Biochemical characterization of a surfactant-stable keratinase purified from Proteus vulgaris EMB-14 grown on low-cost feather meal

Babalola, Michael Oluyemi; Ayodeji, Adeyemi Oluwadare; Bamidele, Olufemi S.; Ajele, Joshua O.

doi:10.1007/s10529-020-02976-0

Cited by 13 publications

(9 citation statements)

References 45 publications

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“…The results of the puri cation showed a nal purity of 6.13 times higher with a yield of 19.4%, which was consistent with the results of Jaouadi et al [27] on B. tequilensis Q7. The puri ed keratinase was stable over a wide range of temperatures (20-80°C) and pH (3.5-12) with a maximum keratinolytic activity at 60°C and pH value of 8, which is in line with the results obtained by others [28][29][30]. The enzyme maintained more than 70% of its activity in the wide pH range from acidic to alkaline conditions (5.5-9), and more than 80% of its stability in the wide range of temperature (30-60°C), which can be considered as a unique feature of the present keratinase for commercialization.…”

Section: Discussionsupporting

confidence: 90%

“…Optimization of the culture conditions was conducted using one factor at a time method. The factors including temperature (20,30,37,40, 45 and 50°C), pH (3 to 12.5 with a difference of 0.5 units), feather substrate concentration (0.5, 1, 2, 3, 4, 5, 6 and 7), shaking speed (125, 150, 175, 200 and 225 rpm), additional carbon source (glucose, fructose, starch, dextrose and sucrose 1%), additional nitrogen source (organic sources of peptone, tryptone, yeast extract and mineral sources of ammonium nitrate, ammonium chloride, ammonium sulfate and potassium nitrate), aeration (25, 50, 75 and 85%) and bacterial inoculation (1, 2, 4, 8 and 16%) were studied step by step. Data were statistically analyzed by SPSS software version 16 at 95% con dence level.…”

Section: Optimization Of Keratinase Productionmentioning

confidence: 99%

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Characterization of a Novel Keratinase With Surfactant Stability in a Wide Range of pH Activity From a Native Isolate, Bacillus Mojavensis FUM125

Jeddi

Sharifmoghadam

Asoodeh

et al. 2021

Preprint

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Keratinases are enzymes with the most diverse sources and applications. Different forms of keratinase have been applied in environment and variety of industries, highlighting the necessity for novel potential keratinases, which could be applicable in variety of industries. Accordingly, the present study aimed to identify and characterize a novel keratinase producing bacterium with high potential in variety of industries. In the present study, the native isolate of Bacillus sp. FUM125 was isolated, identified and optimized for the keratinolytic activity. The keratinase was purified and characterized using biochemical assays. The Bacillus sp. FUM125 isolate was identified as Bacillus mojavensis R-OH-1 with 99.8% similarity. The isolate showed the maximum keratinolytic activity at pH of 8.5 after 24-hour incubation at 37°C (2.1-fold enzyme production). According to the biochemical analysis, the keratinase belonged to a serine protease family, whit 33.5 kDa molecular weight and was stable in a wide range of pH and temperature with maximum keratinolytic activity at 60°C and pH 8. Among the metal ions, K+, Ca2+, Na2+ and Mg2+ increased the enzyme activity. The activity was increased by the reducing agents of DTT and beta-mercaptoethanol. Based on the substrate profile findings, the enzyme was active in various soluble and insoluble substrates. The enzyme showed a half-life of 98 min in the optimal temperature and the ratio of keratinolytic:caseinolytic to be 0.95. Our enzyme with higher temperature and pH stability compared to existing commercial enzymes can be considered as a potential candidate for use in various industries.

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Section: Discussionsupporting

confidence: 90%

Section: Optimization Of Keratinase Productionmentioning

confidence: 99%

Characterization of a Novel Keratinase With Surfactant Stability in a Wide Range of pH Activity From a Native Isolate, Bacillus Mojavensis FUM125

Jeddi

Sharifmoghadam

Asoodeh

et al. 2021

Preprint

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“…Keratinase exhibits the enzyme activity at temperatures ranging from 30 to 70 °C or higher, and the optimal temperature of Fervidobacterium islandicum AW-1 is 100 °C [ 13 – 15 ]. The optimum pH for most keratinases is between 7.0 and 10.0, whilst the optimal pH for Trichophyton schoenleinii is 5.5 [ 16 – 18 ]. Moridshahi et al reported that the effect of metal ions on keratinase from B. zhangzhouensis , Ca 2+ , K + , Na + and Mn 2+ could improve enzyme activity [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Isolation and identification of a feather degrading Bacillus tropicus strain Gxun-17 from marine environment and its enzyme characteristics

