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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
Published: 05 June 2020 by MDPI in MOL2NET'20, Conference on Molecular, Biomed., Comput. & Network Science and Engineering, 6th ed. congress CHEMBIOMOL-06: Chem. Biol. & Med. Chem. Workshop, Bilbao-Rostock, Germany-Galveston, Texas, USA, 2020
https://doi.org/10.3390/mol2net-06-06856 (registering DOI)
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.
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Comments on this paper
Humbert G. Díaz
9 January 2021
Bioinformatics Evolutionary study and Biotechnology applications
Dear authors, thank you for submitting this very interesting paper, couple of post-publication questions here.

Have you considered to do an accelerated mutation evolutionary study to detect mutants of this enzyme with improved activity, is it possible in this case?

WHat are the potential applications of this enzyme in Biotechnology?
Bassem JAOUADI
11 January 2021
I would like to express my sincere gratitude to Prof. Dr. Humbert G. Díaz for this interest about this short publication. I’m glad to learn that he has found my paper interesting. Regarding your comment, the authors are very interested in creating mutants and docking studies to determine the involvement of some key amino-acids residues in the physico-chemical and catalytic properties of this kind of enzyme.

SAPV showed an outstanding and high resistance to several organic solvents. Furthermore, this peptidase exhibited an excellent detergent stability and compatibility. Accordingly, SAPV enzyme could be a promising potential candidate for future applications in detergent formulations.


Sondes.


Dr. MECHRI Sondes

Assistante contractuelle en Biochimie à l'Université de Gabés, Institut supérieur de Biologie Appliquée de Médenine (ISBAM)
Département Génie Biologique, Route El Jorf Km 22,5 - Médenine 4119. Site web: http://www.isbam.rnu.tn
Chercheuse au Centre de Biotechnologie de Sfax (CBS), Université de Sfax,
Laboratoire de Biotechnologie Microbienne, Enzymatique et de Biomolécules (LBMEB), Route Sidi Mansour km 6,
BP 1177 - Sfax 3018. Site web: http://www.cbs.rnrt.tn
Humbert G. Díaz
11 January 2021
formulation & toxicity testing
Dear Dr. MECHRI Sondes thank you for your answer, couple of questions.

Have been these results already published in a journal or only the early communication presented here?

What could be the formulation type for detergents using SAPV enzyme, powder, nanoparticle-sized micelles, ....?

Have you done Skin allergy, toxicity, eco-toxicity, etc., testing?

Thank you very much for your support

Please, feel to post your own questions to authors of other papers in this or other workshops to stimulate fruitful cross-over discussions.
Amanda Loreens
30 July 2021
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