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  • 1
    Electronic Resource
    Electronic Resource
    Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1138-1140 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The enzyme 6-phospho-3-hexulose isomerase (YckF) from Bacillus subtilis has been prepared and crystallized in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop method at 291 K using polyethylene glycol 2000 monomethylether as precipitant. They diffract beyond 1.7 Å using an in-house Cu Kα source and belong to either space group P6522 or P6122, with unit-cell parameters a = b = 72.4, c = 241.2 Å, and have two molecules of YckF in the asymmetric unit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744490100748X
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1141-1143 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Biological recycling of plant material is essential for biosphere maintenance. This perpetual task involves a complex array of enzymes, including extracellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known about the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P21, with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Å, β = 92.0°, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Å using synchrotron radiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901007491
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Evidence that the Piromyces gene family encoding endo-l,4-mannanases arose through gene duplication (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 141 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The sequences of two Piromyces cDNAs (manB and manC) encoding functional mannanases, defined as mannanase B (MANB) and mannanase C (MANC), revealed that both the cDNAs, and the encoded enzymes, exhibited extensive sequence identity with each other and with a previously described Piromyces mannanase. MANB and MANC, which belong to glycosyl hydrolase family 26, hydrolyse several forms of mannan but do not attack the other major plant structural polysaccharides. The data presented in this paper indicate that the Piromyces gene family encoding mannanases arose through gene duplication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08382.x
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  • 4
    Electronic Resource
    Electronic Resource
    Cellulases and hemicellulases of the anaerobic fungus Piromyces constitute a multiprotein cellulose-binding complex and are encoded by multigene families (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 125 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract More than 80% of the extracellular Avicelase, endoglucanase, xylanase and mannanase activities of the anaerobic fungus Piromyces were associated with a cellulose-binding complex. The complex was composed of at least 10 polypeptides ranging in size from 190 kDa to 50 kDa, and contained numerous endoglucanases, xylanases and mannanases. Multiple genes encoding each of these activities were isolated from an expressing cDNA library.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07329.x
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Immobilization of Rhodococcus AJ270 and Useof Entrapped Biocatalyst for the Productionof Acrylic Acid (2000)
    Springer
    Monatshefte für Chemie 131 (2000), S. 655-666 
    Details
    ISSN: 1434-4475
    Keywords: Keywords. Acrylamide; Amidase; Acrylate; Biocatalysis; Rhodococcus.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary.  Rhodococcus AJ270 is adsorbed by Dowex 1 at 15.4  mg dry weight per g resin with maximum amidase specific activity observed at lower loadings. Bacteria form a monolayer on the resin surface, and adsorption is complete within 2 min. AJ270 can be entrapped in agar and agarose gels (optimum loading: 20 mg dry weight bacteria per cm3 gel). Adsorption and entrapment improve amidase thermal stability 3–4 fold, and entrapment shifts the pH optimum from 8 to 7. Adsorbed and free bacteria show similar values for K m and V max, but entrapped bacteria have higher K m values. Compared with bacteria adsorbed to Dowex, the activity per cm3 of matrix of agar-entrapped AJ270 is eight-fold higher. In stirred-tank reactors, exposure to acrylic acid reduces the amidase activity of the biocatalyst in the hydrolysis of acrylamide. In column reactors, entrapped AJ270 suffers little reduction in amidase activity against 0.25 M acrylamide over 22 h continuous operation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007060070094
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Polymer hydrolysis in a cold climate (1999)
    Springer
    Extremophiles 3 (1999), S. 81-87 
    Details
    ISSN: 1433-4909
    Keywords: Key words Psychrophilic bacteria ; Enzymes ; Plant cell wall hydrolysis ; β-Glycanases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this review we discuss the activity of an ecologically significant group of psychrophilic bacteria, which are involved in the hydrolysis of plant cell wall polymers. Until now these organisms have been largely overlooked, despite the key role they play in releasing organic carbon fixed by primary producers in permanently cold environments such as Antarctica. This review details a specific group of plant cell wall polymer-degrading enzymes known as β-glycanases. Studies on "cold" enzymes in general are in their infancy, but it has been shown that many exhibit structural and functional modifications that enable them to function at low temperature. β-Glycanases in particular are intriguing because their substrates (cellulose and xylan) are very refractile, which may indicate that their "cold" modifications are pronounced. In addition, mesophilic β-glycanases have been extensively studied and the current state of our knowledge is reviewed. This body of information can be exploited to enable meaningful comparative studies between mesophilic and psychrophilic β-glycanases. The aim of such investigations is to obtain a deeper insight into those structural and functional modifications that enable these enzymes to function at low temperature and to examine the evolutionary relationship between mesophilic and psychrophilic β-glycanases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050102
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    Paper (German National Licenses)
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