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Research Article
Jiang-Shiou Hwang
National Taiwan Ocean University
Corresponding Author
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Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 ℃) ranges, with maximal hydrolytic activities at pH 10 and at 50 ℃ temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non- anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicate that the protein is suitable for waste management and value-added product synthesis as well as several research applications.
Keywords
Bacillus cereus, natural product, subtilase, SLSP-k, extremophile, keratin
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CURRENT STATUS: Under Review
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Posted 28 Dec, 2020
No community comments so far
Editorial decision: Major revision
On 16 Feb, 2021
Reviews received
Received 11 Feb, 2021
Reviews received
Received 27 Jan, 2021
Reviewers agreed
On 16 Jan, 2021
Reviewers agreed
On 14 Jan, 2021
Reviewers invited
Invitations sent on 11 Jan, 2021
Editor assigned
On 11 Jan, 2021
Editor invited
On 24 Dec, 2020
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On 24 Dec, 2020
First submitted
On 08 Dec, 2020
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This preprint is under consideration at Scientific Reports. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
Jiang-Shiou Hwang
National Taiwan Ocean University
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 28 Dec, 2020
No community comments so far
Editorial decision: Major revision
On 16 Feb, 2021
Reviews received
Received 11 Feb, 2021
Reviews received
Received 27 Jan, 2021
Reviewers agreed
On 16 Jan, 2021
Reviewers agreed
On 14 Jan, 2021
Reviewers invited
Invitations sent on 11 Jan, 2021
Editor assigned
On 11 Jan, 2021
Editor invited
On 24 Dec, 2020
Submission checks complete
On 24 Dec, 2020
First submitted
On 08 Dec, 2020
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 ℃) ranges, with maximal hydrolytic activities at pH 10 and at 50 ℃ temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non- anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicate that the protein is suitable for waste management and value-added product synthesis as well as several research applications.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
This is a list of supplementary files associated with this preprint. Click to download.
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