• Proceedings of the Korean Society of Sericultural Science Conference
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• 2004.10a
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• pp.61-61
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• 2004

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2004.10a
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• pp.62-62
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• 2004

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2002.11a
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• pp.142-142
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• 2002

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2005.11a
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• pp.65-65
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• 2005

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.10a
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• pp.129-129
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• 2002

No Abstract, See Full Text

• The Korean Journal of Pesticide Science
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• v.5 no.3
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• pp.47-49
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• 2001

The toxicity of benfuracarb and ${\lambda}$-cyhalothrin on oak longicorn beetle, Moechotypa diphysis was investigated in terms of residual effect and control efficacy in the field. Mycelial growth inhibition of Lentinula edodes was also investigated in the laboratory. Benfuracarb and ${\lambda}$-cyhalothrin showed 100% of control values and over 90% residual activities of benfuracarb and ${\lambda}$-cyhalothrin were continued for 15 and 20 days after treatment, respectively. Benfuracarb and ${\lambda}$-cyhalothrin did not affect the mycelial growth of L. edodes Imhyup 1 variety. These results indicate that benfuracarb and ${\lambda}$-cyhalothrin might be used for the control of M. diphysis adults in the field.

• International Journal of Industrial Entomology and Biomaterials
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• v.14 no.1
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• pp.51-56
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• 2007

In a previous study, three larval cuticle protein genes were cloned from the mulberry longicorn beetle, Apriona germari (Comp. Biochem. Physiol. B 136, 803-811, 2003). In the present study, the genomic structures of these three larval cuticle protein genes (AgLCP9.2, AgLCP12.6 and AgLCP12.3) were elucidated. All three cuticle protein genes consist of one intron and two exons. Southern blot analysis of genomic DNA suggested that three cuticle protein genes are a single copy gene. In addition, a novel larval cuticle protein gene, AgLCP10.6, was cloned from A. germari in this study. The AgLCP10.6 cDNA contains an ORF of 300 nucleotides that are capable of encoding a 100-amino acid polypeptide with a predicted molecular mass of 10.6 kDa. The amino acid sequence deduced from the AgLCP10.6 cDNA contained a type-specific consensus sequence identifiable in other insect cuticle proteins and is most homologous to Drosophila melanogaster cuticle protein ACP65A (51 % protein sequence identity). Northern blot analysis revealed that AgLCP10.6 showed epidermis-specific expression.

• Journal of Microbiology and Biotechnology
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• v.16 no.11
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• pp.1753-1759
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• 2006

Paenibacillus sp. HY-8 isolated from the digestive tracts of the longicorn beetle, Moechotypa diphysis, produced an extracellular endoxylanase with a molecular weight of 20 kDa estimated by SDS-PAGE. The xylanase was purified to near electrophoretic homogeneity from the culture supernatant after ammonium sulfate precipitation, gel filtration, and ionexchange chromatography. The purified xylanase exhibited the highest activities at pH 6.0 and $50^{\circ}C$. The $K_m\;and\;V_{max}$ values were 7.2 mg/ml and 16.3 U/mg, respectively, for birchwood xylan as the substrate. Nucleotide sequence of the PCR-cloned gene was determined to have the open reading frame encoding a polypeptide of 212 amino acids. The N-terminal amino acid sequence and the nucleotide sequence analyses predicted that the precursor xylanase contained a signal peptide composed of 28 amino acids and a catalytically active 19.9-kDa peptide fragment. The deduced amino acid sequence shared extensive similarity with those of the glycoside hydrolase family 11 of xylanases from other bacteria. The predicted amino acid sequence contained two glutamate residues, previously identified as essential and conserved for active sites in other xylanases of the glycoside hydrolase family 11.

• Journal of Microbiology
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• v.45 no.5
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• pp.409-417
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• 2007

Burkholderia sp. HY-10 isolated from the digestive tracts of the longicorn beetle, Prionus insularis, produced an extracellular lipase with a molecular weight of 33.5 kDa estimated by SDS-PAGE. The lipase was purified from the culture supernatant to near electrophoretic homogenity by a one-step adsorption-desorption procedure using a polypropylene matrix followed by a concentration step. The purified lipase exhibited highest activities at pH 8.5 and $60^{\circ}C$. A broad range of lipase substrates, from $C_4\;to\;C_{18}$ p-nitrophenyl esters, were hydrolyzed efficiently by the lipase. The most efficient substrate was p-nitrophenyl caproate ($C_6$). A 2485 bp DNA fragment was isolated by PCR amplification and chromosomal walking which encoded two polypeptides of 364 and 346 amino acids, identified as a lipase and a lipase foldase, respectively. The N-terminal amino acid sequence of the purified lipase and nucleotide sequence analysis predicted that the precursor lipase was proteolytically modified through the secretion step and produced a catalytically active 33.5 kDa protein. The deduced amino acid sequence for the lipase shared extensive similarity with those of the lipase family 1.2 of lipases from other bacteria. The deduced amino acid sequence contained two Cystein residues forming a disulfide bond in the molecule and three, well-conserved amino acid residues, $Ser^{131},\;His^{330},\;and\;Asp^{308}$, which composed the catalytic triad of the enzyme.

• Korean journal of applied entomology
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• v.45 no.2 s.143
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• pp.189-194
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• 2006

Fumigant toxicity of 18 plant essential oils were tested against the adults of oak longicorn beetle, Moechotypa diphysis. Among them, eucalyptus, rosemary and pennyroyal oils showed 100% mortality and sage oil showed 85% mortality at 10 $\mu\ell/\ell$ (air) dose. Eucalyptus and rosemary oils showed 100% mortality within 6 hr after treatment at 10 $\mu\ell/\ell$ (air) dose. GC and GC/MS analysis of the four essential oils and bioassay of their components revealed that 1,8-cineole (a major component of eucalyptus, rosemary and sage oils), thujone (a major component of sage oil) and pulegone (a major component of pennyroyal oil) showed higher adulticidal activity than others.