ABSTRACT
Os ácaros tetraniquídeos representam importantes pragas para diversas culturas agrícolas em todo o mundo. Durante a prospecção em mudas de Erytrina velutina no distrito de São Cristovão, Estado de Sergipe, Brasil, a ocorrência destes foi observada em 15 por cento das mudas que foram levadas ao laboratório para a caracterização dos danos. As mudas apresentavam sintomas de redução e encarquilhamento do limbo. Foram coletados 100 indivíduos destas plantas, os quais foram montados em lâminas de microscopia para a identificação taxonômica. Os ácaros foram identificados como pertencentes à espécie Tetranychus neocaledonicus (Acari: Tetranychidae). Este é o primeiro relato em E. velutina, como hospedeira para T. neocaledonicus no Brasil.
Spider mites are important pests to several crops worldwide. During prospecting in Erytrina velutina specimens from São Cristovão District, Sergipe State, Brazil, their occurrence was observed in 15 percent seedlings, which were taken to the laboratory for description of damages. The seedlings presented leaf blade reduction and crumpling symptoms. One hundred mites were collected from these seedlings and mounted on microscope slides for taxonomic identification. The identified mites belonged to the species Tetranychus neocaledonicus (Acari: Tetranychidae). This is the first report of E. velutina as host for T. neocaledonicus in Brazil.
Subject(s)
Acari/growth & development , Trees/parasitology , Brazil , Erythrina/growth & development , Erythrina/parasitology , Plant Shoots/parasitology , Host-Parasite InteractionsABSTRACT
An elastase-like chymotrypsin was purified by aprotinin-agarose affinity chromatography from the midgut extract of cardamom shoot and capsule borer, Conogethes punctiferalis. The purified enzyme had a Vmax of 687.6 +/- 22.1 nmole pNA released/min/mg protein, Km of 0.168 +/- 0.012 mM with SAAPLpNA as substrate and gave a single band on SDS-PAGE with a molecular mass of 72.1 kDa. Casein zymogram revealed one clear zone of proteolytic activity, which corresponded to the band obtained with SDS-PAGE indicating that this could be a single-polypeptide enzyme.