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1.
Molecules ; 27(19)2022 Sep 24.
Article in English | MEDLINE | ID: mdl-36234848

ABSTRACT

Lysozymes are hydrolytic enzymes characterized by their ability to cleave the ß-(1,4)-glycosidic bonds in peptidoglycan, a major structural component of the bacterial cell wall. This hydrolysis action compromises the integrity of the cell wall, causing the lysis of bacteria. For more than 80 years, its role of antibacterial defense in animals has been renowned, and it is also used as a preservative in foods and pharmaceuticals. In order to improve the antimicrobial efficacy of lysozyme, extensive research has been intended for its modifications. This manuscript reviews the natural antibiotic compound lysozyme with reference to its catalytic and non-catalytic mode of antibacterial action, lysozyme types, susceptibility and resistance of bacteria, modification of lysozyme molecules, and its applications in the food industry.


Subject(s)
Anti-Infective Agents , Muramidase , Animals , Anti-Bacterial Agents/pharmacology , Antiviral Agents , Bacteria/metabolism , Food Industry , Muramidase/chemistry , Peptidoglycan/metabolism , Pharmaceutical Preparations
2.
Environ Sci Pollut Res Int ; 29(3): 3510-3520, 2022 Jan.
Article in English | MEDLINE | ID: mdl-34389949

ABSTRACT

This study explores the chemotactic potential of Bacillus subtilis MB378 against industrial dyes. Initial screening with swim plate assay showed significant movement of Bacillus subtilis MB378 towards test compounds. According to quantitative capillary assay, B. subtilis MB378 exhibited high chemotaxis potential towards Acid Orange 52 (CI: 9.52), followed by Direct Red 28 (CI: 8.39) and Basic Green 4 (CI: 5.21) in glucose-supplemented medium. Sequencing and gene annotation results evidently showed presence of chemotaxis genes and flagellar motor proteins in Bacillus subtilis draft genome. Methyl-accepting proteins (involved in chemotaxis regulation) belonged to pfam00672, pfam00072, and pfam00015 protein families. Annotated chemotaxis machinery of MB378 comprised 8 Che genes, 5 chemoreceptor genes, associated flagellar proteins, and rotary motors. Chemotaxis genes of B. subtilis MB378 were compared with genes of closely related Bacillus strains (168, WK1, and HTA426), depicting highly conserved regions showing evolutionary relation between them. Considering results of present study, it can be speculated that test compounds triggered chemotactic genes, which made these compounds bioavailable to the bacterium. Hence, the bacterium recognized and approached these compounds and facilitated biodegradation and detoxification of these compounds.


Subject(s)
Bacillus subtilis , Chemotaxis , Water Decolorization , Bacillus subtilis/genetics , Bacterial Proteins/genetics , Membrane Proteins/genetics , Methyl-Accepting Chemotaxis Proteins/genetics , Multigene Family , Coloring Agents
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