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 aim of the study was enhancing keratinase production from Streptomyces sp. The concentrated culture supernatants were submitted to zymography, as described above, with gelatin or keratin as substrates copolymerized. It has been reported previously, maximum keratinase production was achieved in yeast extract supplemented media as organic nitrogen source Sivakumar et al.

Keratinase has highly efficient keratin hydrolyzing activity. Keratinase production and keratin degradation by mutant strain of Bacillus subtilis. Decomposition of native keratin by Streptomyces fradiaeJ.

Properties The molecular weight of keratinase that has been isolated and purified is quite different, ranging from dozens of kDa to several hundred kDa. Effect of pH on keratinase activity. Keratinase enzyme was assayed by azokeratin assay adopting the method of Lin et al.

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

The bacterium had a neutral pH range for keratinase production. Although wool gave satisfactory performance for fermentation process as a substrate, it is not readily available when compared to glucose.

Hydrophilicity results of treated and ketatinase fabrics. Further increase in the inoculums size, greatly decreased the production might be due to rapid growth of bacteria and depletion of essential nutrients by bacteria in productionn early stages.

Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. Production, purification and characterization of keratinase using chicken feather as a substrate by Bacillus sp.


The sequences are deposited in GenBank with accession numbers EU Further biochemical characterization was carried out adopting standard tests as described in Collee et al.

Effect of temperature on keratinase activity. The molecular weight of most keratinases is concentrated between 30 and 70 kDa. Keratinase positive bacteria were cultured on skim milk agar and feather meal agar plates. Shrinkage Properties Table 4 shows the area shrinkage of wool fabrics treated with enzymes.

Keratinase – Creative Enzymes

An investigation into keratinolytic productioh to enhance ungual drug delivery. Wool fibers are strongly hydrophobic due to the epicuticle and exocuticle layers of wool scales. Protein concentration in culture supernatant of B. After the enzymatic treatment, smaller peptide and protein segments are removed, proteolytic reaction increases and hydrophilic surface occurs.

Optimization of Nutritional and Physical Parameters For optimization of nutritional parameters, basal medium was supplemented with nine different carbon sources individually at concentration range from 0. Some enyme reduce the disulfide bonds through the sulfites secreted on the surface of the mycelia and the acidic environment, while Streptomyces through the production of intracellular reductase.

The ability of a microorganism to degrade keratin and the resulting levels of keratinase produced vary according to the specie, chemical composition, the molecular structure of keratianse substrates, and the culture conditions [ 3132 ].

Similarities and specificities of fungal keratinolytic proteases: Screening and production of extra cellular feather degrading enzyme from Bacterial isolates. The authors would like to thank the technical assistance of Ms.

Subsequently, the produced keratinase and commercial enzyme were compared for prodution the hydrophilicity, dyeing and shrinkage properties of wool fabrics.

Finally, ammonia and sulfide are produced by transamination to completely hydrolyze keratin. Keratlnase the keratinase production in the fermentation medium containing 0. Bacterial keratinases have potentiality because of their activity on degradation of specific insoluble keratin substrates and generally on a variety of protein materials Lin et al.



keratlnase In this study, to facilitate the usage of wool by the Streptomyces sp. The structure and chemistry of keratin fibers, in: Felting and shrinkage are the major problems for wool keratinasf.

Int Res J Biol Sci. Enzyne J Microbiol Res. This was followed by spread to shaft region leading to its rupture and disintegration of the shaft to needle like structures by the sixth day leading to complete degradation of feather Figure 4. Morphological and biochemical characterization of BF isolates. The maximum enzyme production was recorded Therefore, its usage as raw substrate for fermentation process, requires additional interventions such as surface-active compounds.

FK 28 isolated in Thailand. Enzyme unhairing of heavy hides. Saitou N, Nei M. Moreover, proteases remove the scale cuticles, which have a tendency keratniase felting shrinkage, or smoothed the edges. On the basis of this approach, Streptomyces sp. FK46 [ 10 ]. Enzymatic treatment is an alternative for improving the quality of wool fabrics [4, 5].

Materials and methods Isolation of bacteria from local soil sample The soil samples were collected from Hazaribagh tannery industry, Dhaka and local poultry farms of Savar, Dhaka. However, different concentrations of the SDS and triton X were keratinass supplied microbial growth so; further experiments were not performed with these surface-active compounds.

Alteration of the keratinase activity according to the time 3. Competing interests The authors declare that they have no competing interests.