Journals / Turkish Journal of Biology / 2013 / Cilt: 37 - Sayı: 6

Characterization, antifungal activity, and cell immobilization of a chitinase from Serratia marcescens MO-1

Pages
639–644
Publication Date
2013-06-01
DOI
—
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AI Summary & Key Takeaways

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⚡ TL;DR(Too Long; Didn't Read)

Our results showed that the chitinase from S. marcescens MO-1 seems to be valuable in terms of its biotechnological applications; it can be produced using immobilized cells and can be used against fungal pathogens as an alternative to chemical pesticides.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Chitinases have the potential to control many pathogen species, such as fungi containing chitin on their cell walls.
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Key Findings & Data:In the present study, chitinase from novel isolate Serratia marcescens MO-1, isolated from Poecilimon tauricola (Orthoptera: Tettigoniidae) in Turkey, was investigated.
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Conclusion & Impact:Our results showed that the chitinase from S. marcescens MO-1 seems to be valuable in terms of its biotechnological applications; it can be produced using immobilized cells and can be used against fungal pathogens as an alternative to chemical pesticides.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Key words: Serratia marcescens · chitinase · cell immobilization

Abstract

Chitinases have the potential to control many pathogen species, such as fungi containing chitin on their cell walls. In the present study, chitinase from novel isolate Serratia marcescens MO-1, isolated from Poecilimon tauricola (Orthoptera: Tettigoniidae) in Turkey, was investigated. The optimum pH and temperature for the chitinase activity were found to be pH 7.0 (36.6 U/mL) and 50 °C (37.1 U/mL), respectively. Moreover, the activity was still high in acidic (23.0 U/mL at pH 3.0) and basic (17.3 U/mL at pH 11.0) conditions as well as at lower (29.5 U/mL at 20 °C) and higher (28.7 U/mL at 80 °C) temperatures. The enzyme was highly thermotolerant, keeping 63.7% (23.5 U/mL) of its activity after incubation at 90 °C for 15 min. Antifungal activity of the chitinase against Alternaria citri, Fusarium oxysporum, Trichoderma harzianum, Aspergillus niger, and Rhizopus oryzae was determined. In addition, chitinase production by immobilized S. marcescens MO-1 cells was monitored over 10 days; the enzyme activity was found to be 3641 U/mL during this period. Our results showed that the chitinase from S. marcescens MO-1 seems to be valuable in terms of its biotechnological applications; it can be produced using immobilized cells and can be used against fungal pathogens as an alternative to chemical pesticides.

Özet

Chitinases have the potential to control many pathogen species, such as fungi containing chitin on their cell walls. In the present study, chitinase from novel isolate Serratia marcescens MO-1, isolated from Poecilimon tauricola (Orthoptera: Tettigoniidae) in Turkey, was investigated. The optimum pH and temperature for the chitinase activity were found to be pH 7.0 (36.6 U/mL) and 50 °C (37.1 U/mL), respectively. Moreover, the activity was still high in acidic (23.0 U/mL at pH 3.0) and basic (17.3 U/mL at pH 11.0) conditions as well as at lower (29.5 U/mL at 20 °C) and higher (28.7 U/mL at 80 °C) temperatures. The enzyme was highly thermotolerant, keeping 63.7% (23.5 U/mL) of its activity after incubation at 90 °C for 15 min. Antifungal activity of the chitinase against Alternaria citri, Fusarium oxysporum, Trichoderma harzianum, Aspergillus niger, and Rhizopus oryzae was determined. In addition, chitinase production by immobilized S. marcescens MO-1 cells was monitored over 10 days; the enzyme activity was found to be 36–41 U/mL during this period. Our results showed that the chitinase from S. marcescens MO-1 seems to be valuable in terms of its biotechnological applications; it can be produced using immobilized cells and can be used against fungal pathogens as an alternative to chemical pesticides.

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Cite This Article

OKAY, S., ÖZDAL, M., KURBANOĞLU, E. B. (2013). Characterization, antifungal activity, and cell immobilization of a chitinase from Serratia marcescens MO-1. Turkish Journal of Biology, Cilt: 37 - Sayı: 6, 639–644. https://ajindex.com/articles/182461

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