The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles

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Abstract

Billions of tons of keratin bio-wastes are generated by poultry industry annually but discarded that result in serious environmental pollution. Keratinase is a broad spectrum protease with the unique ability to degrade keratin, providing an eco-friendly way to convert keratin wastes to valuable amino acids. In this report, a feather-degrading thermophilic bacterium, Meiothermus taiwanensis WR-220, was investigated due to its ability to apparently complete feather decay at 65 °C in two days. By genomics, proteomics, and biochemical approaches, the extracellular heat-stable keratinase (MtaKer) from M. taiwanensis WR-220 was identified. The recombinant MtaKer (rMtaKer) possesses keratinolytic activities at temperatures ranging from 25 to 75 °C and pH from 4 to 11, with a maximum keratinolytic activity at 65 °C and pH 10. The phylogenetic and structural analysis revealed that MtaKer shares low sequence identity but high structural similarity with known keratinases. Accordingly, our findings have enabled the discovery of more keratinases from other extremophiles, Thermus and Deinococcus. Proteins encoded in the extremophiles shall be evolved to be functional in the extreme conditions. Hence, our study expands the current boundary of hunting keratinases that can tolerate extreme conditions for keratin wastes biorecycle and other industrial applications.

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Subtilases: the superfamily of subtilisin-like serine proteases.

Roland J. Siezen, J D Leunissen (1997)

Subtilases are members of the clan (or superfamily) of subtilisin-like serine proteases. Over 200 subtilases are presently known, more than 170 of which with their complete amino acid sequence. In this update of our previous overview (Siezen RJ, de Vos WM, Leunissen JAM, Dijkstra BW, 1991, Protein Eng 4:719-731), details of more than 100 new subtilases discovered in the past five years are summarized, and amino acid sequences of their catalytic domains are compared in a multiple sequence alignment. Based on sequence homology, a subdivision into six families is proposed. Highly conserved residues of the catalytic domain are identified, as are large or unusual deletions and insertions. Predictions have been updated for Ca(2+)-binding sites, disulfide bonds, and substrate specificity, based on both sequence alignment and three-dimensional homology modeling.

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Microbial keratinases and their prospective applications: an overview.

P. Ramnani, Rani Gupta (2006)

Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide "keratin" recalcitrant to the commonly known proteolytic enzymes trypsin, pepsin and papain. These enzymes are largely produced in the presence of keratinous substrates in the form of hair, feather, wool, nail, horn etc. during their degradation. The complex mechanism of keratinolysis involves cooperative action of sulfitolytic and proteolytic systems. Keratinases are robust enzymes with a wide temperature and pH activity range and are largely serine or metallo proteases. Sequence homologies of keratinases indicate their relatedness to subtilisin family of serine proteases. They stand out among proteases since they attack the keratin residues and hence find application in developing cost-effective feather by-products for feed and fertilizers. Their application can also be extended to detergent and leather industries where they serve as specialty enzymes. Besides, they also find application in wool and silk cleaning; in the leather industry, better dehairing potential of these enzymes has led to the development of greener hair-saving dehairing technology and personal care products. Further, their prospective application in the challenging field of prion degradation would revolutionize the protease world in the near future.

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Extremophiles as a source for novel enzymes.

Bertus Van den Burg (2003)

Microbial life does not seem to be limited to specific environments. During the past few decades it has become clear that microbial communities can be found in the most diverse conditions, including extremes of temperature, pressure, salinity and pH. These microorganisms, called extremophiles, produce biocatalysts that are functional under extreme conditions. Consequently, the unique properties of these biocatalysts have resulted in several novel applications of enzymes in industrial processes. At present, only a minor fraction of the microorganisms on Earth have been exploited. Novel developments in the cultivation and production of extremophiles, but also developments related to the cloning and expression of their genes in heterologous hosts, will increase the number of enzyme-driven transformations in chemical, food, pharmaceutical and other industrial applications.

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Contributors

Meng-Chiao Ho:

ORCID: http://orcid.org/0000-0002-5424-4524

joeho@gate.sinica.edu.tw

Shih-Hsiung Wu: shwu@gate.sinica.edu.tw

Journal

Journal ID (nlm-ta): Sci Rep

Journal ID (iso-abbrev): Sci Rep

Title: Scientific Reports

Publisher: Nature Publishing Group UK (London )

ISSN (Electronic): 2045-2322

Publication date (Electronic): 5 July 2017

Publication date PMC-release: 5 July 2017

Publication date Collection: 2017

Volume: 7

Electronic Location Identifier: 4658

Affiliations

[1 ]ISNI 0000 0001 2287 1366, GRID grid.28665.3f, Institute of Biological Chemistry, , Academia Sinica, ; Taipei, 11529 Taiwan

[2 ]ISNI 0000 0004 0573 0416, GRID grid.412146.4, General Education Center, , National Taipei University of Nursing and Health Sciences, ; Taipei, 11219 Taiwan

[3 ]ISNI 0000 0004 0546 0241, GRID grid.19188.39, Institute of Biochemical Sciences, College of Life Sciences, , National Taiwan University, ; Taipei, 10617 Taiwan

[4 ]ISNI 0000 0004 0546 0241, GRID grid.19188.39, Department of Chemistry, , National Taiwan University, ; Taipei, 10617 Taiwan

[5 ]ISNI 0000 0001 2287 1366, GRID grid.28665.3f, Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, , Academia Sinica, ; Taipei, 11529 Taiwan

Author information

Meng-Chiao Ho http://orcid.org/0000-0002-5424-4524

Article

Publisher ID: 4723

DOI: 10.1038/s41598-017-04723-4

PMC ID: 5498600

PubMed ID: 28680127

SO-VID: 8b8949d1-755a-4810-a12d-580d23adc93d

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Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

History

Date received : 27 February 2017

Date accepted : 18 May 2017

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The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles

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Hematology and Oncology Discovery

Most cited references 40

Subtilases: the superfamily of subtilisin-like serine proteases.

Microbial keratinases and their prospective applications: an overview.

Extremophiles as a source for novel enzymes.

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