EventsMOL2NET'20, Conference on Molecular, Biomed., Comput. & Network Science and Engineering, 6th ed.
Event submissions
Published
with-doi10.3390/mol2net-06-06856 (registering DOI)
This submission belongs to the session 01. CHEMBIOMOL-06: Chem. Biol. & Med. Chem. Workshop, Bilbao-Rostock, Germany-Galveston, Texas, USA, 2020 of the event MOL2NET'20, Conference on Molecular, Biomed., Comput. & Network Science and Engineering, 6th ed.
Published date
05 Jun, 2020
Citation
Sondes MECHRI, Khelifa Bouacem, Meriam Amziane, Ahlem Dab, Farida Nateche, Bassem Jaouadi, Purification, biochemical characterization, and molecular elucidation of a new biotechnologically compatible serine peptidase from Virgibacillus natechei strain FarDT, in Proceedings of MOL2NET'20, Conference on Molecular, Biomed., Comput. & Network Science and Engineering, 6th ed., 30 January 2020–30 January 2021, MDPI: Basel, Switzerland, doi: 10.3390/mol2net-06-06856
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Purification, biochemical characterization, and molecular elucidation of a new biotechnologically compatible serine peptidase from Virgibacillus natechei strain FarDT

Sondes MECHRI 1
Khelifa Bouacem 1,2
Meriam Amziane 3
Ahlem Dab 1
Farida Nateche 3
Bassem Jaouadi 1
1. Laboratory of Microbial Biotechnology, Enzymatic, and Biomolecules (LMBEB), Centre of Biotechnology of Sfax (CBS), University of Sfax, P.O. Box 1177, Sfax 3018, Tunisia
2. Laboratory of Cellular and Molecular Biology (LCMB), Microbiology Team, Faculty of Biological Sciences, University of Sciences and Technology of Houari Boumediene (USTHB), PO Box 32, El Alia, Bab Ezzouar, 16111 Algiers, Algeria
3. Laboratory of Cellular and Molecular Biology (LCMB), Microbiology Team, Faculty of Biological Sciences, University of Sciences and Technology of Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, 16111 Algiers, Algeria
Abstract

A new peptidase designated as SAPV produced from a moderately halophilic Virgibacillus natechei sp. nov., strain FarDT was investigated by purification to homogeneity followed by biochemical and molecular characterization purposes. Through optimization, it was determined that the optimum peptidase activity to be 16,000 U/mL in the optimized liquid medium that contains only white shrimp shell by-product as sole energy and carbon sources. The SAPV enzyme is a monomer protein with a molecular mass of 31 kDa. The sequence of its NH2-terminal amino-acid residues showed homology with those of Bacillus peptidases S8/S53 superfamily. The SAPV showed optimal activity at pH 9 and 60 °C. The sapV gene was cloned, sequenced, and heterologously over expressed in the extracellular fraction of E. coli BL21(DE3)pLysS. The biochemical properties of the recombinant peptidase (rSAPV) were similar to those of native one. The highest sequence identity value (97.66%) of SAPV was obtained with peptidase S8 from Virgibacillus massiliensis DSM 28587, with 9 amino-acid residues of difference. Interestingly, rSAPV exhibited an excellent detergent stability and compatibility than Alcalase 2.4 L FG and Bioprotease N100L

Keywords
Peptidase
Virgibacillus natechei
Moderately halophilic
Heterologous expression
Organic solvents
Detergent.
Manuscript
Manuscript_MOL2NET_1_2020.pdf
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