Purification and Characterization of Keratinase from &lt;i&gt;Bacillus licheniformis&lt;/i&gt; dcs1 for Poultry Waste Processing

Liaqat, Iram; Ali, Sikander; Butt, Abida; Durrani, Arjumand Iqbal; Zafar, Urooj; Saleem, Sadiah; Naseem, Sajida; Ahsan, Fatima

doi:10.5650/jos.ess21426

Cited by 9 publications

(2 citation statements)

References 26 publications

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“…Pseudomonas aeruginosa (E2) and Pseudomonas putida (B2) also showed the highest keratinase activity on the nutrient medium with feathers, and the lowest activity on the medium with nails [15]. Similar results were obtained for B. licheniformis dcs1 keratinase, whose ability to hydro-lyze various keratin-containing substrates can be ranked as follows: feathers (48.5 U/mL) < bovine hair (35 U/mL) < baby nails (12 U/mL) < baby hair (10 U/mL) [18].…”

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confidence: 74%

Substrate Specificity of Bacillus megaterium UСM B-5710 Keratinase

Avdiyuk,

Varbanets

2023

Mikrobiol. Z.

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The specifics of the processing of livestock and poultry products is that in the process of obtaining the main marketable products, about half the feedstock at various stages of the technological process turns into waste that pollutes the environment. These by-products contain large amounts of the hard-to-digest keratin protein. The use of specific enzymes capable of degrading this protein helps not only to reduce the negative anthropogenic impact on nature but also to obtain valuable hydrolysates that can be used as a fertilizer for plants or a feed additive. The aim of this work was to study the ability of Bacillus megaterium UCM B-5710 to split various keratin-containing substrates: black and white chicken feathers, white turkey feathers, parrot feathers of various colors, sheep wool, pig bristles, and baby hair and nails. Methods. The culture was grown under conditions of submerged cultivation at 40 °C, with a nutrient medium stirring rate of 201 rpm for 6 days. For growth, a basic nutrient medium containing 0.5% defatted chicken feathers or other keratin-containing substrates as sole sources of carbon and nitrogen were used. Keratinase activity was assessed by UV absorption at 280 nm of hydrolysis products of keratin-containing raw materials. Protein was determined by the Lowry method, caseinolytic (total proteolytic) activity was determined by the Anson method modified by Petrova, and amino acid content was determined by the ninhydrin method. The degree of hydrolysis of the substrates was evaluated by the ratio of the initial and final weight of the substrate. Results. It was shown that the synthesis of keratinase by the culture of B. megaterium UCM B-5710 begins from the 6th hour of cultivation. The level of protein and proteolytic activity and the content of amino acids increased throughout the entire period of culture growth. The supernatant of the culture liquid of B. megaterium UCM B-5710 was most effective in splitting white chicken’s and turkey’s feathers, a little slower — feathers of black chicken and blue parrots, as well as wool of white sheep. According to the degree of splitting, the substrates used can be arranged in the following order: white turkey feathers > white chicken feathers > black chicken feathers > blue parrot feathers > white sheep wool > baby nails > pig bristle > baby hair. The study of the effect of feather color on the resistance to decomposition showed that black, blue, and red feathers are more resistant, which coincides with the literature data. Conclusions. B. megaterium UCM B-5710 produces keratinase capable of splitting both α- and β-keratins, however, with different efficiencies and rates.

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confidence: 74%

Substrate Specificity of Bacillus megaterium UСM B-5710 Keratinase

Avdiyuk,

Varbanets

2023

Mikrobiol. Z.

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“…Современные подходы к гидролизу кератина основаны на применении протеолитических ферментов бактериального и грибного происхождения [4,5]. В настоящее время существует обширная база сведений о бактериальных кератиназах и их продуцентах [6][7][8][9][10]. В том числе известно множество коммерческих кератинолитических препаратов на основе бактериальных протеаз [11,12], однако проблема переработки кератинсодержащих отходов сельского хозяйства остается нерешенной.…”

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Keratinolytic Potential of Micromycete Aspergillus Clavatus VKPM F-1593 and Comparison of Its Enzymes With the Commercial Keratinase Preparation

TIMORSHINA,

POPOVA,

KULESHOVA

et al. 2024

Vestn. Mosk. Univ. Ser. 16. Biol.

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Animal husbandry is a rapidly developing branch of agriculture, increasing the volume of production annually, and keratin-containing waste (feathers, bristles) make up the majority of all waste from this industry. The development of methods of environmentally friendly processing of such waste to obtain valuable resources (amino acids and oligopeptides) is an important mission of modern science, including biotechnology. One of the ways to dispose of animal husbandry waste that meets modern trends in the development of a green economy is the use of microorganisms and their enzymes. The possibility of obtaining keratinolytic enzymes of Aspergillus clavatus VKPM F-1593 under deep conditions with various sources of nitrogen and carbon, including with the growth of the producer on animal waste, was studied. The highest target activity (96.1 E) was achieved using mixed carbon and nitrogen sources: inorganic - sodium nitrate, easily digestible organic - fi sh meal hydrolysate and hard-toreach organic - ground chicken feather. Varying the content of various substrates in the composition of fermentation media allowed not only to regulate the level of proteolytic activity, but also to reach the peak of producer activity on diff erent days of cultivation. The specifi c keratinase activity of A. clavatus VKPM F-1593 (pI 9.3) to various protein substrates with the activity of a commercial proteinase K. Both enzymes showed a similar level of activity regarding most of the substrates used. However, protease A. clavatus VKPM F-1593 has a greater overall proteolytic activity, which confi rms the prospects of this culture for biodegradation of animal waste

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