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Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation
Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation
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Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation
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Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation
Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation

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Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation
Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation
Journal Article

Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by Didymella keratinophila AUMC 15399 in Submerged Fermentation

2023
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Overview
A distinctive isolate was discovered and visually recognized as a member of the genus Didymella during a routine examination of Coelomycetes isolated from diverse fruit juices. Based on sequencing of the internal transcribed spacer (ITS), the fungus was identified as Didymella keratinophila since it showed a 100% identity to the type strain. The strain thrived and produced keratinase and collagenase enzymes by hydrolyzing native chicken feathers in submerged fermentation (SmF). After 10 days of fermentation at 30 °C, pH 9 using sodium nitrate as a nitrogen supply produced the highest keratinase activity of 8780 ± 620 U/mL/min, while pH 6 and beef extract produced the maximum collagenase activity of 11,230 ± 1290 U/mL/min. The partially-purified keratinase enzyme worked best at pH 7.0 and 45 °C, exhibiting a specific activity of 44,903 ± 1555 U/mg protein. The activity of the partially-purified collagenase enzyme was excellent at pH 6.0 at 35 °C, generating 15,753 ± 110 U/mg enzyme-specific activity. Mn2+ and K+ were the most efficient inhibitors of keratinases and collagenase, respectively. Both EDTA and metal ions significantly decreased the activity of keratinase and collagenase. This report identified a workable supplier of collagenase and keratinase enzymes derived from chicken feathers, offering a reliable way to exploit and manage these wastes for obtaining high-value products.