Characterization of α-amylase in the midgut and the salivary glands of rice striped stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)

Digestive enzymes of large cabbage white butterfly,Pieris brassicaeL. (Lepidoptera: Pieridae) from developmental and site of activity perspectives

“…Mehrabadi et al (2009) found a little difference in the amylolytic activity extracted from soluble and membrane-bound fractions from four regions in the midgut of Eurygaster integriceps Puton (Hemiptera: Scutelleridae) so that membranebound fractions of V1 and V4 parts of the midgut had higher amylolytic activity than soluble ones but no differences were found in V2 and V3. The majority of studies on α-amylase showed higher amylolytic activity in soluble fractions of the midgut in addition to the two last larval instars, which coincides with our study (Gutierrez et al 1990;Abraham et al 1992;Ferreira et al 1999;Mendiola-Olaya et al 2000;Zibaee et al 2008a;Yazdani et al 2010). …”

“…Meanwhile, it was found that glycosidases had higher activity in membrane-bound fractions than in soluble ones. This point has been indicated in previous studies that glycosidases exist in perimicrovillar membrane vesicles (PMMV) and plasma membrane markers (Riberio & Periera 1984;Terra et al 1996;Damasceno-Sa et al 2007;Zibaee et al 2009). Almost all naturally occurring plant glycosides are β-linked o-glycosyl compounds (Hsiao 1985), so β-glycosidases are the key enzymes for their metabolism.…”

“…These enzymes are active upon large ranges of components in plants, so these components may be involved in plant resistance to insects. The majority of these components are L-glycosides that release cyanide (or other toxic compounds) upon hydrolysis and are toxic for many herbivorous insects (Zibaee et al 2009). Therefore, it could be concluded that these enzymes have considerable activities in species that cause damage to plants such as P. brassicae, although there have been some reports on their activities in insects having sucrose in their diets.…”

“…Glycosidases (EC 3.2) are classified according to their substrate specificities (Ferriera et al 1999). They catalyse cleavage of internal bonds in polysaccharides and hydrolyse oligosaccharides as well as disaccharides (Zibaee et al 2009). Lipases (triacylglycerol-acyl-hydrolase EC 3.1.1.3), which catalyse the hydrolysis of fatty acid ester bonds, are widely distributed among animals, plants and microorganisms (Grillo et al 2007;Zibaee et al 2008b).…”

Botanical Insecticides and Their Effects on Insect Biochemistry and Immunity

“…Shekari et al (2008) demonstrated that a-amylase activity level in elm leaf beetle treated by A. annua extract decreased after 24 h and sharply increased after 48 h. Zibaee & Bandani (2010a) showed that Artemisia annua extract caused the reduction of a-amylase activity in Eurygaster integriceps Puton (Hemiptera: Scutelleridae), and this reduction increased by higher concentrations of plant extract. After amylase, glycosidases digest carbohydrate oligomers to monosaccharides (Terra and Ferriera, 2005;Zibaee et al, 2008a;Zibaee et al, 2009a). On the other hands, glycosidases catalyze the hydrolysis of terminal, non-reducing 1, 4-linked alpha-Dglucose residues with releasing of alpha-D-glucose.…”