The aim of the current study was to isolate keratinolytic bacteria from the soil samples collected from different feather processing areas in Vellore, TN, India. The isolation was performed by serial dilution and plating method. Total eight bacteria were isolated from the collected soil samples. All isolates were screened for keratinolytic activity by Casein agar plate method, among eight bacterial isolates only one (H5) isolate showed the keratinolytic activity in Casein agar medium. H5 isolate (potential strain) was identified as Bacillus sp. by microscopic and biochemical experiments. The best enzyme activity was observed at pH 7 and temperature 30ºC. Keywords: Keratinolytic; Spread plate method; Bacillus sp.; Bacteria. © 2010 JSR Publications. ISSN: 2070-0237 (Print); 2070-0245 (Online). All rights reserved. DOI: 10.3329/jsr.v2i3.4567 J. Sci. Res. 2 (3), 559-565 (2010)

H prasad v

G kumar

L kartik

Br kv

Fulltext

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Journal of Scientific Research

The study was planned to screen the marine actinobacterial extract for the protease inhibitor activity and its anti- Pf activity under in vitro and in vivo conditions. Out of 100 isolates, only 3 isolates exhibited moderate to high protease inhibitor activities on trypsin, chymotrypsin and proteinase K. Based on protease inhibitor activity 3 isolates were chosen for further studies. The potential isolate was characterized by polyphasic approach and identified as Streptomyces sp LK3 (JF710608). The lead compound was identified as peptide from Streptomyces sp LK3. The double-reciprocal plot displayed inhibition mode is non-competitive and it confirms the irreversible nature of protease inhibitor. The peptide from Streptomyces sp LK3 extract showed significant anti plasmodial activity (IC50: 25.78 μg/ml). In in vivo model, the highest level of parasitemia suppression (≈45%) was observed in 600 mg/kg of the peptide. These analyses revealed no significant changes were observed in the spleen and liver tissue during 8 dpi. The results confirmed up-regulation of TGF-β and down regulation of TNF-α in tissue and serum level in PbA infected peptide treated mice compared to PbA infection. The results obtained infer that the peptide possesses anti- Pf activity activity. It suggests that the extracts have novel metabolites and could be considered as a potential source for drug development. © 2014 Karthik et al.

PLoS ONE

Protease inhibitors from marine actinobacteria as a potential source for antimalarial compound

Microbiological Research

Keratinolytic activity of Bacillus megaterium F7-1, a feather-degrading mesophilic bacterium

International Journal of Poultry Science

Production of an Extra Cellular Feather Degrading Enzyme by Bacillus licheniformis Isolated from Poultry Farm Soil in Namakkal District (Tamilnadu)

Journal of Zhejiang University SCIENCE B

Keratinase production and keratin degradation by a mutant strain of Bacillus subtilis

Brazilian Journal of Microbiology

Keratinolytic bacteria isolated from feather waste

Screening of Extracellular Keratinase Producing Bacteria from Feather Processing Areas in Vellore, Tamil Nadu, India

Journal	Journal of Scientific Research
Publisher	Bangladesh Journals Online (JOL)
ISSN	2070-0237
Open Access	Yes