomonas mobilis has a restricted substrate range, namely glucose, fructose and sucrose. It would be useful to expand its substrate range to include other carbohydrates.Z. mobilis was screened for growth on 30 different carbohydrates and organic acids. A single spontaneous mutant,Z mobilis CP4.60, was isolated which illustrated feeble growth on mannitol as the sole carbohydrate source after three months of incubation. Growth ofZ. mobilis CP4.60 for several months in continuous culture with excess mannitol, and including a round of NTG (N-methyl-N'-nitro-N-nitrosoguanidine) mutagenesis in the chemostat, led to the isolation a sequential series of mutants (CP4.62, CP4.64 and CP4.66), each with improved growth rates on mannitol. Metabolism of mannitol byZ. mobilis is oxygen-dependent, resulting in limited production of ethanol and incresed production of lactic acid. This is an initial example of extension of the substrate range ofZymomonas. The conversion of mannitol to fructose could be via an altered alcohol dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00939321
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Cellobiose-quinone oxidoreductase —application in monitoring cellobiohydrolase purification (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 299-305 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The enzymatic saccharification of cellulose has traditionally been monitored via total reducing sugar analyses. Yet with cellobiohydrolase being a major component of fungal and actinomycete cellulases, there is a need for a more specific measurement of cellobiose besides other soluble cellulodextrin products without interference from glucose, the major product of cellulose saccharification. One approach is to utilize cellobiose: quinone oxidoreductase (CBOase) from the fungus Phanerochaete chrysosporium to monitor saccharification. We describe here methods for the production of CBQase and a specialized application to monitor the chromatographic separation of cellobiohydrolase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252934
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Growth ofZymomonas mobilis CP4 on mannitol (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 275-281 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The ethanologenZymomonas mobilis has a restricted substrate range, namely glucose, fructose and sucrose. It would be useful to expand its substrate range to include other carbohydrates.Z. mobilis was screened for growth on 30 different carbohydrates and organic acids. A single spontaneous mutant,Z mobilis CP4.60, was isolated which illustrated feeble growth on mannitol as the sole carbohydrate source after three months of incubation. Growth ofZ. mobilis CP4.60 for several months in continuous culture with excess mannitol, and including a round of NTG (N-methyl-N'-nitro-N-nitrosoguanidine) mutagenesis in the chemostat, led to the isolation a sequential series of mutants (CP4.62, CP4.64 and CP4.66), each with improved growth rates on mannitol. Metabolism of mannitol byZ. mobilis is oxygen-dependent, resulting in limited production of ethanol and incresed production of lactic acid. This is an initial example of extension of the substrate range ofZymomonas. The conversion of mannitol to fructose could be via an altered alcohol dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982916
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Purification and some properties of extracellular invertase B from Zymomonas mobilis (1992)
    Springer
    Applied microbiology and biotechnology 38 (1992), S. 341-346 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Zymomonas mobilis is a Gram-negative ethanologen that can ferment glucose, fructose, and sucrose. Three enzymes that hydrolyze sucrose were found in a zymogram of electrophoretically separated proteins of Z. mobilis CP4. Two were invertase,, Inv A and Inv B; the latter was studied. Inv B is extracellular and accounts for at least 60% of the saccharolytic activity found in the culture broth of Z. mobilis CP4. The enzyme was purified 51-fold in 17% yield from culture broth of Z. mobilis grown on sucrose. It is a β-fructosidase, monomeric with a molecular mass of 47 kDa and pI of 4.3. Its K m for sucrose is 86 mm, and it has high catalytic activity (V max = 1800 μmol product/min per milligram protein). The purification and some properties of Inv B are presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170083
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Transformation of Zymononas mobilis by electroporation (1993)
    Springer
    Applied microbiology and biotechnology 39 (1993), S. 305-308 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Zymomonas mobilis is being considered for the industrial production of ethyl alcohol. Expansion of its substrate range of glucose, fructose and sucrose could be advantageous, but genetic manipulation of Z. mobilis is restricted as it is resistant to transformation. We present a protocol using electroporation for high efficiency transformation of this bacterium. Optimal parameters included cooled cells (0–4° C), use of 10% glycerol as an osmotic support medium, a pulse in the 12 kV/cm range for 10 ms and outgrowth on GYx medium prior to selection. The routine efficiency achieved was greater than 1.0 × 107/μg DNA, a major increase over other transformation methods in which yields ranged from 100–2000/μg DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00192083
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Antibiotic disks - an improvement in the filter paper assay for cellulaseJournal paper of the New Jersey Agricultural Experiment Station, Rutgers, The State University of New Jersey, New Brunswick, N.J. 08903 (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 297-300 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260200213
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...