Effect of<i>Bombyx mori</i>Chitinase against Japanese Pine Sawyer (<i>Monochamus alternatus</i>) Adults as a Biopesticide

Kabir, Khondkar Ehteshamul; Sugimoto, Hiroyuki; Tado, Hiroyuki; Endo, Katsuhiko; Yamanaka, Akira; Tanaka, Shuhei; Koga, Daizo

doi:10.1271/bbb.70.219

Cited by 28 publications

(24 citation statements)

References 43 publications

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“…Despite their involvement in environmental and human health problems, chemical pesticides have been used in the killing of pest organisms for over 55 years (1). Moreover, there is difficulty in discovering new classes of chemicals for the management of these pests because of their increasing resistance to chemical pesticides (1).…”

Section: Introductionmentioning

confidence: 99%

“…Since fungal cell walls and insect exoskeletons contain chitin, a homopolymer of β-1,4-linked N-acetyl-Dglucosamine residues as a major structural component, chitinases have been reported for their potential as biopesticides for the control of the plant diseases caused by various phytopathogenic fungi (3,4) and insect pests (1,5). Chitin is degraded into disaccharides and larger oligomeric saccharides by the action of chitinases (EC 3.2.1.14) through hydrolysis of the β-(1,4)-linkages (6), and these enzymes have been divided into 2 separate families, GH18 and GH19, based on amino acid sequences and their catalytic mechanisms (4).…”

Section: Introductionmentioning

confidence: 99%

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

Okay¹,

Özdal²,

Kurbanoğlu³

2013

Turk J Biol

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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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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Okay¹,

Özdal²,

Kurbanoğlu³

2013

Turk J Biol

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“…The peritrophic membrane chitin was degraded by Bm-CHI, but the midgut epithelium was not affected [29].…”

Section: Transgene Source and Mode Of Action Example Of Usementioning

confidence: 91%

“…This in turn has led to a search for new insecticidal proteins and their encoding genes that have commercial potential for plant protection [8,24]. They include -amylase inhibitors [25,26], vegetative insecticidal protein [27,28], chitinases [29] and protease inhibitors [30,31], as well as several other proteins directed to targets in the insect gut (Table 1).…”

Section: Introductionmentioning

confidence: 99%

Biotechnological Approaches for the Control of Insect Pests in Crop Plants

Stevens¹,

Dunse²,

Fox³

et al. 2012

Pesticides - Advances in Chemical and Botanical Pesticides

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“…Further, You and Fujisaki (2009) injected baculovirus expressed Haemaphysalis longicornis chitinase to mice and found that the mice showed a specific protective anti-tick immune response affecting tick molting. Purified chitinase (75kDa) from Bombyx mori on oral ingestion (11μg/50μl) caused high mortality as well as significant decrease in feed consumption and slight reduction of body weight in Japanese pine sawyer (JPS), a beetle Monochamus alternatus (Kabir et al, 2006). These studies have shown that chitinase is capable of negatively affecting growth and moults of the larvae and thereby, can act as insecticides.…”

Section: Respectively and Have The Consensus Sequences Motif I-kxx(mentioning

confidence: 99%

Expression of a Variant Chitinase Transcript of Helicoverpa armigera in E. coli

2016

IJSR

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Gene encoding for chitinase was isolated and sequenced from the cotton bollworm Helicoverpa armigera, using the polymerase chain reaction technique directed by primers designed from the chitinase cDNA of the same insect reported by Ahmad et al. (2003). The nucleotide sequence analysis suggested that the gene is of 1737 bp showing homolgy of 96% with the reference chitinase sequence (AY325496) and 80% homology with that of Manduca sexta, the first cloned insect chitinase gene (U02270). The cDNA encoded a polypeptide of 578 amino acids, short of 10 amino acid residues compared to reference sequence. The major differences in the protein sequence to the one reported earlier was in proline threonine linker region where four threonine residues were replaced by alanine and one threonine by serine and further, condensation of protein towards the C-terminal region. Surprisingly the protein sequence of chitin binding domain shows 98% homolgy to Lymantria dispar chitinase (KP337328.1) and 96% homology to Phyllonorycter ringoniella chitinase (JN607321.1) and 100% homology to the reference protein(AAQ91786.1). Expression of the gene in bacterial system resulted in the formation of inclusion bodies retaining enzymatic activity. Bioassay for insecticidal activity against Helicoverpa armigera showed 60% mortality for injection assay, reduction in larval weight gain in case of oral application and 40% mortality for topical application.

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Effect ofBombyx moriChitinase against Japanese Pine Sawyer (Monochamus alternatus) Adults as a Biopesticide

Cited by 28 publications

References 43 publications

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

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

Biotechnological Approaches for the Control of Insect Pests in Crop Plants

Expression of a Variant Chitinase Transcript of Helicoverpa armigera in E. coli

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