Note: A new pest,Liriomyza trifolii, on cotton in the Büyük Menderes Valley, Turkey
The study was conducted to evaluateLiriomyza trifolii (Burgess) in the cotton fields of the Büyük Menderes Valley, Turkey, from 1999 to 2000. Leaves were sampled weekly from the middle of June to the middle of August and kept in the laboratory to observe emerging leafminers. Leafminers were initially found on cotton leaves from 35 to 66 days after sowing. The numbers of larval mines varied from one to four per leaf. The largest number of infested leaves was observed in Aydın (Center), where 18.8% and 17.7% of the sampled leaves were infested in 1999 and 2000, respectively. We conclude thatL. trifolii is a potential pest in the cotton fields of Turkey and more research is needed.
GEOGRAPHICAL DISTRIBUTION, HOST RANGE AND PARASITOIDS OF SERPENTINE LEAF MINER, Liriomyza trifolii (Burgess) IN SOUTH INDIA
Survey conducted for assessing the incidence and severity of the serpentine leaf miner, Liriomyza trifolii (Burgess) in Andhra Pradesh, Karnataka, Maharashtra and Tamil Nadu during November, 1992 and February, 1993 revealed its occurrence in all these states. Its damage was characterised by sharply curled and contorted leaf mines which had a continuous black trail of frass. It was recorded on 70 host plants covering fibre crops, pulses, vegetables, ornamentals, green manures, fodder, narcotics and weeds belonging to 16 families. The incidence was relatively severe on tomato, okra, field bean, ridge gourd, cucumber, potato, castor and cotton. The severity of damage varied depending on the plant height. Leaves in the top canopy had fewer mines as compared to leaves in the middle and bottom canopy. A few indigenous parasitoids have been recorded on the insect.
Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785
A maltotriose-forming amylase (G3Amy) from Kitasatospora sp. MK-1785 was successfully isolated from a soil sample by inhibiting typical extracellular α-amylases using a proteinaceous α-amylase inhibitor. G3Amy was purified from the MK-1785 culture supernatant and characterized. G3Amy produced maltotriose as the principal product from starch and was categorized as an exo-α-amylase. G3Amy could also transfer maltotriose to phenolic and alcoholic compounds. Therefore, G3Amy can be useful for not only maltotriose manufacture but also maltooligosaccharide-glycoside synthesis. Further, the G3Amy gene was cloned and expressed in Escherichia coli cells. Analysis of its deduced amino acid sequence revealed that G3Amy consisted of an N-terminal GH13 catalytic domain and two C-terminal repeat starch-binding domains belonging to CBM20. It is suggested that natural G3Amy was subjected to proteolysis at N-terminal region of the anterior CBM20 in the C-terminal region. As with natural G3Amy, recombinant G3Amy could produce and transfer maltotriose from starch.