Heterologous expression and purification of keratinase from Actinomadura viridilutea DZ50: feather biodegradation and animal hide dehairing bioprocesses

The keratin-degrading bacterium Actinomadura viridilutea DZ50 secretes a keratinase (KERDZ) with potential industrial interest. Here, the ker DZ gene was extracellularly expressed in Escherichia coli BL21(DE3)pLysS using pTrc99A vector. The recombinant enzyme (rKERDZ) was purified and biochemically ...

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Published in:	Environmental science and pollution research international Vol. 28; no. 8; pp. 9921 - 9934
Main Authors:	Ben Elhoul, Mouna, Zaraî Jaouadi, Nadia, Bouacem, Khelifa, Allala, Fawzi, Rekik, Hatem, Mechri, Sondes, Khemir Ezzine, Haifa, Miled, Neila, Jaouadi, Bassem
Format:	Journal Article
Language:	English
Published:	Berlin/Heidelberg Springer Berlin Heidelberg 01-02-2021 Springer Nature B.V
Subjects:	Actinomadura Actinomycetales Animals Aquatic Pollution Atmospheric Protection/Air Quality Control/Air Pollution Biochemical characteristics Biochemical oxygen demand Biochemistry Biodegradation Cattle Chemical oxygen demand Chemical reactions Collagen Dehairing E coli Earth and Environmental Science Ecotoxicology Environment Environmental Chemistry Environmental Health Environmental perception Environmental science Enzymes Feathers Fiber orientation Hair Hair removal Hides Keratin Keratinase Leather Oxygen demand Peptide Hydrolases Rabbits Research Article Scanning electron microscopy Sheep Sodium sulfide Sulfides Tannery wastes Waste Water Technology Wastewater Water Management Water Pollution Control Wool Keratinase Animal hide dehairing Feather degradation Leather industry Heterologous expression
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Summary:	The keratin-degrading bacterium Actinomadura viridilutea DZ50 secretes a keratinase (KERDZ) with potential industrial interest. Here, the ker DZ gene was extracellularly expressed in Escherichia coli BL21(DE3)pLysS using pTrc99A vector. The recombinant enzyme (rKERDZ) was purified and biochemically characterized. Results showed that the native and recombinant keratinases have similar biochemical characteristics. The conventional dehairing with lime and sodium sulfide degrades the hair to the extent that it cannot be recovered. Thus, these chemical processes become a major contributor to wastewater problem and create a lot of environmental concern. The complete dehairing was achieved with 2000 U/mL rKERDZ for 10 h at 40 °C. In fact, keratinase assisted dehairing entirely degraded chicken feather (45 mg) and removed wool/hair from rabbit, sheep, goat, or bovine’ hides (1.6 kg) while preserving the collagen structure. The enzymatic process is the eco-friendly option that reduces biological (BOD) (50%) and chemical (COD) oxygen demands (60%) in leather processing. Consequently, the enzymatic hair removal process could solve the problem of post-treatments encountering the traditional leather processing. The enzymatic (rKERDZ) dehaired leather was analyzed by scanning electron microscopic (SEM) studies, which revealed similar fiber orientation and compactness compared with control sample. Those properties support that the rKERDZ enzyme–mediated process is greener to some extent than the traditional one.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0944-1344 1614-7499
DOI:	10.1007/s11356-020-11371-1