Year: 2014 | Month: July | Volume 7 | Special Issue
Study of Keratinolytic Activity of Thermophilic and Alkaliphilic Actinomycetes: Saccharomonospora Viridis SJ-21
Abstract:
Keratins are insoluble proteins from feathers, wool, silk, collagens, elastin, horn, hair and nail. They are not easily degraded by common proteolytic enzymes like trypsin, pepsin and papain.The resistant property of these compounds are due to their disulphide bonds, hydrogen bonds, salt linkages and cross linkages and hydrophobic interactions. Actinomycetes are known to digest keratins by synthesizing specific class of extracellular enzymes called alkaline thermo stable proteases which degrade keratin into small peptides that can be utilized by cell. Alkaline protease producing thermophilic actinomycete strain was screened from hot water spring of Tulsishyam Gujarat and was identified as Saccharomonospora viridis SJ-21 on the basis of colony characters, biochemical activity, spore nature, growth patterns and pigmentation and 16 S r RNA sequencing.The partially purified protease of Saccharomonospora viridis SJ-21 and the isolate itself were employed to check feather degradation. The feathers were degraded successfully within 72h at 45ºC. The degraded samples were analyzed for release of various amino acids by HPLC- Fluorescence with post column Derivatization. The aminoacids released were tyrosine, phenylalanine, leucine, valine, cysteine, arginine, methionine, etc. S. viridis SJ-21 is found having a significant keratinolytic activity and may serve dual purpose for degradation of poultry waste and production of amino acid rich feed supplement. The protein rich, concentrated feather meal can also be used for organic farming as semi-slow release, nitrogen fertilizer.
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