A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55

A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55. The synthesis of keratinases by psychrophilic and psychrotolerant microorganisms has not received much attention, despite the fact that they can be an effective stand-in for substrate conversion at a low energy cost. In this study, some psychrophilic fungi isolated from three cold storage locations near Riyadh, Saudi Arabia, were tested for their cold-active keratinase potential. Penicillium lanosocoeruleum , a recently isolated fungus from Saudi Arabia, was the potent strain that produced cold-active keratinase. The Penicillium species was identified using sequencing of the internal transcribed spacer region (ITS). The generation of cold-active keratinase by P. lanosocoeruleum KSA-55 was optimized by two factors at time (TFAT). At pH 9.0 and 15°C, the keratinase activity was 28.9 ± 2.8 U/mL/min which increased to 41.7 ± 3.8 U/mL/min after 6 d of fermentation using peptone as a nitrogen source. The produced keratinase was chromatographed by MP 800 anion exchange resin and Sephadex G 100 size exclusion gel. At pH 9.0 and 10°C, the pure keratinase displayed the maximum specific activity of 210.3 ± 8.4 U/mg. Zn 2+ , Fe 2+ , ethylenediaminetetraacetic acid (EDTA), sodium dodecyl sulfate (SDS), and phenylmethanesulfonyl fluoride (PMSF), demonstrated severe inhibitory effects on the keratinase activity. Mn 2+ ions activated the keratinase by 166.85 ± 15.6%. PMSF significantly reduced keratinase activity. P. lanosocoeruleum strain KSA-55 is presented here as a new prospective producer of cold-active keratinase for a variety of biotechnological uses, including the management of keratinous waste in the poultry industry, cosmetics, and medical applications. How to cite: Alhomaidi E. A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55. Electron J Biotechnol 2025;74. https://doi.org/10.1016/j.ejbt.2024.10.003 .

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Publication Details

Journal
Electronic Journal of Biotechnology
Published
2024-12-20
DOI
https://doi.org/10.1016/j.ejbt.2024.10.003
Citations
3
Primary Topic
Enzyme Production and Characterization
Type
article
Field-Weighted Citation Impact
1.16

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article

A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55

Eman Alhomaidi
3 citations
Electronic Journal of Biotechnology
Enzyme Production and Characterization
1.16
article

A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55

Eman Alhomaidi
article en
3 citations

Abstract

A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55. The synthesis of keratinases by psychrophilic and psychrotolerant microorganisms has not received much attention, despite the fact that they can be an effective stand-in for substrate conversion at a low energy cost. In this study, some psychrophilic fungi isolated from three cold storage locations near Riyadh, Saudi Arabia, were tested for their cold-active keratinase potential. Penicillium lanosocoeruleum , a recently isolated fungus from Saudi Arabia, was the potent strain that produced cold-active keratinase. The Penicillium species was identified using sequencing of the internal transcribed spacer region (ITS). The generation of cold-active keratinase by P. lanosocoeruleum KSA-55 was optimized by two factors at time (TFAT). At pH 9.0 and 15°C, the keratinase activity was 28.9 ± 2.8 U/mL/min which increased to 41.7 ± 3.8 U/mL/min after 6 d of fermentation using peptone as a nitrogen source. The produced keratinase was chromatographed by MP 800 anion exchange resin and Sephadex G 100 size exclusion gel. At pH 9.0 and 10°C, the pure keratinase displayed the maximum specific activity of 210.3 ± 8.4 U/mg. Zn 2+ , Fe 2+ , ethylenediaminetetraacetic acid (EDTA), sodium dodecyl sulfate (SDS), and phenylmethanesulfonyl fluoride (PMSF), demonstrated severe inhibitory effects on the keratinase activity. Mn 2+ ions activated the keratinase by 166.85 ± 15.6%. PMSF significantly reduced keratinase activity. P. lanosocoeruleum strain KSA-55 is presented here as a new prospective producer of cold-active keratinase for a variety of biotechnological uses, including the management of keratinous waste in the poultry industry, cosmetics, and medical applications. How to cite: Alhomaidi E. A sustainable exploitation of high-protein feather waste for production of cold-adapted keratinase by Penicillium lanosocoeruleum KSA-55. Electron J Biotechnol 2025;74. https://doi.org/10.1016/j.ejbt.2024.10.003 .

Electronic Journal of BiotechnologyVol. 74
Princess Nourah bint Abdulrahman University (SA)
Princess Nourah Bint Abdulrahman University
Responsible consumption and production
Openalex Percentile: Top 21%
Enzyme Production and Characterization
1.16
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