Evaluation of the Antimicrobial Activity of Natural Animal Proteins/Peptides In Vitro
Evaluation of the Antimicrobial Activity of Natural Animal Proteins/Peptides In Vitro
dc.contributor.author | Greiner, L. | |
dc.contributor.author | Stahly, T. | |
dc.contributor.author | Stanton, T. | |
dc.date | 2018-02-12T23:57:33.000 | |
dc.date.accessioned | 2020-07-02T07:01:01Z | |
dc.date.available | 2020-07-02T07:01:01Z | |
dc.date.copyright | Mon Jan 01 00:00:00 UTC 2001 | |
dc.date.embargo | 2012-08-13 | |
dc.date.issued | 2001-01-01 | |
dc.description.abstract | <p>The objectives of this research were to validate the sensitivity and precision of an <em>in vitro</em> assay for evaluating the efficacy of antimicrobials, to evaluate the ability of natural animal proteins/peptides to kill <em>in vitro</em> antibiotic-resistant, as well as, -susceptible bacteria, and to determine the effects of key components of animal digesta (e.g., pH, mineral content, and proteolytic digestive enzymes) on the estimated antimicrobial activity of these proteins/peptides.</p> <p>The minimum inhibitory concentrations (MIC) for polymyxin B (control antibiotic) were determined to be .76, .76, and .90 µg/mL for <em>Escherichia coli</em>, <em>Escherichia coli</em> (nalidixic acid-resistant), and <em>Staphylococcus aureus</em>, respectively. The intra- and inter-assay variation for MIC determination was .18 and .2%, respectively.</p> <p>The natural animal proteins and peptides (lactoferrin, lactoferricin B, hen egg lysozyme, and alpha-lactalbumin LDT2) were determined in<em> in vitro</em> (acetic acid medium) to kill selected bacteria. Each of the tested proteins/peptides was active against an antibiotic-resistant (nalidixic acid) strain of <em>E. coli</em>; however, the required concentrations for antimicrobial activity were 10 to 15 times higher than that of the nonantibiotic-resistant strain. The antimicrobial activity of each protein/peptide in animal digesta fluid was 130 to 300% greater than that in the acetic acid media. Overall, the intra- and inter-assay variation values for the tested proteins/peptides was 3 and 3.4%, respectively.</p> <p>The antimicrobial activity of two of the three proteins/peptides was not affected by the presence of cationic minerals. The change in pH (digesta fluid and acetic acid media) from 7 to 2 resulted in a loss of antimicrobial activity of 33% for all proteins/peptides. Therefore, the increase in antimicrobial activity associated with the digesta fluid is not related to change in H or the mineral concentration of the digesta. Based on these data, natural proteins/peptides represent potential antibiotic substitutes.</p> | |
dc.format.mimetype | application/pdf | |
dc.identifier | archive/lib.dr.iastate.edu/swinereports_2000/1/ | |
dc.identifier.articleid | 1014 | |
dc.identifier.contextkey | 3209911 | |
dc.identifier.s3bucket | isulib-bepress-aws-west | |
dc.identifier.submissionpath | swinereports_2000/1 | |
dc.identifier.uri | https://dr.lib.iastate.edu/handle/20.500.12876/91229 | |
dc.language.iso | en | |
dc.relation.ispartofseries | Animal Science Research Reports | |
dc.relation.ispartofseries | ASL R658 | |
dc.source.bitstream | archive/lib.dr.iastate.edu/swinereports_2000/1/asl_658.pdf|||Fri Jan 14 17:27:50 UTC 2022 | |
dc.subject.disciplines | Agriculture | |
dc.subject.disciplines | Animal Sciences | |
dc.subject.keywords | ASL R658 | |
dc.title | Evaluation of the Antimicrobial Activity of Natural Animal Proteins/Peptides In Vitro | |
dc.type | article | |
dc.type.genre | nutrition | |
dspace.entity.type | Publication | |
relation.isSeriesOfPublication | 7f3839b7-b833-4418-a6fa-adda2b23950a |
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