Production, Partial Purification, and Biochemical Characterization of a Thermotolerant Alkaline Metallo-protease from Staphylococcus sciuri

Abu-Khudir, Rasha; Salem, Maha M.; Allam, Nanis G.; Ali, Ehab M.M.

doi:10.1007/s12010-019-02983-6

Cited by 15 publications

(4 citation statements)

References 41 publications

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“…Similarly, an alkaline metalloprotease was isolated from the Bacillus alkaliterlluris TWI3, where the Ca +2 , Mn +2 and Mg +2 increased the activity of metalloprotease while Hg +2 , Cu +2 , Zn +2 and Fe +2 inhibited enzyme activity (Anandharaj et al 2016b, Yilmaz et al 2016. The metalloprotease from the TS2 has optimum activity at pH of 10 and at 80 °C, which was also quite similar with previous findings where the alkaline protease showed maximum activity at high temperature and pH (Abu-Khudir et al 2019, Yang et al 2020.…”

Section: Discussionsupporting

confidence: 87%

Characterization of alkaline metalloprotease isolated from halophilic bacterium Bacillus cereus and its applications in various industrial processes

SAEED,

RIAZ,

ADIL

et al. 2023

An. Acad. Bras. Ciênc.

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Microbial proteases are one of the most demanding enzymes for various industries with diverse applications in food, pharmaceutics, and textile industries to name the few. An extracellular alkaline metalloprotease was produced and purified from moderate halophilic bacterial strain, Bacillus cereus TS2, with some unique characteristics required for various industrial applications. The protease was produced in basal medium supplemented with casein and was partially purified by ion exchange chromatography followed by ammonium sulphate precipitation. The alkaline metalloprotease has molecular weight of 35 kDa with specific activity of 535.4 µM/min/ mg. It can work at wide range of pH from 3 to 12, while showing optimum activity at pH 10. Similarly, the alkaline metalloprotease is stable till the temperature of 80 °C and works at wide range of temperature from 20 to 90 °C with optimum activity at 60 °C.The turnover rate increases in the presence of NaCl and Co +2 with k cat /K M of 1.42 × 10 3 and 1.27 × 10 3 s -1 .M -1 respectively, while without NaCl and Co +2 it has a value of 7.58× 10 2 .The alkaline metalloprotease was relatively resistant to thermal and solvent mediated denaturation. Applications revealed that the metalloprotease was efficient to remove hair from goat skin, remove blood stains and degrade milk, thus can be a potential candidate for leather, detergent, and food industry.

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Section: Discussionsupporting

confidence: 87%

Characterization of alkaline metalloprotease isolated from halophilic bacterium Bacillus cereus and its applications in various industrial processes

SAEED,

RIAZ,

ADIL

et al. 2023

An. Acad. Bras. Ciênc.

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“…The fractions containing high protein content were pooled and assayed for ADA enzyme activity. Finally, the fractions enriched with ADA activity were pooled for kinetics measurements (Mohamed 2006 ; Abu-Khudir et al 2019 ).…”

Section: Methodsmentioning

confidence: 99%

Quercetin mitigates rheumatoid arthritis by inhibiting adenosine deaminase in rats

El-Said

Atta

Mobasher

et al. 2022

Mol Med

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Rheumatoid arthritis (RA) is a chronic inflammatory joint disease characterized by synovial proliferation and bone destruction. Adenosine deaminase (ADA) is a key inflammatory enzyme that increases joint stiffness and pain in RA. In this study, we evaluated the in-silico, and in vivo inhibitory effect of quercetin isolated from Egyptian Fenugreek on ADA enzyme activity. We also determined the combinatorial effect of quercetin on methotrexate mediated anti-inflammatory efficacy and toxicity. In-silico molecular docking was conducted and confirmed in an in vivo RA rat model. The results showed that the inhibition constant of quercetin on joint ADA by docking and in-vitro was 61.9 and 55.5 mM, respectively. Therefore, quercetin exhibits anti-inflammatory effect in a rat RA model as evidenced by reducing the specific activity of ADA in joint tissues, lower jaw volume, enhance body weight, downregulate ADA gene expression, reduce levels of RA cytokines interleukin-1β, interleukin-6, tumor necrosis factor-α, also, rheumatoid factor, C-reactive protein, and anti-cyclic citrullinated peptide RA biomarker levels. These findings demonstrate that the purified quercetin has a promising anti-inflammatory effect against RA disease through its inhibitory effects on the ADA enzyme. Furthermore, isolated quercetin improved the anti-inflammatory efficacy of methotrexate, reduced its toxic effects by increasing antioxidant enzymes and reducing oxidative stress.

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“…Ibrahim et al (2019) reported that in presence of SDS, the activity of the alkaline protease was completely inhibited. Khudir et al (2019) reported that the thermotolerant alkaline protease from Staphylococcus sciuri secures 126.6% of its activity in presence of 0.1% SDS.…”

Section: Effect Of Additives On Protease Activitymentioning

confidence: 99%

Screening, characterization, and kinetic studies of a serine alkaline protease from kitchen wastewater bacteria P2S1An and evaluation of its application in nutraceutical production

Das

Ghosh

2023

Water Environment Research

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This present investigation aimed at characterizing the biochemical potential and kinetic study of the protease isolated from kitchen wastewater bacteria, P2S1An. The enzymatic activity was optimum when incubated for 96 h, at 30°C and pH 9.0. The enzymatic activity of the purified protease (PrA) was 10.47‐folds that of crude protease (S1). PrA was about 35 kDa in molecular weight. The broad pH and thermal stability, chelators, surfactants and solvent tolerance, and favorable thermodynamics suggested the potentiality of the extracted protease PrA. Thermal activity and stability were enhanced in presence of 1‐mM Ca2+ ion at high temperatures. The protease was a serine one as its activity was completely diminished in presence of 1‐mM PMSF. The Vmax, Km, and Kcat/Km suggested stability and catalytic efficiency of the protease. PrA hydrolyzes fish protein with 26.61 ± 0.16% of peptide bond cleavage after 240 min, comparable to Alcalase 2.4L (27.13 ± 0.31%). Practitioner points A serine alkaline protease PrA was extracted from kitchen wastewater bacteria Bacillus tropicus Y14. Protease PrA showed significant activity and stability in a wide temperature and pH range. Protease showed great stability towards additives like metal ions, solvents, surfactants, polyols, and inhibitors. Kinetic study showed that the protease PrA had a prominent affinity and catalytic efficiency for the substrates. PrA hydrolysed fish proteins into short bioactive peptides which signify its potential in the formation of functional food ingredients.

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Production, Partial Purification, and Biochemical Characterization of a Thermotolerant Alkaline Metallo-protease from Staphylococcus sciuri

Cited by 15 publications

References 41 publications

Characterization of alkaline metalloprotease isolated from halophilic bacterium Bacillus cereus and its applications in various industrial processes

Characterization of alkaline metalloprotease isolated from halophilic bacterium Bacillus cereus and its applications in various industrial processes

Quercetin mitigates rheumatoid arthritis by inhibiting adenosine deaminase in rats

Screening, characterization, and kinetic studies of a serine alkaline protease from kitchen wastewater bacteria P2S1An and evaluation of its application in nutraceutical production

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