Production, Purification and Characterisation of Keratinases From Bacillus species Isolated From Poultry Feather Waste

DADA, None Michael Tunde; Wakil, Sherifah Monilola

doi:10.31364/scirj/v8.i4.2020.p0420767

Cited by 3 publications

(3 citation statements)

References 31 publications

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“…All chemicals used were of analytical grade obtained from Sigma-Aldrich (United States). Keratinases; EZYKer-51, EZYKer-50 and EZYKer-53 from keratin degrading Bacillus licheniformis-K51, Bacillus subtilis-K50 and Bacillus sp.-K53 respectively were obtained from a previous work carried out at the Industrial Microbiology of the University of Ibadan [8].…”

Section: Methodsmentioning

confidence: 99%

Stain-removal potential of keratinase produced by Bacillus species isolated from feather waste

DADA¹,

Wakil²

2022

GSC Adv. Res. Rev.

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The aim of this study was to determine the potential of keratinases produced by Bacillus species isolated from poultry feather waste in stain removal. The effect of individual and combined detergent components on the keratinase activity of EZYKer-51, EZYKer-50 and EZYKer-53 enzymes produced from keratin degrading Bacillus licheniformis-K51, Bacillus subtilis-K50 and Bacillus sp.-K53 respectively was determined. EZYKer-51, which had the least enzyme inhibition in the presence of the detergent component was used as the enzyme component in detergent formulation and a wash performance analysis test was carried out to compare the stain removal capacity of DETKER 51 (detergent formulated using EZYKer-51 as enzyme component) with a commercial enzyme. Data were analyzed using descriptive statistics. EZYKer-51 showed a significantly higher (P≤0.05) enzyme activity in the presence of the detergent ingredients for both the crude and purified forms of the enzyme compared with the activities of EZYKer-50 and EZYKer-53, except for the activities (8.02±1.32 U/mL and 7.94±0.63 U/mL) in the presence of 15% LAS and 5% liquid paraffin. Visually, better stain removal was achieved when endogenous protease of commercial enzyme was replaced with EZYKer-51. These results suggest that keratinase EZYKer-51 may be a useful alternative for applications in detergent formulation.

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Section: Methodsmentioning

confidence: 99%

Stain-removal potential of keratinase produced by Bacillus species isolated from feather waste

DADA¹,

Wakil²

2022

GSC Adv. Res. Rev.

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Section: Methodsmentioning

confidence: 99%

“…At 40 min of application, complete hair removal was observed at some parts where the commercial depilatory cream was applied (as indicated by the smooth portion of the rat skin). (Dada and Wakil, 2020) but lack the ability to effectively degrade collagen, which is a crucial property for an enzyme intended to be used in skin dehairing. This characteristic suggests the potential utility of the enzymes in the selective removal of hair without causing any damage in the collagen content of skin and hides.…”

Section: Dehairing Function Of Formulated Depilatory Cream (Depiker 51) On Wistar Ratmentioning

confidence: 99%

Hair Removal Potential of Keratinase Produced by Bacillus Species Isolated From Feather Waste

DADA

Wakil²

2021

J microb biotech food sci

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Keratins are tough, fibrous proteins found as the major protein component in hair. Chemical hair removal is harsh and results in severe toxicity and pollution, hence, a need for a non-chemical enzymatic hair removal process. The aim of this study is to characterise keratinase from isolated keratin-degrading Bacillus licheniformis-K51, Bacillus subtilis-K50 and Bacillus sp.-K53 and investigate its potential in hair removal. The collagenolytic ability of keratin-degrading keratinases obtained from Bacillus licheniformis-K51, Bacillus subtilis-K50 and Bacillus sp.-K53 was determined using standard methods. The depilatory potential of keratinase (directly and as part of the constituent of formulated depilatory cream) was determined in vitro on goat skin and in vivo on Wistar rat. Purified keratinases from Bacillus licheniformis-K51 (EZYKer-51), Bacillus subtilis-K50 (EZYKer-50) and Bacillus sp.-K53 (EZYKer-53) did not show significant collagenolytic activities. In vitro treatment of goat skin with EZYKer-51 showed total hair removal within 24 hours and partial hair removal with EZYKer-50 and EZYKer-53. The formulated depilatory cream containing EZYKer-51 showed highest keratinolytic activity (22.20±0.63 U/mL) followed by EZYKer-50 (20.52±0.46 U/mL) and EZYKer-53 (17.06±0.81 U/mL). In vivo depilatory action using formulated cream took 40 min, while that of commercial cream was achieved within 20 min. Keratinase from Bacillus licheniformis-K51 exhibited complete hair-removal function which makes it potentially suitable in industrial processes involving removal of hair. ARTICLE INFO

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Selection of Optimal Conditions for Cultivation of Bacillus megaterium UCM B-5710 – Producer of Keratinase

Avdiyuk¹,

Roy²

2021

Mikrobiol. Z.

