The α-amylase of the beetle <i>Callosobruchus chinensis</i> properties

Podoler, H.; Applebaum, Shalom W.

doi:10.1042/bj1210321

Cited by 47 publications

(23 citation statements)

References 10 publications

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“…The optimum pH of 6.8 of haemolymph amylase observed in the present study is in contrast to slightly acidic range reported in a variety of insect species (Baker, 1987;Podoler and Applebaum, 1971;Buonocore et aL, 1976). The sharp ascending and descending nature of the amylase activity indicate that the haemolymph amylase isozymes have similar pH optima.…”

Section: Discussioncontrasting

confidence: 54%

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Abraham

Nagaraju

Datta

1992

Insect Biochemistry and Molecular Biology

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Abstract--Different amylase enzymes were identified by analysis of digestive fluid and haemolymph in diapausing and nondiapausing strains of silkworm, Bombyx mori. The diapausing strain showed negligible digestive amylase activity at a pH range of 3-11, while the nondiapausing strain registered strikingly higher amylase activity at pH 9.2. Higher levels of undigested starch was found in the faecal matter of the diapausing strain, which is consistent with the negligible digestive amylase activity. Developmental specific expression of haemolymph amylase activity was seen in nondiapausing and diapausing strains. In the nondiapausing strain the digestive amylase activity was at its peak during intermoult and depressed during moult. PAGE analysis revealed the occurrence of only anodal digestive and haemolymph amylases in the diapausing strain, whereas both cathodal and anodal enzymes were seen in the digestive fluid and haemolymph of the nondiapausing strain.

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Section: Discussioncontrasting

confidence: 54%

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Abraham

Nagaraju

Datta

1992

Insect Biochemistry and Molecular Biology

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“…A similar behavior was described in the carboxylesterase Est 30 from Geobacillus stearothermophilus, which in spite of being a dimer, was not affected neither for 2-mercaptoetanol nor DTT (Ewis et al, 2004). Furthermore, this reducing reagent is regarded as acting by protecting essential thiol groups in their reduced state (Podoler & Applebaum, 1971). Thus 2-mercaptoethanol seems to increase type II esterase activity by protecting the thiol groups that could be involved in the enzyme activity.…”

Section: Effect Of Metal Ions and Inhibitors On Esterase Activitymentioning

confidence: 51%

Enzymatic synthesis of banana flavour (isoamyl acetate) by Bacillus licheniformis S-86 esterase

Torres

Baigorí

Swathy

et al. 2009

Food Research International

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“…They are widely used in the food and textile industries . The first insect α‐amylase studied in some detail was reported from the pulse beetle, Callosobruchus chinensis , in which the enzyme was purified and its properties were reported . Insect α‐amylases digest polysaccharides.…”

Section: Introductionmentioning

confidence: 99%

A digestive tract expressing α‐amylase influences the adult lifespan of Pteromalus puparum revealed through RNAi and rescue analyses

WANG

Yang

Liu

et al. 2019

Pest Management Science

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BACKGROUND Midgut and salivary gland α‐amylases are digestive enzymes required for the development of insects and have been investigated in some insect species. However, α‐amylases in the endoparasitioid wasps have not been reported. Pteromalus puparum (Hymenoptera: Pteromalidae) is a dominant endoparasitioid wasp that parasitizes many butterfly species, including the Brassicaceae pest Pieris rapae (Lepidoptera: Pieridae). Here, we studied the characteristics and functions of three α‐amylases in P. puparum. RESULTS We cloned three genes encoding α‐amylases in P. puparum, PpAmy1, PpAmy2 and PpAmy3. The full length of the PpAmy1 cDNA is 1872 bp, encoding 496 amino acids, the PpAmy2 cDNA is 1863 bp long, encoding 518 amino acids, and PpAmy3 cDNA consists of 1802 bp encoding 521 amino acids. PpAmys are highly similar in amino acid sequences, but they have separate tissue distributions. Phylogenetic results show that gene duplications may occur between PpAmy2 and PpAmy3. PpAmy1 and PpAmy3 are most highly expressed in the digestive tract and the venom apparatus, respectively, while PpAmy2 is broadly expressed in all tissues. We report that PpAmy1 acts in the digestive tract, where it influences lifespan as demonstrated using RNAi and α‐amylase rescue analyses, and there is no significant difference in longevity when PpAmy2 and PpAmy3 are knocked down. CONCLUSION PpAmys probably have roles in carbohydrate metabolism of P. puparum and its host/parasitoid relationships. The characterization and functional study of PpAmys lays the foundation for the protection and utilization of parasitoid resources, and the biological control of agricultural pests. © 2019 Society of Chemical Industry

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The α-amylase of the beetle Callosobruchus chinensis properties

Cited by 47 publications

References 10 publications

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Enzymatic synthesis of banana flavour (isoamyl acetate) by Bacillus licheniformis S-86 esterase

A digestive tract expressing α‐amylase influences the adult lifespan of Pteromalus puparum revealed through RNAi and rescue analyses

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