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International Journal of Agriculture, Environment & Biotechnology

Citation: IJAEB: 7 Special Issue : 479-488 July 2014

Microbiology

Study of Keratinolytic Activity of Thermophilic and

Alkaliphilic Actinomycetes: Saccharomonospora Viridis

SJ-21

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; shilpa_a_jani@yahoo.com

Absract

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.

Highlights

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).