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Partial purification of keratinase from Actinomycetes screened from surrounding places of VIT University for industrial applications | Abstract
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Abstract

Partial purification of keratinase from Actinomycetes screened from surrounding places of VIT University for industrial applications

Author(s): Suneetha V. and Kiran Kumar Vuppu

Enzymes being efficient as biocatalysts are being increasingly employed as replacements or additions for varied applications in various industries. The development of microbial keratinase can play a vital role in various other industries also. Keratinous waste in the form of feathers, which is nearly pure keratin is generated in bulk quantities in commercial poultry processing. Enzymes produced are either intracellular or extra-cellular. Extra-cellular enzymes are secreted into the medium whereas the intracellular enzymes need to be released into medium by cell disruption. In our study the recovery of Keratinase from six strains from Actinomycetes in general involves separation of biomass from the broth by filtration or by centrifugation, followed by precipitation of protein by salt or organic solvents to get a partially purified enzyme. Further steps of purification are selected depending upon the purity of the required product and its application, as recovery cost of a microbial product can vary from as low as 25% to as high as 70% of the total manufacturing costs depending on the level of purity desired for the final product The Polyacrylamide gel showed single bands in all the cases indicating homogenous nature of enzyme with one subunit. The molecular weights of the enzyme were in the range of 30 kDa for KLH104, 34-35 kDa for KLH99 and 43-45 kDa for KLF3, KLF10, KLF14 and KLF16 strains.


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