Production, partial optimization and characterization of keratinase enzyme by Arthrobacter sp. NFH5 isolated from soil samples. Keratinase is an inducible enzyme that is synthesized only when an inducer ( keratin) appears in the environment. Keratinase can be produced by many kinds of. The three Bacillus spp. produced extracellular keratinases and of feather or feather meal on the production of keratinolytic enzymes by three.

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The optimum activity of keratinase enzyme was found at pH 8. The organisms were exposed to sublethal doses of the mutagen for different time intervals.

The isolates those produce clear zones on both media were considered as keratinase producers. On the one hand, it solves the problem of insufficient protein resources in the current feed industry, as well as can solve the problem of environmental pollution.

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Microbial Keratinase Production and Application to Improve the Properties of Wool Fabrics

Acknowledgements Authors are grateful to Microbial Biotechnology Division, National Institute of Biotechnology for providing research facilities. There was no significant variation in biomass production in three media. Biodegradation of chicken feathers waste directed by Bacillus subtilis recombinant cells: Fermentation media designed with starch as carbon source and soya bean meal as nitrogen source supported high levels of enzyme production.

Identification of Bacterial Isolates Identification of the keratinolytic bacterial isolates was carried out by determining morphological, cultural, biochemical, and genetic characters. Preliminary study on keratinase from two Indonesian isolates.

Enzyme Research

Keratinases were detected in a range of 45—80 kDa in B. Conclusions It has been determined that in the production of keratinase from Streptomyces prdouction. Int J Environ Sustain Dev.

Readings were carried out in a spectrophotometer at nm. J Indian Leather Technol Assoc. Enzyme production was monitored according to the keratinase activity. The degradation started with the adhesion of the bacteria to the feather. Nirmal Chandra Barman, Email: Distributors To view the contact information for a specific location, select the desired country: Materials and Methods 2.

Keratinases with molecular masses ranging from 15 to kDa have been reported [ 33 ]; however the majority of keratinases presented molecular masses varying from 20 to 50 kDa [ 34 ]. Various authors have reported that, among the keratinolytic microorganisms, some species of Bacillus [ 10 — 12 ], actinomycetes [ 91314 ], and fungi [ 15 — 17 ] are able to produce these keratinases and peptidases.

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The area shrinkage of untreated prouction wool samples subjected to different treatments as a function of keratinzse Wascator shrinkage test cycles. After cultivation in minimal medium with feather as the sole carbon and nitrogen source, three isolates, presenting a pronounced growth and feather degradation, priduction selected and identified as Bacillus subtilis LFB-FIOCRUZB. Isolation and identification of feather degrading bacteria from feather dumped soil.

Effect of different substrates on keratinase production by Arthrobacter sp. Enzyme production might be declined in the presence of higher concentration of feather meal indicating catabolic suppression Saibabu et al.

Among all of them, best one keratinase producing bacterium NFH5 has been selected based on their enzyme activity. There are also known promising keratinase producers in actinomycetes especially from Streptomyces genus [9, 10], Streptomyces fradiae [11], Streptomyces pactum [12], Streptomyces graminofaciens [13], Streptomyces gulbarguensis [14] and Thermoactinomyces sp.

Inorganic nitrogen source in the form of NH 4 Cl had no significant effect on the production of keratinase for the MBF isolates, with the yield being either lower than or comparable to controls. The maximum enzyme production was recorded While the keratinase production in the fermentation medium containing 0.

The soil samples were collected from Hazaribagh tannery industry, Dhaka and local poultry farms of Savar, Dhaka.

Keratinase

The ratio of sulphur compounds released by MBF isolates showed that the inorganic sulphate concentration was significantly lower than the organic sulphur in the culture filtrate for the isolates. At present, it is generally believed that the degradation process of keratinase is divided into three steps, namely denaturation, hydrolysis and transamination.

Feather degradation with a thermotolerant Streptomyces graminofaciens strain, World J. Sources As early as the beginning of the 19th century, people discovered that some organisms could degrade keratin, and the separation of such strains nezyme been ongoing since then.

In most cases, keratin degradation is executed by gram positive bacteria Gupta and Ramnani Extracellular keratinases of proxuction Bacillus such as B. The use of keratinase to improve the permeability of drugs in keratin can improve the efficacy of skin external medicine.

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According to the results, tween 80 increased the keratinase production to high levels comparing to the control group. Some fungi reduce the disulfide bonds through the sulfites secreted on the surface of the mycelia and keratijase acidic environment, while Streptomyces through enzhme production of intracellular reductase. Materials and Methods Producyion were collected from the feather dumps, poultry manure, and fresh poultry litter from local poultry farms in and around Tirupati, Andhra Pradesh, India.

Considering that the presence of keratinous substrates usually induces keratinase production, the main aim of the study was to compare the influence of feather or feather meal on the production of keratinolytic enzymes by three Bacillus spp. Screening and production of extra cellular feather degrading enzyme from Bacterial isolates. Among the organic nitrogen supplemented media, maximum amount of keratinase production was found These results showed the potential of feather meal as a substrate for microbial fermentation.

NFH5 was found Discussion The demand of keratinolytic proteases is still increasing due to its potential usage in different industries.

The animal has a complete range of essential amino acids, which is a good source of feed protein that can replace or partially replace fish meal. These dehairing chemicals contain a high amount of pollutants such as soda-lime, salts, chromate, sulphide, solvent flashy, emulsified fatty matter, waste lime liquor. In general, production of keratinase requires high aeration and submerged conditions with the exception of keratinase reported from thermophilic anaerobic bacteria where enzyme production was favored by static anaerobic conditions [ 730 ].

Gelatin a and keratin b zymogram analysis of extracellular peptidases from B. Samples were collected from productjon feather dumps, poultry manure, and fresh poultry litter from local poultry farms in and around Tirupati, Andhra Pradesh, India.

Optimization of growth conditions for maximum keratinase production The enzyme production was assayed by bacterium before optimizing the parameter of media components and culture condition.