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Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A

Chitinases have the ability of chitin digestion that constitutes a main compound of the cell wall in many of the phytopathogens such as fungi. In the following investigation, a novel chitinase with antifungal activity was characterized from a native Serratia marcescens B4A. Partially purified enzyme...

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Autores principales: Zarei, Mandana, Aminzadeh, Saeed, Zolgharnein, Hossein, Safahieh, Alireza, Daliri, Morteza, Noghabi, Kambiz Akbari, Ghoroghi, Ahmad, Motallebi, Abbasali
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Sociedade Brasileira de Microbiologia 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768790/
https://www.ncbi.nlm.nih.gov/pubmed/24031719
http://dx.doi.org/10.1590/S1517-838220110003000022
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author Zarei, Mandana
Aminzadeh, Saeed
Zolgharnein, Hossein
Safahieh, Alireza
Daliri, Morteza
Noghabi, Kambiz Akbari
Ghoroghi, Ahmad
Motallebi, Abbasali
author_facet Zarei, Mandana
Aminzadeh, Saeed
Zolgharnein, Hossein
Safahieh, Alireza
Daliri, Morteza
Noghabi, Kambiz Akbari
Ghoroghi, Ahmad
Motallebi, Abbasali
author_sort Zarei, Mandana
collection PubMed
description Chitinases have the ability of chitin digestion that constitutes a main compound of the cell wall in many of the phytopathogens such as fungi. In the following investigation, a novel chitinase with antifungal activity was characterized from a native Serratia marcescens B4A. Partially purified enzyme had an apparent molecular mass of 54 kDa. It indicated an optimum activity in pH 5 at 45°C. Enzyme was stable in 55°C for 20 min and at a pH range of 3–9 for 90 min at 25°C. When the temperature was raised to 60°C, it might affect the structure of enzymes lead to reduction of chitinase activity. Moreover, the K(m) and V(max) values for chitin were 8.3 mg/ml and 2.4 mmol/min, respectively. Additionally, the effect of some cations and chemical compounds were found to stimulate the chitinase activity. In addition, Iodoacetamide and Idoacetic acid did not inhibit enzyme activity, indicating that cysteine residues are not part of the catalytic site of chitinase. Finally, chitinase activity was further monitored by scanning electronic microscopy data in which progressive changes in chitin porosity appeared upon treatment with chitinase. This enzyme exhibited antifungal activity against Rhizoctonia solani, Bipolaris sp, Alternaria raphani, Alternaria brassicicola, revealing a potential application for the industry with potentially exploitable significance. Fungal chitin shows some special features, in particular with respect to chemical structure. Difference in chitinolytic ability must result from the subsite structure in the enzyme binding cleft. This implies that why the enzyme didn’t have significant antifungal activity against other Fungi.
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spelling pubmed-37687902013-09-12 Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A Zarei, Mandana Aminzadeh, Saeed Zolgharnein, Hossein Safahieh, Alireza Daliri, Morteza Noghabi, Kambiz Akbari Ghoroghi, Ahmad Motallebi, Abbasali Braz J Microbiol Medical Microbiology Chitinases have the ability of chitin digestion that constitutes a main compound of the cell wall in many of the phytopathogens such as fungi. In the following investigation, a novel chitinase with antifungal activity was characterized from a native Serratia marcescens B4A. Partially purified enzyme had an apparent molecular mass of 54 kDa. It indicated an optimum activity in pH 5 at 45°C. Enzyme was stable in 55°C for 20 min and at a pH range of 3–9 for 90 min at 25°C. When the temperature was raised to 60°C, it might affect the structure of enzymes lead to reduction of chitinase activity. Moreover, the K(m) and V(max) values for chitin were 8.3 mg/ml and 2.4 mmol/min, respectively. Additionally, the effect of some cations and chemical compounds were found to stimulate the chitinase activity. In addition, Iodoacetamide and Idoacetic acid did not inhibit enzyme activity, indicating that cysteine residues are not part of the catalytic site of chitinase. Finally, chitinase activity was further monitored by scanning electronic microscopy data in which progressive changes in chitin porosity appeared upon treatment with chitinase. This enzyme exhibited antifungal activity against Rhizoctonia solani, Bipolaris sp, Alternaria raphani, Alternaria brassicicola, revealing a potential application for the industry with potentially exploitable significance. Fungal chitin shows some special features, in particular with respect to chemical structure. Difference in chitinolytic ability must result from the subsite structure in the enzyme binding cleft. This implies that why the enzyme didn’t have significant antifungal activity against other Fungi. Sociedade Brasileira de Microbiologia 2011 2011-09-01 /pmc/articles/PMC3768790/ /pubmed/24031719 http://dx.doi.org/10.1590/S1517-838220110003000022 Text en © Sociedade Brasileira de Microbiologia http://creativecommons.org/licenses/by-nc/3.0/ All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License
spellingShingle Medical Microbiology
Zarei, Mandana
Aminzadeh, Saeed
Zolgharnein, Hossein
Safahieh, Alireza
Daliri, Morteza
Noghabi, Kambiz Akbari
Ghoroghi, Ahmad
Motallebi, Abbasali
Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A
title Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A
title_full Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A
title_fullStr Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A
title_full_unstemmed Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A
title_short Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A
title_sort characterization of a chitinase with antifungal activity from a native serratia marcescens b4a
topic Medical Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768790/
https://www.ncbi.nlm.nih.gov/pubmed/24031719
http://dx.doi.org/10.1590/S1517-838220110003000022
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