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  • 1
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 653-654 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: In the title compound, [Pt(C3H2O4)(C7H16N2O2)], the Pt atom is coordinated to two O and two N atoms in a square-planar arrangement. The two independent molecules, which have very similar structures, are approximately related by pseudo-twofold screw-axis symmetry. The six-membered chelate ring in the leaving ligand assumes a conformation intermediate between the half-chair and boat forms. The seven-membered ring in the carrier ligand assumes a twist-chair conformation and the oxolane ring assumes an envelope conformation. The crystal packing consists of extensive hydrogen-bonding networks which form two-dimensional molecular layers, and there are weak van der Waals interactions between these layers.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 948-956 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of aspergillopepsin I (AP) from Aspergillus phoenicis has been determined at 2.18 Å resolution and refined to R and Rfree factors of 21.5 and 26.0%, respectively. AP has the typical two β-barrel domain structure of aspartic proteinases. The structures of the two independent molecules are partly different, exemplifying the flexible nature of the aspartic proteinase structure. Notably, the `flap' in one molecule is closer, with a largest separation of 4.0 Å, to the active site than in the other molecule. AP is most structurally homologous to penicillopepsin (PP) and then to endothiapepsin (EP), which share sequence identities of 68 and 56%, respectively. However, AP is similar to EP but differs from PP in the combined S1′–S2 subsite that is delineated by a flexible ψ-loop in the C-terminal domain. The S1′ and S2 subsites are well defined and small in AP, while there is no definite border between S1′ and S2 and the open space for the S2 subsite is larger in PP. Comparison of the structures indicates that the two amino-acid residues equivalent to Leu295 and Leu297 of AP are the major determining factors in shaping the S1′–S2 subsite in the fungal aspartic proteinases.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 775-777 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Dihydrofolate reductase (DHFR) from bacteriophage T4 is a homodimer consisting of 193-residue subunits. It has been crystallized in the presence of the cofactor (NADPH) and an inhibitor (aminopterin) at 296 K using sodium chloride as precipitant. The crystals are tetragonal, belonging to the space group P4122 (or P4322), with unit-cell parameters a = b = 61.14, c = 123.23 Å under cryogenic conditions. The asymmetric unit contains a single subunit, with a corresponding Vm of 2.65 Å3 Da−1 and a solvent content of 53.6%. Native data have been collected from a crystal to 1.9 Å resolution using synchrotron X-rays.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Quantitative analysis of mixtures of free fatty acids, monoacyl-, diacyl-, and triacylglycerols by a simple and rapid gas chromatography method has been developed. The analysis was carried out on a short capillary column without derivatization. When the triacontane was used as an internal standard, we obtained relative response factors for each lipid class with reproducibility and accuracy. This method could be applied for not only compositional analysis of fats and oils but also monitoring lipase reactions.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 204-210 
    ISSN: 0006-3592
    Keywords: immobilization ; interesterification ; cocoa butter equivalent ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In order to investigate quantitatively the interesterification reaction, triolein and stearic acid were used as substrates and eight commercially available lipases were tested for their suitability for the reaction. Three fungal lipase preparations were found to be suitable. The hydrolytic activity of the commercial lipases was tested with olive oil, and it 2was noted that there was no correlation between their hydrolytic and interesterification activities. Among the lipases tested, Mucor miehei lipase was chosen for further study because of it high protein content and its relatively high hydrolytic and interesterification activities, both of which are required for effective interesterification. The effect of water activity of the interesterification reaction was investigated. interesterification activity was shown to be maximum at the water activity of 0.25. As the water activity of the lipase increased, hydrolysis of triglyceride was accelerated. At zero water activity, high conversion was achieved, although interesterification activity was relatively lower than that at the water activity of 0.25. A new and simple immobilization method was developed in order to render hydrophobicity to the lipase and hence to improve the interesterification activity of the lipase. The lipase was immobilized covalently with glutaraldehyde or with six alkyl chains as spacers onto Florisil (magnesium silicate, a inorganic matrix). Interesterification activity of the immobilized lipase with the hydrophobic spacers were increased against that of re lipase. The increase of activity was up to 8-fold that of the original activity of free lipase when the spacer was 7-aminoheptanoic acids. Relatively high stability of the immobilized lipase was shown in a continuous packed bed column reactor with a half-life of 97 days. © 1993 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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