Nocardiopsis sp. SD5: A potent feather degrading rare actinobacterium isolated from feather waste in Tamil Nadu, India. (17th July 2013)
- Record Type:
- Journal Article
- Title:
- Nocardiopsis sp. SD5: A potent feather degrading rare actinobacterium isolated from feather waste in Tamil Nadu, India. (17th July 2013)
- Main Title:
- Nocardiopsis sp. SD5: A potent feather degrading rare actinobacterium isolated from feather waste in Tamil Nadu, India
- Authors:
- Saha, Subhasish
Dhanasekaran, D.
Shanmugapriya, S.
Latha, S. - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="jobm201200105-sec-0001" sec-type="section"> <p>Feather waste, generated in large quantities as a byproduct of commercial poultry processing, is nearly pure keratin protein, and keratin in its native state is not degradable by common proteolytic enzymes. The aim of the study was to find a potent feather degrading actinobacteria from feather waste soil. Out of 91 actinobacterial isolates recorded from feather waste soil in Tiruchirappalli and Nammakkal District, Tamil Nadu, India, isolate SD5 was selected for characterization because it exhibited significant keratinolytic activity. On the basis of the phenotypic, biochemical characterization and 16S rRNA gene‐sequencing studies, the isolate was identified as <italic>Nocardiopsis</italic> sp. SD5. Protease and keratinase activity of <italic>Nocardiopsis</italic> sp. SD5 were analyzed. The enzyme was more stable over the neutral pH and the temperature of 40 °C. The optimum temperature and pH for both proteolytic and keratinolytic activity was determined at 50 °C and pH 9, respectively. Enzyme inhibitors, detergents and chelator declined the enzyme activity with increasing concentration. Nondenaturing polyacrylamide gel electrophoresis and zymogram elucidated the presence of 30 and 60 kDa protease enzymes. These findings indicated that thermo alkaliphilic feather degrading strain <italic>Nocardiopsis</italic> sp. SD5 could<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="jobm201200105-sec-0001" sec-type="section"> <p>Feather waste, generated in large quantities as a byproduct of commercial poultry processing, is nearly pure keratin protein, and keratin in its native state is not degradable by common proteolytic enzymes. The aim of the study was to find a potent feather degrading actinobacteria from feather waste soil. Out of 91 actinobacterial isolates recorded from feather waste soil in Tiruchirappalli and Nammakkal District, Tamil Nadu, India, isolate SD5 was selected for characterization because it exhibited significant keratinolytic activity. On the basis of the phenotypic, biochemical characterization and 16S rRNA gene‐sequencing studies, the isolate was identified as <italic>Nocardiopsis</italic> sp. SD5. Protease and keratinase activity of <italic>Nocardiopsis</italic> sp. SD5 were analyzed. The enzyme was more stable over the neutral pH and the temperature of 40 °C. The optimum temperature and pH for both proteolytic and keratinolytic activity was determined at 50 °C and pH 9, respectively. Enzyme inhibitors, detergents and chelator declined the enzyme activity with increasing concentration. Nondenaturing polyacrylamide gel electrophoresis and zymogram elucidated the presence of 30 and 60 kDa protease enzymes. These findings indicated that thermo alkaliphilic feather degrading strain <italic>Nocardiopsis</italic> sp. SD5 could be used to control the feather waste pollution and to convert keratin rich feather waste into useful feedstock for poultry industry.</p> </sec> </abstract> … (more)
- Is Part Of:
- Journal of basic microbiology. Volume 53:issue 7(2013:Jul.)
- Journal:
- Journal of basic microbiology
- Issue:
- Volume 53:issue 7(2013:Jul.)
- Issue Display:
- Volume 53, Issue 7 (2013)
- Year:
- 2013
- Volume:
- 53
- Issue:
- 7
- Issue Sort Value:
- 2013-0053-0007-0000
- Page Start:
- 608
- Page End:
- 616
- Publication Date:
- 2013-07-17
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1521-4028 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jobm.201200105 ↗
- Languages:
- English
- ISSNs:
- 0233-111X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4951.125000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4196.xml