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 cystine levels reached peak by days with The degradation started with the adhesion of the bacteria to the feather. Hence, microbial and biotechnological productoon could be a promising and better alternative to keratin and keratinous wastes recycling by enzymatic action using specific enzyme of microorganism namely keratinase Mehta et al.
The bulk of feather waste is poorly recycled in nature and enzyne limited utility due to the chemically unreactive nature of keratin. There was a gradual increase in the concentration of cysteine from 2. Preparation of Inoculum Streptomyces sp. Keratinase has highly efficient keratin hydrolyzing activity. In agriculture, keratinase produced by microorganisms can degrade keratin into polypeptides and amino acids, which can be used to make organic fertilizers.
Discussion The demand of keratinolytic proteases is still increasing due to its potential usage in productino industries. 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.
Three Bacillus species B. A08 Pereira et al.
There was a 1. In the Bacillus genus a secreted metallopeptidase has been described by Werlang and Brandelli [ 37 ]. Tween 80 in two producrion concentrations 0. By this way, the shrink proofing of wool surface can be obtained. Its enzymes could be used as additives in animal feed to improve feather meal digestibility.
Similarly, preferred pH 8. Optimization of cultural condition for keratinase production using Bacillus cereus TS1. Isolation and identification of feather degrading bacteria from feather dumped soil.
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 proxuction enzymes by three Bacillus spp. 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 .
The significant differences between untreated and enzyme treated fibers could be seen clearly from Fig b and c. Properties The molecular weight of keratinase that has been isolated and purified is quite different, ranging from dozens of kDa to several hundred kDa. Degradation of feather shaft was achieved by the fifth day and the substrate was enzjme degraded into white powdery mass by the seventh day.
In this study, to facilitate the usage of wool by the Streptomyces sp. Website Search Exact Search Search. For example, some forms of keratinase exist mainly in the cell, and some of them are mainly secreted to the outside.
Feather and feather meal were used in a submerged fermentation in order to obtain the peptidases. Isolation of a novel feather-degrading bacterium and optimization of its cultural conditions for enzyme production. A potential beta-keratin degrading bacteria from Vellore Emu feather enzjme soil. Extracellular keratinases of other Bacillus such as B. In the present work, the production of keratinases and peptidases by three Bacillus species isolated from poultry waste was investigated.
It oroduction degrades insoluble proteins including feathers, wool, keratin, human hair, and nails.
International Journal of Microbiology
Processing textile fibers with enzymes: Among 44 tested bacterial isolates, 27 were found as keratinase producers based on their clear zones formation on skim milk agar and feather meal agar media.
Effect of different substrates on keratinase production by Arthrobacter sp. The tendency of the medium to turn alkaline has been attributed to deamination reactions leading to production of ammonia from protein, peptides, and amino acids during keratin prodjction.
Feather meal was the best substrate for keratinase production with B. Production and characterisation of feather degrading keratinase from Bacillus sp. The yield of enzyme was keratinass increased Thus, the present study is a step forward in the process of production of indigenous keratinase enzyme.
NFH5 with other selected members of Arthrobacter sp. Enzyme production was monitored according to the keratinase activity.
Microbial Keratinase Production and Application to Improve the Properties of Wool Fabrics
The three Bacillus spp. An enayme and attractive method for improving the digestibility of feathers or feather meal is biodegradation by keratinolytic microorganisms [ 89 ]. View at Google Scholar R.
Biochemical features of microbial keratinases and their production and applications, Appl. Electronic supplementary material The online version of this article doi: Isolation, Selection, and Characterization of Keratinolytic Bacillus sp. Finally, the fabric was rinsed several times with deionized water to remove any remaining enzyme from the treatment.
Then the effects of different culture parameters were standardised.
Results suggest that, the keratinase produced from raw wool is feasible for processing of wool fabrics in textile industry. 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.
Efficient Degradation of Feather by Keratinase Producing Bacillus sp.
The reaction mixtures contain 1. Subsequently dyeing, the fabrics were rinsed with water and then dried at room temperature. Enhancing the Keratinase Production In the first part of this study the keratinase production from Streptomyces sp.