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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Three different surface-active compounds were added to the fermentation medium in two different concentrations and the growth of microorganism and enzyme activity were monitored. Additionally the percentage of degradation of feather, or feather meal by the three stains, was evaluated. Yeast extracts were the other nitrogen sources supporting enzyme production.

Efficient Degradation of Feather by Keratinase Producing Bacillus sp.

These keratins are biologically insoluble, fibrous, recalcitrant and biochemically rigid molecules which are resistant to degradation by most common proteolytic enzymes McGovern ; Riffel et al. The structure and chemistry of keratin fibers, in: Potential keratinolytic isolates were reisolated as productoon cultures and confirmed for keratinase production in basal medium and complete media [ 14 ].

High diversity among feather-degrading bacteria from a dry meadow soil.

Keratinase production from feathers wastes using some local Streptomyces isolates. Enzymographic analysis using keratin substrate Enzyke 5 demonstrated that the enzymatic extract obtained from the Bacillus was able to hydrolyze keratin.

Sources As early as the beginning of the 19th century, people discovered that some organisms could degrade keratin, and the separation of such strains has been ongoing since then. Identification of Enzgme Isolates Identification of the keratinolytic bacterial isolates was carried out by determining morphological, cultural, biochemical, and genetic characters. Alteration of the keratinase activity according to the time 3. This yield was significantly higher than several of the keratinase producing bacterial species reported earlier but was comparable with Bacillus licheniformis PWD1 [ 1231 ].


So the properties of this enzyme increase the probability in industrial application at high temperature. After the enzymatic treatment, smaller peptide and protein segments are removed, proteolytic reaction increases and hydrophilic surface occurs.

A total of 44 morphologically well-formed single colonies were selected from ten different soil samples on the basis of their morphological difference in nutrient agar plates. Useful enzymes for bioprocessing agroindustrial wastes and beyond, Food Bioprocess. Glucose had no effect on keratin degradation with Bacillus sp.

Shrinkage Properties Table 4 shows the area shrinkage of wool fabrics treated with enzymes. In terms of growth, the organisms showed less growth at pH 4. We denoted the isolate as Arthrobacter sp. Afr J Microbiol Res. Synthesis and regulation of extracellular keratinase in three fungi isolated from the grounds of a gelatin factory, Jabalpur, India.

Soft keratin skin and callus is less resistant to chemical agents and degradation process comparing to hard keratin feather, wool, nails because of their low cysteine content [3]. The cell free supernatant was collected and used for the assay of keratinase activity. Optimization of cultural conditions for keratinase production The production of keratinase by bacterial inoculums was studied by considering the media components and culture enzyne. The production of keratinase by bacterial inoculums was studied by considering the media components and culture conditions.

The study was conducted to select the best promising keratinolytic bacterial strain. For proteolytic detection the gels were incubated in coomassie blue as described above, overnight, and decolorized with methanol: Further increase in the inoculums size, greatly decreased the production might be due to rapid growth of bacteria keratinse depletion of essential nutrients by bacteria in the early stages.

Enzyme Research

Degradation of feather substrate was found to be associated with significant increase in pH of the medium to alkalinity, thus serving as an indicator for the efficiency of degradation. Enhancing the Keratinase Production In the first part of this study the keratinase production from Streptomyces sp.


Confidence limits on phylogenies: Hence, optimum enzyme production by Arthrobacter sp. Some fungi 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.

Hydrolysis of feather keratin by immobilized keratinase. However, the full commercial potential of keratinases is yet to be realized.

This was followed by spread to shaft prodjction 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.

Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. Maximizing the Production of Keratinase The two selected native isolates were subjected to treatment with a combination of physical UV light and chemical hydroxylamine hydrochloride HA and ethyl methyl sulphonate EMSmutagens adopting nezyme method of Eisentadt [ 23 ].

Finally, the fabric was rinsed several times with deionized water to remove any remaining enzyme from the treatment.

The enzyme was also partly characterized in the study. The optimum pH of some keratinase can reach about After the runs the gels were washed twice with Triton-X 2.

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 keratin substrates, and the culture conditions [ 3132 ].

Proteolytic and keratinolytic activity of B.