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  • 1
    Electronic Resource
    Electronic Resource
    Sialylated endogenous glycoconjugates in plant cells (2003)
    [s.l.] : Nature Publishing Group
    Nature biotechnology 21 (2003), S. 1470-1471 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Bioengineered plants are emerging as promising systems for the production of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt912
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and characterization of the recombinant alginate lyase from Pseudomonas sp. leaked by Escherichia coli upon addition of glycine (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The plasmid pAL205 encodes an alginate lyase gene of Pseudomonas sp. OS-ALG-9, fused in frame to the β-galactosidase α-peptide gene. The alginate lyase (Aly) expressed in Escherichia coli (pAL205) was significantly secreted into the medium by the addition of glycine. The extracellular enzyme isolated from the culture of E. coli JM109 (pAL205) was purified over 15 000-fold by successive chromatography and subjected to amino acid sequence analysis. The sequence determined was identical to that of the intracellular protein. Since the activity and molecular size of the extracellular Aly is identical to the intracellular protein and to the Aly isolated from Pseudomonas, the glycine does not affect or modify the Aly during its leakage into the medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07384.x
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  • 3
    Electronic Resource
    Electronic Resource
    High gene expression in Escherichia coli of recombinant alginate lyase as a fused protein with β-galactosidase α-peptide (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Escherichia coli LE392 (pAL28) was previously isolated as a positive clone harboring the alginate lyase gene (aly) from an alginate-degrading strain, Pseudomonas sp. OS-ALG-9. The plasmid pAL205, one of the constructs obtained after successive subcloning of pAL28, gave the highest expression of aly in E. coli cells. A 8-fold increase in the alginate lyase (Aly) activity in E. coli JM109 (pAL205) was induced with isopropyl-β-d-thiogalactoside, which was 210 times higher than that in E. coli LE392 (pAL28). The highly significant increase in the expression of the Aly enzyme with pAL205 was investigated through the nucleotide sequence around the 5′ region of aly as well as the N-terminal sequence of the purified enzyme. It was found that the Aly expressed in E. coli (pAL205) was a fused protein containing 7 residues from the N-terminus of β-galactosidase α-peptide and the mature protein found in the Pseudomonas sp. except for three residues in the N-terminal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07383.x
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  • 4
    Electronic Resource
    Electronic Resource
    The nylon oligomer biodegradation system ofFlavobacterium andPseudomonas (1994)
    Springer
    Biodegradation 5 (1994), S. 185-194 
    Details
    ISSN: 1572-9729
    Keywords: 6-aminohexanoate-oligomer ; degradative plasmid pOAD2 ; enzyme evolution ; hybrid enzyme ; nylon oligomer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract This review article is a compendium of the available information on the degradation of a man-made compound, 6-aminohexanoate-oligomer, inFlavobacterium andPseudomonas strains, and discusses the molecular basis for adaptation of microorganisms toward these xenobiotic compounds. Three plasmid-encoded enzymes, 6-aminohexanoate-cyclic-dimer hydrolase (EI), 6-aminohexanoate-dimer hydrolase (EII), and endo-type 6-aminohexanoate-oligomer hydrolase (EIII) are responsible for the degradation of the oligomers. Two repeated sequences, designated RS-I and RS-II, are found on plasmid pOAD2, which is involved in 6-aminohexanoate degradation inFlavobacterium. RS-I appears 5 times on the pOAD2, and all copies have the same sequences as insertion sequence IS6100. RS-II appears twice on the plasmid. RS-IIA contains the gene encoding EII, while RS-IIB contains the gene for the analogous EII' protein. Both EII and EII' are polypeptides of 392 amino acids, which differ by 46 amino acid residues. The specific activity of the EII enzyme is 200-fold higher than that of EII'. Construction of various hybrid genes demonstrated that only the combination of two amino acid residues in the EII' enzyme can enhance the activity of the EII' to the same level as that of EII enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00696459
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  • 5
    Electronic Resource
    Electronic Resource
    On-line monitoring of cell concentration of Perilla frutescens in a bioreactorThis article was presented at the symposium Horizons of Biotechnology and Bioengineering, 25th Autumn Meeting of the Society of Chemical Engineers (Japan), Tokyo, November 30 to October 2, 1992. (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 542-546 
    Details
    ISSN: 0006-3592
    Keywords: on-line monitoring ; perilla frutescens ; cell concentration ; plant cell culture ; bioreactor cultivation ; turbidimetric measurement ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article demonstrates the successful in situ real-time monitoring of the cell concentration of Perilla frutescens in a bioreactor by using a laser turbidimeter. It was found that turbidity measurements at 780 nm with the laser sensor were hardly affected by the red color of the anthocyanin produced by P. frutescens cells, nor by the aeration rate or agitation speed within the ranges investigated. There was an excellent linear relationship, with a correlation coefficient (r2) higher than 0.99, between the sensor's response and the cell concentration. The whole growth stage of the cells, i.e., lag, logarithmic, and stationary phases, in bioreactor cultivations, could be satisfactorily estimated on-line by means of the in situ turbidimeter. However, during the declining phase of the cells, an apparent deviation was observed between the on-line estimations and off-line measurements of cell concentrations by dry cell weight, while the wet cell weight could be estimated by the same turbidimeter system. We found that this deviation was caused by a decrease in the cell density due to an increase of the individual cell volume and a decrease of the cell dry weight during the declining phase. © 1993 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420420
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  • 6
    Electronic Resource
    Electronic Resource
    A quantitative analysis of shear effects on cell suspension and cell culture of perilla frutescens in bioreactors (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 649-654 
    Details
    ISSN: 0006-3592
    Keywords: anthocyanin production ; bioreactor cultivation ; Perilla frutescens ; plant cell culture ; shear effects ; metabolism ; secondary ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The short-time effects of shear on suspended cells of Perilla frutescens were quantitatively analyzed by exposing the cells to a well-defined flow field in a rotating drum reactor. It was found that both shear rate and shearing time significantly affected cell viability. The quantitative effects of shear on cell growth and the production of anthocyanin, a secondary metabolite, by the cell cultures were further investigated in a series of batch cultivations using a 5-L plant cell bioreactor with a marine impeller. The results indicated that there was an optimum range of shear rate; i.e., an average shear rate of 20 to 30 s-1 or an impeller tip speed of 5 to 8 dm/s, which maximized all the values of the following parameters: the specific growth rate, the maximum cell concentration, the (specific) production and productivity of anthocyanin, and the cell and anthocyanin yields. © 1994 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260440512
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