et al. 2022

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Background Feathers are the most abundant agricultural waste produced by poultry farms. The accumulation of a large number of feathers not only seriously pollutes the environment but also causes the waste of protein resources. The degradation of feather waste by keratinase-producing strains is currently a promising method. Therefore, screening high-producing keratinase strains from marine environment and studying the fermentation conditions, enzymatic properties and feather degradation mechanism are crucial for efficient degradation of feathers. Results A novel efficient feather-degrading bacteria, Gxun-17, isolated from the soil sample of a marine duck farm of Beibu Gulf in Guangxi, China, was identified as Bacillus tropicus. The optimum fermentation conditions were obtained by single factor and orthogonal tests as follows: feather concentration of 15 g/L, maltose concentration of 10.0 g/L, MgSO4 concentration of 0.1 g/L, initial pH of 7.0 and temperature of 32.5 °C. The strain completely degraded the feathers within 48 h, and the highest keratinase activity was 112.57 U/mL, which was 3.18-fold that obtained with the basic medium (35.37 U/mL). Detecting the keratinase activity and the content of sulphur-containing compounds in the fermentation products showed that the degradation of feathers by the strain might be a synergistic effect of the enzyme and sulphite. The keratinase showed optimal enzyme activity at pH 7.0 and temperature of 60 °C. The keratinase had the best performance on the casein substrate. When casein was used as the substrate, the Km and Vmax values were 15.24 mg/mL and 0.01 mg/(mL·min), respectively. Mg2+, Ca2+, K+, Co2+, Al3+, phenylmethylsulphonyl fluoride and isopropanol inhibited keratinase activity, which indicated that it was a serine keratinase. Conversely, the keratinase activity strongly increased with the addition of Mn2+ and β-mercaptoethanol. Conclusions A novel feather-degrading B. tropicus Gxun-17 was obtained from marine environment. The strain adapted the extreme conditions such as low temperature, high salt and high pressure. Thus, the keratinase had high activity, wide range of temperature and pH, salt tolerance and other characteristics, which had potential application value.

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“…Despite this, metal ions, especially mercury, are powerful inhibitors of bioremediation, as is the case with many xenobiotics. As the dialysis tube approach may shield the bioreduction process from heavy metals, it is an appealing bioremoval technology [37][38][39][40][41]. This work reports for the first time the possible application of this approach in safeguarding molybdenum removal by a bacterium in the presence of mercury.…”

Section: Introductionmentioning

confidence: 99%

Entrapment of Mo-reducing Bacterium Increase its Resistance towards Mercury

Uba

Shukor

Yakasai

2022

J Environ Bioremed Toxicol

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In ruminants, even trace amounts of molybdenum can be lethal. In areas with high pollution, molybdenum levels in soil and mine tailings can exceed 20,000 ppm. Bioremediation of molybdenum can be challenging when toxic mercury is also present. This research presents a novel approach using dialysis tubing and the molybdenum-reducing activity of Enterobacter sp. strain Dr. Y13 for molybdenum removal from aqueous solutions. Molybdenum blue (Mo-blue), produced during enzymatic reduction, is insoluble in dialysis tubing and this can be a twofold advantage as a method of removal and as a method to protect bacterial cells from heavy metal inhibition, especially mercury. In this experiment, we assess the toxicity-shielding effect of dialysis tubing for molybdenum reduction to Mo-blue by this bacterium in the presence of mercury. As the concentrations of mercury were increased, both free and immobilized cells were strongly inhibited. Modelling using the dissociationone phase exponential decay model gave an IC50 value for the immobilized form of 0.1107 mg/L (95% confidence interval from 0.073 to 0.217 while the IC50 value for the free cell system was 0.023 mg/L (95% C.I. from 0.019 to 0.028). Since the confidence interval for the IC50 values did not overlap, the immobilized system gave better protection from mercury than the free cell system. Toxicity to free cells was higher than toxicity to cells trapped in dialysis tubes, suggesting that trapping Mo-reducing cells may be an effective strategy for bioremediation of water or wastewater contaminated with multiple heavy metals.

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Biochemical characterization of a surfactant-stable keratinase purified from Proteus vulgaris EMB-14 grown on low-cost feather meal

Cited by 13 publications

References 45 publications

Characterization of a Novel Keratinase With Surfactant Stability in a Wide Range of pH Activity From a Native Isolate, Bacillus Mojavensis FUM125

Characterization of a Novel Keratinase With Surfactant Stability in a Wide Range of pH Activity From a Native Isolate, Bacillus Mojavensis FUM125

Isolation and identification of a feather degrading Bacillus tropicus strain Gxun-17 from marine environment and its enzyme characteristics

Entrapment of Mo-reducing Bacterium Increase its Resistance towards Mercury

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