International Journal of Agriculture, Environment & Biotechnology
Citation: IJAEB: 7 Special Issue : 479-488 July 2014
©2014 New Delhi Publishers. All rights reserved
Study of Keratinolytic Activity of Thermophilic and
Alkaliphilic Actinomycetes: Saccharomonospora Viridis
Shilpa Jani 1 and Harshad Patel 2
1 Microbiology Department, J and J college of Science, Nadiad, Gujarat, India.
2 Microbiology Department,V.P. and R.P.T.P Science College, Vallabh Vidyanagar,Gujarat, India.
Corresponding author: Shilpa Jani; firstname.lastname@example.org
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.
Screening of alkaline protease producing thermophilic actinomycetes .
Identification of the potent protease producing thermophilic actinomycete.
Alkaline Protease production and characterization
Checking feather degrading capacity of isolate and protease produced by the isolate.
Amino acid profiling of degraded feather sample by HPLC.
Keratin occurs in nature mainly in the form of hair, horn,
carpet beetles and chewing lice are known to digest
nails, feathers and cornified tissue. Keratin by virtue of
keratin (Riffel, A, 2007). They hydrolyze the keratin by
its insolubility and resistance to proteolytic enzymes is
synthesizing specific class of extracellular enzymes called
not attacked by most of living organisms. Nevertheless,
alkaline thermostable proteases which degrade keratin
keratin does not accumulate in the nature and therefore
into small peptides that can be utilized by cells. Several
biological agencies may be presumed to accomplish its
feather-degrading bacteria have been isolated from soil,
removal (Laemmli, U. K., 1970). Along with bacteria
poultry wastes, hair debris and animal skin and most of
and fungi, some insects, including cloth mouth larvae,
the isolates were confined to genera Streptomyces and
Bacillus (Dalev, P. (1990).