Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin

Acinetobacter baumannii is a ubiquitous bacteria that is increasingly becoming a formidable nosocomial pathogen. Due to its clinical relevance, studies on the bacteria’s secretory molecules especially extracellular proteases are of interest primarily in relation to the enzyme’s role in virulence. Be...

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Main Authors: Muhammed, N. S., Hussin, N. F., Lim, A. S., Jonet, M. A., Mohamad, S. E., Jamaluddin, H.
Format: Article
Language:English
Published: Springer 2021
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Online Access:http://eprints.utm.my/id/eprint/94638/1/NurSyafiqahMuhammed2021_RecombinantProductionandCharacterization.pdf
http://eprints.utm.my/id/eprint/94638/
http://dx.doi.org/10.1007/s10930-021-09986-5
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spelling my.utm.946382022-03-31T15:13:30Z http://eprints.utm.my/id/eprint/94638/ Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin Muhammed, N. S. Hussin, N. F. Lim, A. S. Jonet, M. A. Mohamad, S. E. Jamaluddin, H. Q Science (General) Acinetobacter baumannii is a ubiquitous bacteria that is increasingly becoming a formidable nosocomial pathogen. Due to its clinical relevance, studies on the bacteria’s secretory molecules especially extracellular proteases are of interest primarily in relation to the enzyme’s role in virulence. Besides, favorable properties that extracellular proteases possess may be exploited for commercial use thus there is a need to investigate extracellular proteases from Acinetobacter baumannii to gain insights into their catalytic properties. In this study, an extracellular subtilisin-like serine protease from Acinetobacter baumannii designated as SPSFQ that was isolated from fermented food was recombinantly expressed and characterized. The mature catalytically active form of SPSFQ shared a high percentage sequence identity of 99% to extracellular proteases from clinical isolates of Acinetobacter baumannii and Klebsiella pneumoniae as well as a moderately high percentage identity to other bacterial proteases with known keratinolytic and collagenolytic activity. The homology model of mature SPSFQ revealed its structure is composed of 10 β-strands, 8 α-helices, and connecting loops resembling a typical architecture of subtilisin-like α/β motif. SPSFQ is catalytically active at an optimum temperature of 40 °C and pH 9. Its activity is stimulated in the presence of Ca2+ and severely inhibited in the presence of PMSF. SPSFQ also displayed the ability to degrade several tissue-associated protein substrates such as keratin, collagen, and fibrin. Accordingly, our study shed light on the catalytic properties of a previously uncharacterized extracellular serine protease from Acinetobacter baumannii that warrants further investigations into its potential role as a virulence factor in pathogenicity and commercial applications. Springer 2021 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/94638/1/NurSyafiqahMuhammed2021_RecombinantProductionandCharacterization.pdf Muhammed, N. S. and Hussin, N. F. and Lim, A. S. and Jonet, M. A. and Mohamad, S. E. and Jamaluddin, H. (2021) Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin. Protein Journal, 40 (3). ISSN 1572-3887 http://dx.doi.org/10.1007/s10930-021-09986-5 DOI: 10.1007/s10930-021-09986-5
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic Q Science (General)
spellingShingle Q Science (General)
Muhammed, N. S.
Hussin, N. F.
Lim, A. S.
Jonet, M. A.
Mohamad, S. E.
Jamaluddin, H.
Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
description Acinetobacter baumannii is a ubiquitous bacteria that is increasingly becoming a formidable nosocomial pathogen. Due to its clinical relevance, studies on the bacteria’s secretory molecules especially extracellular proteases are of interest primarily in relation to the enzyme’s role in virulence. Besides, favorable properties that extracellular proteases possess may be exploited for commercial use thus there is a need to investigate extracellular proteases from Acinetobacter baumannii to gain insights into their catalytic properties. In this study, an extracellular subtilisin-like serine protease from Acinetobacter baumannii designated as SPSFQ that was isolated from fermented food was recombinantly expressed and characterized. The mature catalytically active form of SPSFQ shared a high percentage sequence identity of 99% to extracellular proteases from clinical isolates of Acinetobacter baumannii and Klebsiella pneumoniae as well as a moderately high percentage identity to other bacterial proteases with known keratinolytic and collagenolytic activity. The homology model of mature SPSFQ revealed its structure is composed of 10 β-strands, 8 α-helices, and connecting loops resembling a typical architecture of subtilisin-like α/β motif. SPSFQ is catalytically active at an optimum temperature of 40 °C and pH 9. Its activity is stimulated in the presence of Ca2+ and severely inhibited in the presence of PMSF. SPSFQ also displayed the ability to degrade several tissue-associated protein substrates such as keratin, collagen, and fibrin. Accordingly, our study shed light on the catalytic properties of a previously uncharacterized extracellular serine protease from Acinetobacter baumannii that warrants further investigations into its potential role as a virulence factor in pathogenicity and commercial applications.
format Article
author Muhammed, N. S.
Hussin, N. F.
Lim, A. S.
Jonet, M. A.
Mohamad, S. E.
Jamaluddin, H.
author_facet Muhammed, N. S.
Hussin, N. F.
Lim, A. S.
Jonet, M. A.
Mohamad, S. E.
Jamaluddin, H.
author_sort Muhammed, N. S.
title Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
title_short Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
title_full Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
title_fullStr Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
title_full_unstemmed Recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
title_sort recombinant production and characterization of an extracellular subtilisin-like serine protease from acinetobacter baumannii of fermented food origin
publisher Springer
publishDate 2021
url http://eprints.utm.my/id/eprint/94638/1/NurSyafiqahMuhammed2021_RecombinantProductionandCharacterization.pdf
http://eprints.utm.my/id/eprint/94638/
http://dx.doi.org/10.1007/s10930-021-09986-5
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