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

A distinctive isolate was discovered and visually recognized as a member of the genus <i>Didymella</i> 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 <i>Didy...

Full description

Bibliographic Details
Main Authors: Osama Abdel-Hafeez Mohamed Al-Bedak, Ahmed Mohamed Moharram, Nemmat Abdel-Gawad Hussein, Doaa Mohamed Taha, Steven L. Stephenson, Fuad Ameen
Format: Article
Language:English
Published: MDPI AG 2023-05-01
Series:Fermentation
Subjects:
Online Access:https://www.mdpi.com/2311-5637/9/6/507
_version_ 1797594881913257984
author Osama Abdel-Hafeez Mohamed Al-Bedak
Ahmed Mohamed Moharram
Nemmat Abdel-Gawad Hussein
Doaa Mohamed Taha
Steven L. Stephenson
Fuad Ameen
author_facet Osama Abdel-Hafeez Mohamed Al-Bedak
Ahmed Mohamed Moharram
Nemmat Abdel-Gawad Hussein
Doaa Mohamed Taha
Steven L. Stephenson
Fuad Ameen
author_sort Osama Abdel-Hafeez Mohamed Al-Bedak
collection DOAJ
description A distinctive isolate was discovered and visually recognized as a member of the genus <i>Didymella</i> 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 <i>Didymella keratinophila</i> 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. Mn<sup>2+</sup> and K<sup>+</sup> 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.
first_indexed 2024-03-11T02:29:54Z
format Article
id doaj.art-9fa89831a51d4ea29e7009e6ff85da9f
institution Directory Open Access Journal
issn 2311-5637
language English
last_indexed 2024-03-11T02:29:54Z
publishDate 2023-05-01
publisher MDPI AG
record_format Article
series Fermentation
spelling doaj.art-9fa89831a51d4ea29e7009e6ff85da9f2023-11-18T10:20:44ZengMDPI AGFermentation2311-56372023-05-019650710.3390/fermentation9060507Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged FermentationOsama Abdel-Hafeez Mohamed Al-Bedak0Ahmed Mohamed Moharram1Nemmat Abdel-Gawad Hussein2Doaa Mohamed Taha3Steven L. Stephenson4Fuad Ameen5Assiut University Mycological Centre, Assiut University, Assiut 71511, EgyptAssiut University Mycological Centre, Assiut University, Assiut 71511, EgyptAssiut University Mycological Centre, Assiut University, Assiut 71511, EgyptAssiut University Mycological Centre, Assiut University, Assiut 71511, EgyptDepartment of Biological Sciences, University of Arkansas, Fayetteville, AR 72701, USADepartment of Botany & Microbiology, College of Science, King Saud University, Riyadh 11451, Saudi ArabiaA distinctive isolate was discovered and visually recognized as a member of the genus <i>Didymella</i> 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 <i>Didymella keratinophila</i> 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. Mn<sup>2+</sup> and K<sup>+</sup> 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.https://www.mdpi.com/2311-5637/9/6/507bioconversioncollagenase<i>Didymella</i>eco-friendlyfeatherkeratinase
spellingShingle Osama Abdel-Hafeez Mohamed Al-Bedak
Ahmed Mohamed Moharram
Nemmat Abdel-Gawad Hussein
Doaa Mohamed Taha
Steven L. Stephenson
Fuad Ameen
Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged Fermentation
Fermentation
bioconversion
collagenase
<i>Didymella</i>
eco-friendly
feather
keratinase
title Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged Fermentation
title_full Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged Fermentation
title_fullStr Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged Fermentation
title_full_unstemmed Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged Fermentation
title_short Microbial Exploitation of Feather Wastes for Sustainable Production of Keratinase and Collagenase Enzymes by <i>Didymella keratinophila</i> AUMC 15399 in Submerged Fermentation
title_sort microbial exploitation of feather wastes for sustainable production of keratinase and collagenase enzymes by i didymella keratinophila i aumc 15399 in submerged fermentation
topic bioconversion
collagenase
<i>Didymella</i>
eco-friendly
feather
keratinase
url https://www.mdpi.com/2311-5637/9/6/507
work_keys_str_mv AT osamaabdelhafeezmohamedalbedak microbialexploitationoffeatherwastesforsustainableproductionofkeratinaseandcollagenaseenzymesbyididymellakeratinophilaiaumc15399insubmergedfermentation
AT ahmedmohamedmoharram microbialexploitationoffeatherwastesforsustainableproductionofkeratinaseandcollagenaseenzymesbyididymellakeratinophilaiaumc15399insubmergedfermentation
AT nemmatabdelgawadhussein microbialexploitationoffeatherwastesforsustainableproductionofkeratinaseandcollagenaseenzymesbyididymellakeratinophilaiaumc15399insubmergedfermentation
AT doaamohamedtaha microbialexploitationoffeatherwastesforsustainableproductionofkeratinaseandcollagenaseenzymesbyididymellakeratinophilaiaumc15399insubmergedfermentation
AT stevenlstephenson microbialexploitationoffeatherwastesforsustainableproductionofkeratinaseandcollagenaseenzymesbyididymellakeratinophilaiaumc15399insubmergedfermentation
AT fuadameen microbialexploitationoffeatherwastesforsustainableproductionofkeratinaseandcollagenaseenzymesbyididymellakeratinophilaiaumc15399insubmergedfermentation