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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Keratinase – Creative Enzymes

Synthesis and regulation of extracellular keratinase in three fungi isolated from the grounds of a gelatin factory, Jabalpur, India. SEM images of untreated and treated wool fibers a Untreated, b Treated with keratinase, c Treated with protease 4.

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 ]. Extracellular keratinase and peptidases were obtained after growth of the Bacillus sp.

Two isolates BF11 and BF21 exhibiting maximum keratinase were selected and the keratinase production was compared in three liquid media. Feather and Feather Meal Degradation The percentage of substrate degradation was measured by weight loss.

International Journal of Microbiology

The significant differences between untreated and enzyme treated fibers could be seen clearly from Fig b and c. 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. Keratinase activity with respect to time and the positive effect of tween 80 on the enzyme activity were shown in Figure 2.

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A good keratinase positive bacterium isolated from the soil samples of Hazaribagh tannery industrial zone, Dhaka was identified as Arthrobacter genus depending on the conventional techniques and confirmed as Arthrobacter sp.

Enzyme Research

Kasetsart J Nat Sci ; FK46 [ 10 ]. These results showed the potential of feather meal as a substrate for microbial fermentation. The application potential of keratinase showed similar results in terms of hydrophilicity, dyeing and shrinkage properties of wool fabrics compared to commercial protease enzyme at lower temperatures.

Therefore, the development and utilization of waste feathers have important application prospects. However, presence of glucose as carbon source was found to stimulate the keratinase production in Streptomyces sp.

Salimullah3 and Abu Hashem 2. Keratinase production with required specifications for treating wool fabrics by utilizing raw wool as a substrate was the main idea of this study. Enhancing Keratinase Production Using Surface-active Compounds Raw sheep wool supplied from local butcher was used as a solid substrate for the production of keratinase from Streptomyces sp. Proteases are commonly used for the enzymatic treatment of wool fabrics in the textile industry.

The dyes used were kindly supplied by DyStar Company and the commercial protease enzyme was supplied by Novozyme. Seventeen different keratinolytic microorganisms were isolated from poultry waste in decomposition. The smaller keratinase is a monomeric enzyme with a molecular weight of 18 kDa; the larger one is a complex enzyme, such as keratinase produced by thermophilic anaerobic bacteria, whose molecular weight is up to kDa or more.

Efficient Degradation of Feather by Keratinase Producing Bacillus sp.

Keratinase has highly efficient keratin hydrolyzing activity. A huge amount of feather and leather wastes are generated every year as a by-product from the poultry and tannery industry due to continuous meat consumption worldwide.

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The production of keratinase by bacterial inoculums was studied by considering the media components and culture conditions.

There are several studies with Streptomyces species for protease production and also keratinase producer members of them have been described [6, 9]. Feather meal was the best substrate for keratinase and peptidase production in B.

The presence of tween 80 might be solved the waxy lipids on the wool surface in fermentation medium and thus improve the productivity by facilitation of the degradation process.

The clear zone forming isolates were producion as keratinase producer. The highest keratinase production In previous researches, keratinase production was performed by generally kerafinase microorganisms therefore; there are very limited studies about wool-degrading microorganisms [15, 21]. This yield was significantly higher than several of the keratinase producing bacterial species reported earlier but was comparable with Bacillus licheniformis PWD1 [ 1231 ].

This resistance is due to the constituent amino acid composition and configuration that provide structural rigidity. 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 ].

This article has been cited by other articles in PMC. The presence of the products of sulphitolysis such as peptides, cysteine, cysteine, and sulphate in the culture filtrate of MBF isolates confirmed the disulphide breakdown.