Action mode of cuminaldehyde against Staphylococcus aureus and its application in sauced beef

The preservative potential of Octopus scraps peptides−Zinc chelate against Staphylococcus aureus: Its fabrication, antibacterial activity and action mode

Food Control ◽

10.1016/j.foodcont.2018.11.015 ◽

2019 ◽

Vol 98 ◽

pp. 24-33 ◽

Cited By ~ 14

Author(s):

Zheng Fang ◽

Liangzong Xu ◽

Yanlan Lin ◽

Xixi Cai ◽

Shaoyun Wang

Keyword(s):

Staphylococcus Aureus ◽

Antibacterial Activity ◽

Action Mode

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Synergistic Antibacterial Effect and Antibacterial Action Mode of Chitosan-Ferulic Acid Conjugate against Methicillin-Resistant Staphylococcus aureus

Journal of Microbiology and Biotechnology ◽

10.4014/jmb.1511.11046 ◽

2016 ◽

Vol 26 (4) ◽

pp. 784-789 ◽

Cited By ~ 18

Author(s):

Sung-Hwan Eom ◽

Shin-Kook Kang ◽

Dae-Sung Lee ◽

Jeong-In Myeong ◽

Jinhwan Lee ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Ferulic Acid ◽

Methicillin Resistant Staphylococcus Aureus ◽

Antibacterial Effect ◽

Antibacterial Action ◽

Methicillin Resistant ◽

Action Mode ◽

Acid Conjugate

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Action mode of bacteriocin BM1829 against Escherichia coli and Staphylococcus aureus

Food Bioscience ◽

10.1016/j.fbio.2020.100794 ◽

2020 ◽

pp. 100794

Author(s):

Hong Yan ◽

Yingying Lu ◽

Xin Li ◽

Yanglei Yi ◽

Xin Wang ◽

...

Keyword(s):

Escherichia Coli ◽

Staphylococcus Aureus ◽

Action Mode ◽

And Staphylococcus Aureus

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Action mode of cranberry anthocyanin on physiological and morphological properties of Staphylococcus aureus and its application in cooked meat

Food Microbiology ◽

10.1016/j.fm.2020.103632 ◽

2021 ◽

Vol 94 ◽

pp. 103632

Author(s):

Shaoying Gong ◽

Peng Fei ◽

Qi Sun ◽

Ling Guo ◽

Liange Jiang ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Morphological Properties ◽

Action Mode ◽

Cooked Meat

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Cytochemical Studies of Cell Wall Biosynthesis in Staphylococcus Aureus

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100094905 ◽

1972 ◽

Vol 30 ◽

pp. 328-329

Author(s):

Masaatsu Koike ◽

Koichi Nakashima ◽

Kyoko Iida

Keyword(s):

Staphylococcus Aureus ◽

Periodate Oxidation ◽

Early Time ◽

The Other ◽

Penicillin G ◽

Cell Wall Biosynthesis ◽

Septal Wall ◽

Peptidoglycan Biosynthesis ◽

Gram Positive Bacteria ◽

Cross Linkage

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).

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Gold labeling of teichoic acid on adjacent surfaces of staphylococcus aureus

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100160443 ◽

1990 ◽

Vol 48 (3) ◽

pp. 578-579

Author(s):

Margaret Hukee

Keyword(s):

Staphylococcus Aureus ◽

Teichoic Acid ◽

Protein Labeling ◽

Minimal Amount ◽

Section Thickness ◽

Double Labeling ◽

Parallel Surfaces ◽

Supporting Membrane

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.

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