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  1. Article ; Online: Inactivation of Staphylococcal Thermonuclease by an Enzyme-Like Factor Produced by Streptococcus faecalis subsp. liquefaciens.

    Medwid, Richard D / Grant, Dale W

    Journal of food protection

    2019  Volume 43, Issue 3, Page(s) 201–202

    Abstract: The thermonuclease of Staphylococcus aureus was inactivated during incubation with filtrates from cultures of Streptococcus faecalis subsp. liquefaciens . Of 53 isolates, 40 produced a thermonuclease-inactivating factor (TIF). The TIF was heat-labile, ... ...

    Abstract The thermonuclease of Staphylococcus aureus was inactivated during incubation with filtrates from cultures of Streptococcus faecalis subsp. liquefaciens . Of 53 isolates, 40 produced a thermonuclease-inactivating factor (TIF). The TIF was heat-labile, non-dialyzable and optimally active at 55 C and pH 7.0. These characteristics suggest TIF is a proteolytic enzyme. The common occurrence of TIF in cultures of S. faecalis subsp. liquefaciens may limit the value of the thermonuclease test for foods containing large populations of this organism.
    Language English
    Publishing date 2019-01-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 243284-5
    ISSN 1944-9097 ; 0362-028X
    ISSN (online) 1944-9097
    ISSN 0362-028X
    DOI 10.4315/0362-028X-43.3.201
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Evaluation of Escherichia coli cell disruption and inclusion body release using nucleic acid binding fluorochromes and flow cytometry.

    Medwid, Richard D / Krebs, Lara / Welch, Shellie

    BioTechniques

    2007  Volume 43, Issue 6, Page(s) 777–782

    Abstract: Many types of commercially valuable recombinant proteins produced by fermentation are expressed at high levels in Escherichia coli. Often, high-level expression in the host results in the formation of insoluble inclusion bodies. The release of these ... ...

    Abstract Many types of commercially valuable recombinant proteins produced by fermentation are expressed at high levels in Escherichia coli. Often, high-level expression in the host results in the formation of insoluble inclusion bodies. The release of these intracellular inclusion bodies from E. coli following cell disruption is a requirement for further downstream recovery. The ability to discern between intact unruptured cells and granules released from broken cells can provide valuable information for improving recovery yields in downstream purification. This paper describes a rapid and sensitive cytometry-based method that allows the simultaneous measurement of intact heat-killed E. coli and inclusion bodies using staining with nucleic acid binding fluorochromes.
    MeSH term(s) Escherichia coli/genetics ; Escherichia coli/metabolism ; Fermentation ; Flow Cytometry/methods ; Fluorescent Dyes ; Inclusion Bodies ; Molecular Biology/methods ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Solubility
    Chemical Substances Fluorescent Dyes ; Recombinant Proteins
    Language English
    Publishing date 2007-12
    Publishing country England
    Document type Journal Article ; Technical Report
    ZDB-ID 48453-2
    ISSN 1940-9818 ; 0736-6205
    ISSN (online) 1940-9818
    ISSN 0736-6205
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Inactivation of Staphylococcal Thermonuclease by an Enzyme-Like Factor Produced by Streptococcus faecalis subsp. liquefaciens

    Medwid, Richard D / Dale W. Grant

    Journal of food protection. 1980 Mar., v. 43, no. 3

    1980  

    Abstract: The thermonuclease of Staphylococcus aureus was inactivated during incubation with filtrates from cultures of Streptococcus faecalis subsp. liquefaciens. Of 53 isolates, 40 produced a thermonuclease-inactivating factor (TIF). The TIF was heat-labile, non- ...

    Abstract The thermonuclease of Staphylococcus aureus was inactivated during incubation with filtrates from cultures of Streptococcus faecalis subsp. liquefaciens. Of 53 isolates, 40 produced a thermonuclease-inactivating factor (TIF). The TIF was heat-labile, non-dialyzable and optimally active at 55 C and pH 7.0. These characteristics suggest TIF is a proteolytic enzyme. The common occurrence of TIF in cultures of S. faecalis subsp. liquefaciens may limit the value of the thermonuclease test for foods containing large populations of this organism.
    Keywords Enterococcus faecalis ; Staphylococcus aureus ; filtrates ; foods ; micrococcal nuclease ; pH ; proteinases
    Language English
    Dates of publication 1980-03
    Size p. 201-202.
    Publishing place International Association of Milk, Food, and Environmental Sanitarians.
    Document type Article
    ZDB-ID 243284-5
    ISSN 1944-9097 ; 0362-028X
    ISSN (online) 1944-9097
    ISSN 0362-028X
    DOI 10.4315/0362-028X-43.3.201
    Database NAL-Catalogue (AGRICOLA)

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