ALGERIAN JOURNAL OF BIOSCEINCES
https://app.periodikos.com.br/journal/ajbjournal/article/doi/10.5281/zenodo.5055773

ALGERIAN JOURNAL OF BIOSCEINCES

Biology

Characterization of endospore-forming bacteria producing extracellular enzymes isolated from the Djurdjura Mountains in Algeria

Merzouk YAHIAOUI*, Khelifa BOUACEM, Katia-Louiza ASMANI, Sondes MECHRI, Hamdi BENDIF, Mohammed HARIR, and Bassem JAOUADI

Downloads: 3
Views: 399

Abstract

Biodiversity in mountains in Algeria appears scanty and has not been thoroughly investigated. However, the mountain soil has been shown as an almost entire reserve of novel enzymes with interesting properties for industrial and environmental applications. In the present study, thirty bacterial strains were isolated from the Djurdjura Mountains in Kabylia (Algeria) and were studied for their ability to produce enzymes to be possibly used in biotechnological processes such as amylase, caseinase, and chitinase. The characterization of these isolates was carried out using morphological, physiological, and biochemical characteristics. All the data obtained with regards to the phenotypical properties of the isolates, confirmed that the strains belonged to the Bacillus group. In addition, the 16S rRNA gene of the two retained strains KA15 and LK-DZ15 was also amplified and sequenced. Phylogenetic tree was, afterwards, constructed. The nucleotide sequences and blast analyses confirmed that the KA15 and LK-DZ15 strains were closely related to those of the Bacillus altitudinis (accession n°.: MK874318) and Paenibacillus timonensis (accession n°.: MK734103) strains. The presence of amylases, proteases, and chitinases in KA15 and LK-DZ15 isolates are an indicator of their pivotal application in a variety of biotechnological processes.

Keywords

Isolation; Bacillus; Djurdjura Mountains; 16S rRNA; Enzymes.

References

1. Schleifer K.-H. Phylum XIII. Firmicutes Gibbons and Murray 1978, 5 (Firmacutes [sic] Gibbons and Murray 1978, 5). in: Bergey’s Manual® of Systematic Bacteriology, Springer. 2009: 19-1317.
2. Yahiaoui M, Bouacem K, Bendif H, Mechri S, Asmani K.L, Jaouadi B. Identification and characterization of a highly chitinase producing Paenibacillus timonensis strain LK-DZ15 isolated from Djurdjura Mountains in Kabylia, Algeria. MOL2NET. 2021, 6; 2624-5078.
3. Ash C, Priest F, Collins M. Molecular identification of rRNA group 3 bacilli using a PCR probe test. Proposal for the creation of a new genus Paenibacillus. Antonie van Leeuwenhoek. 1993, 64 : 253-260.
4. De Araújo N.K, de Assis C.F, Dos Santo E.S et al. Production of Enzymes by Paenibacillus chitinolyticus and Paenibacillus ehimensis to Obtain Chitooligosaccharides. Appl. Biochem Biotechnol. 2013, 170; 2: 292-300.
5. Mechri S, Bouacem K, Zarai-Jaouadi N et al. Identification of a novel protease from the thermophilic Anoxybacillus kamchatkensis M1V and its application as laundry detergent additive. Extremophiles. 2019, 23; 6: 687-706.
6. Priest F.G, Goodfellow M, Todd C. A. Numerical classification of the genus Bacillus. J. Gen. Microbiol. 1988, 134:1847-1882.
7. Dewan S. Global markets for enzymes in industrial applications. BCC Research, Wellesley. 2014.
8. Naidu K, Maseko S, Kruger G, Lin J. Purification and characterization of α-amylase from Paenibacillus sp. D9 and Escherichia coli recombinants. Biocatal. Biotransfor. 2020, 38; 1: 24-34.
9. Bouacem K, Amziane-Touazi M, Ben Hania W et al. Isolation and characterization of moderately thermophilic aerobic cultivable bacteria from Hammam Righa Hot Spring (Algeria): description of their hydrolytic capacities. Alg. J. Env. Sci. Tech. 2020, 2437-1114.
10. Yahiaoui M, Laribi-Habchi H, Bouacem K. et al. Purifcation and biochemical characterization of a new organic solventtolerant chitinase from Paenibacillus timonensis strain LK-DZ15 isolated from the Djurdjura Mountains in Kabylia, Algeria. Carbohyd. Res. 2019, 483;107747.
11. Asmani K.L, Bouacem K, Ouelhadj A et al. Biochemical and molecular characterization of an acido-thermostable endo-chitinase from Bacillus altitudinis KA15 for industrial degradation of chitinous waste. Carbohyd. Res. 2020, 495;108089.
12. Asmani K.L, Bouacem K, Ouelhadj A et al. Identification of a novel acido-thermostable chitinase from Bacillus altitudinis strain KA15. MOL2NET. 2020, 6; 2624-5078.
13. Schallmey M, Singh A, Ward O.P. Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 2004, 50; 1:1-17.
14. Burhan A, Nisa U, Gökhan C, Ömer C, Ashabil A Osman G. Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6. Process Biochem. 2003, 38:1397-1403.
15. Sambrook J, Fritsch E, Maniatis T. Molecular cloning: A Laboratory Manual, 2nd edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA. 1989 :23-38.
16. Laribi-Habchi H, Bouacem. K, Allala F et al. Characterization of chitinase from Shewanella inventionis HE3 with bio-insecticidal effect against granary weevil, Sitophilus granarius Linnaeus (Coleoptera: Curculionidae). Process Biochem. 2020, 97: 222-233.
17. Li Y, Pan Y, She Q, Chen L. A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates. BMC Biotechnol. 2013, 13; 1: 1-13.
18. Mechri S, Zarai-Jaouadi N, Bouacem K et al. Cloning and heterologous expression of subtilisin SAPN, a serine alkaline protease from Melghiribacillus thermohalophilus Nari2AT in Escherichia coli and Pichia pastoris. Process Biochem. 2021, 105: 27-41.
19. Mesbah N.M, Sarmiento F. Enzymes from Extreme Environments. Front. Bioeng. Biotechnol. 2016, 4; 24.
20. Krithika S, Chellaram C. Isolation, screening, and characterization of chitinase producing bacteria from marine wastes. Int. J. Pharm Pharm Sci. 2016, 8; 0975-1491.


Submitted date:
05/07/2021

Reviewed date:
05/27/2021

Accepted date:
06/20/2021

60ddeafaa9539536cf5599c5 ajbjournal Articles
Links & Downloads

Alger. j. biosciences

Share this page
Page Sections