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Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation

BACKGROUND AND OBJECTIVES: Increasing the amount of protease from microbial sources is in the focus of attention. Random mutagenesis by physical methods like ultraviolet (UV) radiation is a cost effective and convenient procedure for strain improvement. Therefore, in the present study attempts were...

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Autores principales: Kalahroudi, Reyhaneh Jafari, Valizadeh, Vahideh, Atyabi, Seyed Mohammad, Keramati, Malihe, Cohan, Reza Ahangari, Aghai, Atousa, Norouzian, Dariush
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Tehran University of Medical Sciences 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7884282/
https://www.ncbi.nlm.nih.gov/pubmed/33613915
http://dx.doi.org/10.18502/ijm.v12i6.5035
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author Kalahroudi, Reyhaneh Jafari
Valizadeh, Vahideh
Atyabi, Seyed Mohammad
Keramati, Malihe
Cohan, Reza Ahangari
Aghai, Atousa
Norouzian, Dariush
author_facet Kalahroudi, Reyhaneh Jafari
Valizadeh, Vahideh
Atyabi, Seyed Mohammad
Keramati, Malihe
Cohan, Reza Ahangari
Aghai, Atousa
Norouzian, Dariush
author_sort Kalahroudi, Reyhaneh Jafari
collection PubMed
description BACKGROUND AND OBJECTIVES: Increasing the amount of protease from microbial sources is in the focus of attention. Random mutagenesis by physical methods like ultraviolet (UV) radiation is a cost effective and convenient procedure for strain improvement. Therefore, in the present study attempts were made to investigate the effect of UV radiation on Lysobacter enzymogenes in order to increase its protease activity. MATERIALS AND METHODS: UV mutagenesis was induced in L. enzymogenes fresh culture at the distance of 20 cm from light source for different exposure times of 70, 90, 150 and 200 seconds. The mutated isolates were randomly cultured from the nutrient agar medium to casein agar plate, as a selective medium. The primary screening was performed by observing hydrolysis of casein in the plate and the secondary screening was carried out on skim milk agar on the basis of zone of hydrolysis using bacterial supernatants. Quantification of protease activity was done by Anson’s method using tyrosine as standard. RESULTS: UV radiation resulted in obtaining 12 mutants out of 100 examined L. enzymogenes strains with increased protease activity. The mutant M2, at 90s exposure time was selected as the best mutant bacterium which produced 1.96 fold more protease over the parent strain. CONCLUSION: Random mutation by UV radiation is a simple and convenient method to increase the protease activity of Lysobacter enzymogenes. Furthermore, it seems that the middle time of exposure to UV, 90 s, was the best time because it can induce mutagenesis but did not hamper the bacteria growth and viability.
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spelling pubmed-78842822021-02-19 Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation Kalahroudi, Reyhaneh Jafari Valizadeh, Vahideh Atyabi, Seyed Mohammad Keramati, Malihe Cohan, Reza Ahangari Aghai, Atousa Norouzian, Dariush Iran J Microbiol Original Article BACKGROUND AND OBJECTIVES: Increasing the amount of protease from microbial sources is in the focus of attention. Random mutagenesis by physical methods like ultraviolet (UV) radiation is a cost effective and convenient procedure for strain improvement. Therefore, in the present study attempts were made to investigate the effect of UV radiation on Lysobacter enzymogenes in order to increase its protease activity. MATERIALS AND METHODS: UV mutagenesis was induced in L. enzymogenes fresh culture at the distance of 20 cm from light source for different exposure times of 70, 90, 150 and 200 seconds. The mutated isolates were randomly cultured from the nutrient agar medium to casein agar plate, as a selective medium. The primary screening was performed by observing hydrolysis of casein in the plate and the secondary screening was carried out on skim milk agar on the basis of zone of hydrolysis using bacterial supernatants. Quantification of protease activity was done by Anson’s method using tyrosine as standard. RESULTS: UV radiation resulted in obtaining 12 mutants out of 100 examined L. enzymogenes strains with increased protease activity. The mutant M2, at 90s exposure time was selected as the best mutant bacterium which produced 1.96 fold more protease over the parent strain. CONCLUSION: Random mutation by UV radiation is a simple and convenient method to increase the protease activity of Lysobacter enzymogenes. Furthermore, it seems that the middle time of exposure to UV, 90 s, was the best time because it can induce mutagenesis but did not hamper the bacteria growth and viability. Tehran University of Medical Sciences 2020-12 /pmc/articles/PMC7884282/ /pubmed/33613915 http://dx.doi.org/10.18502/ijm.v12i6.5035 Text en Copyright© 2020 The Authors. This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International license, (https://creativecommons.org/licenses/by-nc/4.0/) Non-commercial uses of the work are permitted, provided the original work is properly cited.
spellingShingle Original Article
Kalahroudi, Reyhaneh Jafari
Valizadeh, Vahideh
Atyabi, Seyed Mohammad
Keramati, Malihe
Cohan, Reza Ahangari
Aghai, Atousa
Norouzian, Dariush
Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation
title Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation
title_full Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation
title_fullStr Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation
title_full_unstemmed Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation
title_short Increment in protease activity of Lysobacter enzymogenes strain by ultra violet radiation
title_sort increment in protease activity of lysobacter enzymogenes strain by ultra violet radiation
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7884282/
https://www.ncbi.nlm.nih.gov/pubmed/33613915
http://dx.doi.org/10.18502/ijm.v12i6.5035
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