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Every year the volume of production of poultry products all over the world is growing steadily. This contributes to a constant increase in the amount of by-products of poultry processing in the form of down and feather waste, which are dangerous for the environment due to the hard-to-degrade keratin protein and a large number of microbial pathogens. Therefore, the use of environmentally friendly methods for the destruction of keratin substrates due to keratinases of microorganisms is an urgent area of research. The aim of this work was to select the optimal cultivation conditions for the Bacillus megaterium strain UCM B-5710 to increase the activity of the keratinase synthesized by it. Methods. The culture was grown at 28°C, 201 rpm for 7 days on a basic nutrient medium containing defatted chicken feathers as the only source of carbon and nitrogen. The selection of optimal cultivation conditions was carried out according to the following parameters: temperature (21°C, 28°C, 42°C), stirring speed (201 rpm, 212 rpm), amount of inoculum (5%, 10%, 15% , 20%, 25%), the initial pH value of the nutrient medium (4.0–11.0), concentration of keratin-containing substrate (0.1%, 0.2%, 0.5%, 1.0%, 1.5%, 2.0%), additional carbon source (glucose, galactose, lactose, maltose, sucrose, mannitol, potato and corn starch, soluble starch, soybean meal) and nitrogen (NH4Cl, NH4NO3, (NH4)2SO4, NaNO3, urea, peptone, tryptone, yeast extract and soybean meal) at a concentration of 1%. Keratinase activity was assessed by the UV absorption at 280 nm of the hydrolysis products of keratin-containing raw materials. Protein was determined by the Lowry method. Results. The dynamics of the enzyme synthesis showed that the culture of B. megaterium UCM B-5710 exhibited the highest keratinase activity on the 3rd day, and complete splitting of feathers was observed on the 4–5th days. The selection of the concentration of the keratin-containing substrate showed that 0.5% is the optimal concentration. The study of the influence of the initial pH value of the nutrient medium indicates that the culture grew well at pH 6.0–7.0 and pH 9.0–11.0, but at pH 8.0 its growth was very weak. The culture exhibited the maximum keratinase activity at pH 10.0. In addition, at this pH value, complete splitting of feathers was visually observed. The influence of such a key factor as temperature on the growth and synthesis of the enzyme by B. megaterium UCM B-5710 culture demonstrated complete splitting of feathers already on the 2nd day of cultivation at 42°C, at 21°C the culture split feathers very poorly. The introduction of the inoculum into the composition of the nutrient medium in an amount of 15% of the volume of the medium and the mixing intensity of 212 rpm turned out to be optimal. Besides, it was shown that the introduction of an additional source of carbon or nitrogen had an ambiguous effect on the level of keratinase activity of B. megaterium UCM B-5710. Complete inhibition of enzyme synthesis was observed when ammonium sulfate was added to the nutrient medium, and partial inhibition was observed in the case of glucose, lactose, and maltose. Potato, corn, and soluble starch stimulated keratinase synthesis. The majority of inorganic nitrogen sources (ammonium chloride and nitrate) did not affect the synthesis of B. megaterium UCM B-5710 keratinase, while organic sources (urea, peptone, tryptone, yeast extract) increased the level of keratinase activity by 20–50%. However, the most effective result was obtained using soybean meal, the addition of which to the nutrient medium increased the keratinase activity by 2.5 times. Conclusions. As a result of the studies, the optimal conditions for cultivation of the B. megaterium UCM B-5710 strain were selected: the optimum temperature for the growth and development of the culture is 42°C, the initial pH value is 10.0, the stirring speed is 212 rpm and the amount of inoculum introduced is 15%, an additional source of carbon and nitrogen in the form of soybean meal at a concentration of 0.5%. This made it possible to increase the activity of keratinase by 4 times.

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Production, Purification and Characterisation of Keratinases From Bacillus species Isolated From Poultry Feather Waste

Cited by 3 publications

References 31 publications

Stain-removal potential of keratinase produced by Bacillus species isolated from feather waste

Stain-removal potential of keratinase produced by Bacillus species isolated from feather waste

Hair Removal Potential of Keratinase Produced by Bacillus Species Isolated From Feather Waste

Selection of Optimal Conditions for Cultivation of Bacillus megaterium UCM B-5710 – Producer of Keratinase

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