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Increased production of bacST4SA by Enterococcus mundtii in an industrial-based medium with pH-control /Coetzee, Johannes Cornelius Jacobus January 2007 (has links)
Thesis (MScIng)--University of Stellenbosch, 2007. / Bibliography. Also available via the Internet.
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Examining the structure, function and mode of action of bacteriocins from lactic acid bacteriaMartin-Visscher, Leah Alina. January 2010 (has links)
Thesis (Ph. D.)--University of Alberta, 2010. / Title from pdf file main screen (viewed on June 18, 2010). A thesis submitted to the Faculty of Graduate Studies and Research in partial fulfillment of the requirements for the degree of Doctor of Philosophy, Department of Chemistry, University of Alberta. Includes bibliographical references.
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The role of lactic acid bacteria in fermented sausagesErickson, Raymond Curry, January 1960 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1960. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
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Volatile acid production of "S̲. l̲a̲c̲t̲i̲c̲u̲s̲" and the organisms associated with it in starters ...Hammer, Bernard Wernick, January 1900 (has links)
Thesis (Ph. D.)--University of Chicago, 1920. / "Private edition, distributed by the University of Chicago libraries, Chicago, Illinois." "Reprinted from Iowa state college of agriculture and mechanic arts, Research bulletin, nos. 63 and 65, October, 1920, and November, 1920." Bibliography: p. 96b-96c, 128. Also available on the Internet.
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A study on the metabolism of the lactic acid bacteriaWood, Alexander James January 1938 (has links)
[No abstract available] / Land and Food Systems, Faculty of / Graduate
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The nature of the activators required by the lactic acid bacteriaKadzielawa, Arthur Stephen January 1939 (has links)
[No abstract available] / Land and Food Systems, Faculty of / Graduate
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Studies on the respiratory enzymes of the lactic acid and nitrogen-fixing bacteriaMorgan, Joseph Francis January 1942 (has links)
[No abstract submitted] / Land and Food Systems, Faculty of / Graduate
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Media for the lactic acid group of microorganisms.Perry, Helen Margaret. January 1924 (has links)
No description available.
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Heat resistance and inactivation of meat spoilage lactic acid bacteria.Franz, Charles Marie Antoine Paul January 1993 (has links)
I declare that this is my own, unaided work. It is being
submitted for the degree of Master of Science in the
University of the Witwatersrand, Johannesburg. It has not
been submitted before for any degree or examination in any
other University. / Heat resistance and inactivation of processed meat spoilage
lactic acid bacteria was investigated in vitro and by
in-package pasteurization of South African vacuum-packaged
vienna sausages. In vitro heat resistance of four lactic
acid bacteria strains was low, since reductions of at least
one log cycle in bacterial numbers occurred upon heating at
57, 60 and 63°C in quarter-strength Ringers solution for
one minute. In vitro heat resistance data were used to
calculate three in-package pasteurization treatments of
increasing severity for vacuum-packaged vienna sausages.
Depending on treatment, pasteurization in a water cooker at
67°C increased microbiological shelf life of sausages
10, 14 and 17 times that of control samples, during storage
at 8'C. Although in-package pasteurization successfully
decreased growth of spoilage lactic acid bacteria and
increased product shelf life fit did not entirely prevent
spoilage by pediococci. Since pasteurization also promoted
growth of potentially pathogenic Bacillus and Clostridium,
safety of pasteurized vacuum-packaged vienna sausages was
compromised. / Andrew Chakane 2018
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Cloning, expression, and characterization of lactic acid bacteria recombinant prolidasesYang, Soo In 23 April 2007
<i>Lactobacillus plantarum</i> (<i>Lb. plantarum</i>) NRRL B4496 and <i>Lactococcus lactis</i> (<i>Lc. lactis</i>) NRRL B1821 prolidase genes were isolated, cloned, and sequenced. The sequence-confirmed genes were subcloned into the expression systems. The recombinant prolidases from the pKK223-3 systems were purified through ammonium sulphate precipitation and anion-exchange column chromatography. Recombinant <i>Lb. plantarum prolidase</i>, however, demonstrated a loss of activity during the purification. The following characterization work was performed on purified recombinant <i>Lc. lactis prolidase</i>. <p>The mass spectroscopic result and the molecular modelling suggested a 80 kDa homodimer with two metal cations at the catalytic centre of the prolidase. The optimum temperature was 50 ºC and showed more than 50% activities between 40 and 55 ºC. The enzyme was most stable at 30 ºC and withstood 20 min of heat-treatment up to 60 ºC, however, lost activity over 70 ºC. Circular dichroism indicated a denaturation temperature of 67 ºC. The optimum pH was 6.5 for hydrolyzing Leu-Pro and the enzyme did not display any activity below pH 5.5 nor above pH 7 with this peptide. However, Phe-Pro was hydrolyzed the fastest at pH 7 and Arg-Pro had a maximum rate at pH 9. This metallopeptidase exhibited a broad range of metal cation preference, hydrolyzing Leu-Pro with Mn++, Co++, Zn++, Ca++, and Mg++. Further kinetic analysis showed unusual allostery of the enzyme (Hill coefficient: 1.3). The unique substrate intakes onGlu-Pro and tripeptides were observed while Val-Pro was not hydrolyzed. The molecular modelling of this prolidase suggested a difference in the substrate specificity resulting from a loop structure, L33 to R40, near the substrate binding site.
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