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325660

Quantification of thermo-halotolerant alkaline protease activity derived from Bacillus licheniformis strains isolated from extreme environments in Morocco

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Last updated: 28 Dec 2024

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Abstract

Proteases; especially alkaline proteases, constitute the most used group of enzymes in industry. The wide scope of their application requires varying properties; most commonly stability throughout the conditional changes that would occur during the various industrial processes. This study aimed to identify the potentially interesting bacterial strains obtained from Moroccan extreme environment, and evaluate their proteolytic activity under the various growing conditions. In this study, the impact of temperature and salinity on the alkaline protease activity (pH 11) of 33 Bacillus strains deposited in the Moroccan Coordinated Culture Collection, which originated from the various extreme environments from Morocco, was studied. Bacterial identification to the species level was performed using 16S rRNA gene sequencing and MultiLocus Sequence Typing (MLST), a technique that is much more precise and can identify the bacteria to the strain level. Strain B950 showed a relatively stable protease activity at the tested extreme conditions (i.e., 130.8 U/ ml at 60 °C and 10 % NaCl). On the other hand, strain B961 displayed a better overall activity at either high temperature (140.8 U/ ml) or salinity (137 U/ ml); however, it was not as stable as when grown under both extreme conditions. Regarding identity of the bacterial strains, they were all representatives of Bacillus licheniformis; although B950 and B961 strains belonged to Sequence Types 3 and 5, respectively.

DOI

10.21608/nrmj.2023.325660

Keywords

Alkaline protease, Bacillus licheniformis, Extremo-tolerance, MultiLocus sequence typing scheme

Authors

First Name

Taha

Last Name

Chouati

MiddleName

-

Affiliation

Functional Genomic analysis platform and CCMM, National Center for Scientific and Technical Research (CNRST), Morocco

Email

taha.chouati@gmail.com

City

-

Orcid

0000-0002-1871-5624

First Name

Ounayssa

Last Name

Ayadi

MiddleName

-

Affiliation

Laboratory of physical chemistry and biotechnologies of biomolecules and materials, University Hassan II Casablanca, FSTM, Mohammedia, Morocco

Email

ounayssa-ayadi_total98@hotmail.com

City

-

Orcid

0000-0003-1205-5941

First Name

Mohammed

Last Name

Ajdig

MiddleName

-

Affiliation

Microbiology and Molecular Biology Team, Plant and Microbial Biotechnology, Biodiversity and Environment Center, Faculty of Sciences, Mohammed V University in Rabat, Morocco

Email

-

City

-

Orcid

0000-0003-4616-2104

First Name

Lahcen

Last Name

Ouchari

MiddleName

-

Affiliation

Microbiology and Molecular Biology Team, Plant and Microbial Biotechnology, Biodiversity and Environment Center, Faculty of Sciences, Mohammed V University in Rabat, Morocco

Email

ouchari@cnrst.ma

City

-

Orcid

0000-0001-6599-8180

First Name

Bahia

Last Name

Rached

MiddleName

-

Affiliation

Laboratory of physical chemistry and biotechnologies of biomolecules and materials, University Hassan II Casablanca, FSTM, Mohammedia, Morocco

Email

bahia.rached@gmail.com

City

-

Orcid

0009-0006-4864-3090

First Name

Jamila

Last Name

El Alami

MiddleName

-

Affiliation

Functional Genomic analysis platform and CCMM, National Center for Scientific and Technical Research (CNRST), Morocco

Email

j.elalami@cnrst.ma

City

-

Orcid

0000-0003-4658-4550

First Name

Elmostafa

Last Name

El Fahime

MiddleName

-

Affiliation

Genopath Research Center, ERNN, Faculty of Medicine and Pharmacy, University Mohammed V of Rabat, Morocoo

Email

m.elfahime@gmail.com

City

-

Orcid

0000-0001-7812-0641

Volume

7

Article Issue

6

Related Issue

44294

Issue Date

2023-11-01

Receive Date

2023-10-02

Publish Date

2023-11-01

Page Start

2,199

Page End

2,209

Print ISSN

2537-0286

Online ISSN

2537-0294

Article File

NRMJ_Volume 7_Issue 6_Pages 2199-2209.pdf

PDF . 449.1kB

Link

https://nrmj.journals.ekb.eg/article_325660.html

Detail API

https://nrmj.journals.ekb.eg/service?article_code=325660

Order

325,660

Type

Original Article

Type Code

2,265

Publication Type

Journal

Publication Title

Novel Research in Microbiology Journal

Publication Link

https://nrmj.journals.ekb.eg/

MainTitle

Quantification of thermo-halotolerant alkaline protease activity derived from Bacillus licheniformis strains isolated from extreme environments in Morocco

Details

Type

Article

Created At

28 Dec 2024