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Partial Characterization of Keratinolytic Activity of Local Novel Bacteria Isolated from Feather Waste

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TLDR
Three keratinolytic bacterial isolates were characterized partially for their keratinase activity and showed that keratinae activity of isolate A4 was optimum at 20% of ammonium sulphate, while B4 and B6 were more active at 70%.
Abstract
Three keratinolytic bacterial isolates were characterized partially for their keratinase activity. Bacterial isolates were grown in feather meal agar. Ammonium sulfate precipitation followed by dialysis was performed to know the bacterial isolate keratinase activity in differet pH and temperature. Identification of the bacteria was done by using their 16S rRNA gene sequences. The result showed that bacterial growth was coinciding with keratinase activity. Precipitation with ammonium sulfate showed that keratinae activity of isolate A4 was optimum at 20% of ammonium sulphate, while B4 and B6 were more active at 70%. Keratinase activity increased after dialysis. Keratinase of A4 showed to have optimum activity at temperature of 45oC and pH=8, B4 was optimum at temperature of 35oC and pH=7, while B6 was optimum at temperature of 40oC and pH=7, respectively. Identification of the bacterial isolates using 16S rRNA gen showed that A4, B4, and B6 were closed to Leclercia adecarboxylata strain M-X17B, Azotobacter chroococcum strain ABA-1, and Stenotrophomonas maltophilia strain BIW by 97%, 99%, and 98%, respectively. Two bacteria L. adecarboxylata and A. chroococcum were firstly reported to produce keratinase.

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Journal ArticleDOI

Keratinase Activity of A Newly Keratinolytic Bacteria, Azotobacter chroococcum B4

TL;DR: Based on the metal ion characteristics, this strain produced a serine-protease type of keratinase which may further studied for its application in the field.
References
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Journal ArticleDOI

Design and Evaluation of Useful Bacterium-Specific PCR Primers That Amplify Genes Coding for Bacterial 16S rRNA

TL;DR: PCR primers 63f and 1387r were found to be more useful for 16S rRNA gene amplification in ecological and systematic studies than PCR amplimers that are currently more generally used.
Journal ArticleDOI

Biochemical features of microbial keratinases and their production and applications.

TL;DR: Keratinases are exciting proteolytic enzymes that display the capability to degrade the insoluble protein keratin and their use in biomass conversion into biofuels may address the increasing concern on energy conservation and recycling.
Journal ArticleDOI

Bacterial Keratinases: Useful Enzymes for Bioprocessing Agroindustrial Wastes and Beyond

TL;DR: The use of keratinases to enhance drug delivery in some tissues and hydrolysis of prion proteins arise as novel outstanding applications for these enzymes.
Journal ArticleDOI

Characterization of a new keratinolytic bacterium that completely degrades native feather keratin.

TL;DR: A novel feather-degrading microorganism was isolated from poultry waste, producing a high keratinolytic activity when cultured on broth containing native feather, and complete feather degradation was achieved during cultivation.
Journal ArticleDOI

Keratinolytic bacteria isolated from feather waste

TL;DR: The keratinase activity was detected during growth, but the complete degradation of these substrates was not always achieved, and the keratinases were similar in keratin hydrolysis when compared with commercially available microbial peptidases.
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