A survey of elastase-producing bacteria and characteristics of the most potent producer, Priestia megaterium gasm32

Ninety-one elastase-producing bacterial isolates were recovered from different localities of the Eastern Province of Saudi Arabia. Elastase from the best isolate Priestia megaterium gasm32, from luncheon samples was purified to electrophoretic homogeneity using DEAE-Sepharose CL-6B and Sephadex G-10...

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Bibliographic Details
Published in:PloS one 2023-03, Vol.18 (3), p.e0282963-e0282963
Main Authors: AlShaikh-Mubarak, Ghadah A, Kotb, Essam, Alabdalall, Amira H, Aldayel, Munirah F
Format: Article
Language:English
Subjects:
Analysis
Antibacterial activity
Bacteria
Bacteria - metabolism
Biology and Life Sciences
Calcium ions
Care and treatment
Chromatography
Copper
Damage
Diagnosis
Elastase
Elastin
Elastin - metabolism
Electrophoresis
Enzymatic activity
Enzymes
Ethylenediaminetetraacetic acid
Ethylenediaminetetraacetic acids
Fibers
Heat treatment
Homogeneity
Hydrogen-Ion Concentration
Infectious skin diseases
Ions
Medicine and Health Sciences
Metalloproteinase
Methods
Milk
Pancreatic Elastase - metabolism
Photomicrographs
Phylogenetics
Potassium
Priestia megaterium
Productivity
Proteins
Saudi Arabia
Skin
Substrates
Yeast
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Summary:Ninety-one elastase-producing bacterial isolates were recovered from different localities of the Eastern Province of Saudi Arabia. Elastase from the best isolate Priestia megaterium gasm32, from luncheon samples was purified to electrophoretic homogeneity using DEAE-Sepharose CL-6B and Sephadex G-100 chromatographic techniques. The recovery was 17.7%, the purification fold was 11.7x, and the molecular mass was 30 kDa. Enzymatic activity was highly repressed by Ba2+ and almost completely lost by EDTA, but it was greatly stimulated by Cu2+ ions, suggesting a metalloprotease type. The enzyme was stable at 45°C and pH 6.0-10.0 for 2 hours. Ca2+ ions considerably enhanced the stability of the heat-treated enzyme. The Vmax and Km against the synthetic substrate elastin-Congo red were 6.03 mg/mL, and 8.82 U/mg, respectively. Interestingly, the enzyme showed potent antibacterial activity against many bacterial pathogens. Under SEM, most bacterial cells showed loss of integrity, damage, and perforation. SEM micrographs also showed a time-dependent gradual breakdown of elastin fibers exposed to elastase. After 3 hours, intact elastin fibers disappeared, leaving irregular pieces. Given these good features, this elastase may be a promising candidate for treating damaged skin fibers with the inhibition of contaminating bacteria.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0282963