Alkaline serine protease from the new halotolerant alkaliphilic Salipaludibacillus agaradhaerens strain AK-R: purification and properties

Ibrahim, Abdelnasser S. S.; Elbadawi, Yahya B.; El-Tayeb, Mohamed A.; Almaary, Khalid S.; Maany, Dina A; Ibrahim, Shebl Salah Shebl; Elagib, Atif A.

doi:10.1007/s13205-019-1928-9

Cited by 26 publications

(16 citation statements)

References 43 publications

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“…Among the tested metal ions, only Mn 2+ ion positively regulated the activity of the protease enzyme from strain HM48 at all concentrations [ 10 ], as manganese ions are reported to stabilize the molecular structure of enzymes in some Bacillus cereus derived proteases [ 92 ]. However, Hg 2+ markedly reduced the enzyme activity from lower (1 mM) to highest (10 mM) concentrations, either by binding of Hg 2+ to the critical side-chains of protein changing its active site structure or by causing general unfolding [ 93 ] and a similar trend has been advocated by Ibrahim et al [ 94 ]. Various researchers have reported the positive as well as negative effects of metal ions like Cd 2+ , Cu 2+ , Fe 2+ , and Hg 2+ , Mg 2+ and Mn 2+ ions on enzyme activities from several Bacillus species [ 86 , 95 ].…”

Section: Discussionmentioning

confidence: 73%

“…[ 17 ]. Although anionic surfactant, SDS has been reported to have a negative influence on the protease enzyme activity [ 75 , 94 ], enzymes under the current study retained > 95% of the activity with SDS (1%). Both of the nonionic surfactants (triton-X100 and tween-80), however, were found to increase the activity from 4–12%, respectively.…”

Section: Discussionmentioning

confidence: 75%

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Biochemical Characterization and Functional Analysis of Heat Stable High Potential Protease of Bacillus amyloliquefaciens Strain HM48 from Soils of Dachigam National Park in Kashmir Himalaya

et al. 2021

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A novel temperature stable alkaline protease yielding bacteria was isolated from the soils of Dachigam National Park, which is known to be inhabited by a wide variety of endemic plant and animal species of Western Himalaya. This high-potential protease producing isolate was characterized and identified as Bacillus amyloliquefaciens strain HM48 by morphological, Gram’s staining and biochemical techniques followed by molecular characterization using 16S rRNA approach. The extracellular protease of B. amyloliquefaciens HM48 was purified by precipitating with ammonium sulfate (80%), followed by dialysis and Gel filtration chromatography increasing its purity by 5.8-fold. The SDS–PAGE analysis of the purified enzyme confirmed a molecular weight of about ≈25 kDa. The enzyme displayed exceptional activity in a broad temperature range (10–90 °C) at pH 8.0, retaining its maximum at 70 °C, being the highest reported for this proteolytic Bacillus sp., with KM and Vmax of 11.71 mg/mL and 357.14 µmol/mL/min, respectively. The enzyme exhibited remarkable activity and stability against various metal ions, surfactants, oxidizing agent (H2O2), organic solvents and displayed outstanding compatibility with widely used detergents. This protease showed effective wash performance by exemplifying complete blood and egg-yolk stains removal at 70 °C and efficiently disintegrated chicken feathers making it of vital importance for laundry purpose and waste management. For functional analysis, protease gene amplification of strain HM48 yielded a nucleotide sequence of about 700 bp, which, when checked against the available sequences in NCBI, displayed similarity with subtilisin-like serine protease of B. amyloliquefaciens. The structure of this protease and its highest-priority substrate β-casein was generated through protein modeling. These protein models were validated through futuristic algorithms following which protein–protein (protease from HM48 and β-casein) docking was performed. The interaction profile of these proteins in the docked state with each other was also generated, shedding light on their finer details. Such attributes make this thermally stable protease novel and suitable for high-temperature industrial and environmental applications.

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Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 75%

Biochemical Characterization and Functional Analysis of Heat Stable High Potential Protease of Bacillus amyloliquefaciens Strain HM48 from Soils of Dachigam National Park in Kashmir Himalaya

et al. 2021

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“…These have also been from saline environments like the marine environments, sea sediments, hypersaline lakes, salted food, soda lakes, etc. (Maruthiah et al 2016 ; Boughachiche et al 2016 ; Ibrahim et al 2019 ). Among the bacteria, the genus Bacillus has a very prominent place in terms of the commercial production of proteases, while the fungal sources are dominated by the genera Aspergillus , Trichoderma , Penicillium , etc.…”

Section: Microbial Proteasesmentioning

confidence: 99%

Microbial proteases: ubiquitous enzymes with innumerable uses

Putatunda²,

et al. 2021

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Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of ‘omics’ era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

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“…In addition to liquid detergent, the stability of PyCP in the commercial detergent powders (Tide and Vanish-Oxi) suggests the utility of PyCP as an additive in powder detergents also. Several studies have reported variable stability and compatibility of alkaline proteases produced by diverse microorganisms in different commercial detergents ( Banik and Prakash, 2004 ; Abidi et al, 2011 ; Abdel Wahab and Ahmed, 2018 ; Ibrahim et al, 2019 ). Further PyCP was evaluated for washing performance wherein PyCP showed enhanced washing performance against different stains (ketchup, coffee, and blood) as compared with the commercially available detergent Vanish-Oxi.…”

Section: Discussionmentioning

confidence: 99%

Multipotential Alkaline Protease From a Novel Pyxidicoccus sp. 252: Ecofriendly Replacement to Various Chemical Processes

et al. 2021

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A newly isolated alkaline protease-producing myxobacterium was isolated from soil. The strain was identified as Pyxidicoccus sp. S252 on the basis of 16S rRNA sequence analysis. The extracellular alkaline proteases produced by isolate S252 (PyCP) was optimally active in the pH range of 11.0–12.0 and temperature range of 40–50°C The zymogram of PyCP showed six caseinolytic protease bands. The proteases were stable in the pH range of 8.0–10.0 and temperature range of 40–50°C. The activity of PyCP was enhanced in the presence of Na+, Mg2+, Cu2+, Tween-20, and hydrogen peroxide (H2O2) (hydrogen peroxide), whereas in Triton X-100, glycerol, ethylenediaminetetraacetic acid (EDTA), and Co2+, it was stable. PyCP showed a potential in various applications. The addition of PyCP in the commercial detergent enhanced the wash performance of the detergent by efficiently removing the stains of tomato ketchup and coffee. PyCP efficiently hydrolyzed the gelatin layer on X-ray film to release the embedded silver. PyCP also showed potent dehairing of goat skin and also efficiently deproteinized sea shell waste indicating its application in chitin extraction. Thus, the results of the present study indicate that Pyxidicoccus sp. S252 proteases have the potential to be used as an ecofriendly replacement of chemicals in several industrial processes.

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Alkaline serine protease from the new halotolerant alkaliphilic Salipaludibacillus agaradhaerens strain AK-R: purification and properties

Cited by 26 publications

References 43 publications

Biochemical Characterization and Functional Analysis of Heat Stable High Potential Protease of Bacillus amyloliquefaciens Strain HM48 from Soils of Dachigam National Park in Kashmir Himalaya

Biochemical Characterization and Functional Analysis of Heat Stable High Potential Protease of Bacillus amyloliquefaciens Strain HM48 from Soils of Dachigam National Park in Kashmir Himalaya

Microbial proteases: ubiquitous enzymes with innumerable uses

Multipotential Alkaline Protease From a Novel Pyxidicoccus sp. 252: Ecofriendly Replacement to Various Chemical Processes

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