Response surface methodology for production, characterization and application of solvent, salt and alkali-tolerant alkaline protease from isolated fungal strain Aspergillus niger WA 2017

Wahab, Walaa A. Abdel; Ahmed, Samia A.

doi:10.1016/j.ijbiomac.2018.04.041

Cited by 42 publications

(16 citation statements)

References 35 publications

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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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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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“…However, Jaouadi et al reported that AMPP protease produced by Pseudomonas aeruginosa CTM50182 displayed high stability in the presence of various organic solvents than commercial enzymes [62]. On the other hand, n -butanol showed strong inhibition in protease activity from Aspergillus niger WA 2017 [63]. Thus, the intrinsic organic solvent-tolerance and stability of some enzymes depends on the nature of the used organic solvents, which makes them highly attractive to industry [64, 65].…”

Section: Discussionmentioning

confidence: 99%

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

et al. 2019

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Background: Proteases are hydrolytic enzymes that catalyze peptide linkage cleavage reactions at the level of proteins and peptides with different degrees of specificity. This group draws the attention of industry. More than one protease in three is a serine protease. Classically, they are active at neutral to alkaline pH. The serine proteases are researched for industrial uses, especially detergents. They are the most commercially available enzyme group in the world market. Overall, fungi produced extracellular proteases, easily separated from mycelium by filtration. Results: A new basidiomycete fungus CTM10057, a hyperproducer of a novel protease (10,500 U/mL), was identified as Pleurotus sajor-caju (oyster mushroom). The enzyme, called SPPS, was purified to homogeneity by heattreatment (80°C for 20 min) followed by ammonium sulfate precipitation (35-55%)-dialysis, then UNO Q-6 FPLC ion-exchange chromatography and finally HPLC-ZORBAX PSM 300 HPSEC gel filtration chromatography, and submitted to biochemical characterization assays. The molecular mass was estimated to be 65 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Native-PAGE, casein-zymography, and size exclusion by HPLC. A high homology with mushroom proteases was displayed by the first 26 amino-acid residues of the NH 2-terminal aminoacid sequence. Phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP) strongly inhibit SPPS, revealing that it is a member of the serine-proteases family. The pH and temperature optima were 9.5 and 70°C, respectively. Interestingly, SPPS possesses the most elevated hydrolysis level and catalytic efficiency in comparison with SPTC, Flavourzyme® 500 L, and Thermolysin type X proteases. More remarkably, a high tolerance towards organic solvent tolerance was exhibited by SPPS, together with considerable detergent stability compared to the commercial proteases Thermolysin type X and Flavourzyme® 500 L, respectively. Conclusions: This proves the excellent proprieties characterizing SPPS, making it a potential candidate for industrial applications especially detergent formulations.

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“…Since microbial protease production and chitin extraction were found to depend on different operational parameters, therefore, a Placket-Burman design (PBD) was used to identify the significant variables affecting these targets. Nine variables previously reported as significant factors for protease production, deproteinization, and demineralization of chitin in bacterial fermentation (Maruthiah and Palavesam 2017;Abdel Wahab and Ahmed 2018;Patel et al 2019) were examined. Totally,…”

Section: Significant Factors Affecting Protease Production and Chitin Extraction From Shrimp Shell By Bacillus Cereus Hmrsc30mentioning

confidence: 99%

Optimization of protease production by Bacillus cereus HMRSC30 for simultaneous extraction of chitin from shrimp shell with value-added recovered products

Cahyaningtyas

Suyotha

Cheirsilp

et al. 2021

Environ Sci Pollut Res

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Chitin extraction from shrimp shell powder (SSP) using protease-producing microbes is an attractive approach for valorizing shrimp shell waste because it is simple and environmentally friendly. In this study, the protease production and chitin extraction from SSP by Bacillus cereus HMRSC30 were simultaneously optimized using statistical approaches. As a result, fermentation in medium composed of 30 g/L SSP, 0.2 g/L MgSO 4 · 7H 2 O, 3 g/L (NH 4 ) 2 SO 4 , 0.5 g/L K 2 HPO 4 , and 1.5 g/L KH 2 PO 4 (pH 6.5) for 7 days maximized protease production (197.75 ± 0.33 U/mL) to approximately 1.64-fold compared to unoptimized condition (126.8 ± 0.047 U/mL). This level of enzyme production was enough to achieve 97.42 ± 0.28% deproteinization (DP) but low demineralization (DM) of 53.76 ± 0.21%. The high DM of 90% could be easily accomplished with the post-treatment using 0.4 M HCl and acetic acid. In addition, the study evaluated the possible roadmap to maximize the value of generated products and obtain additional profits from this microbial process. The observation showed the possibility of serving crude chitin as a bio-adsorbent with the highest removal capacity against Coomassie brilliant blue (97.99%), followed by methylene blue (74.42%). The recovered protease exhibited the function to remove egg yolk stain, indicating its potential for use as a detergent in de-staining. The results corroborated the benefits of microbial fermentation by B. cereus HMRSC30 as green process for comprehensive utilization of shrimp shell waste as well as minimizing waste generation along the established process.

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Response surface methodology for production, characterization and application of solvent, salt and alkali-tolerant alkaline protease from isolated fungal strain Aspergillus niger WA 2017

Cited by 42 publications

References 35 publications

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

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

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

Optimization of protease production by Bacillus cereus HMRSC30 for simultaneous extraction of chitin from shrimp shell with value-added recovered products

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