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Chemical defence of turnip sawfly larvae against Japanese tree frogs
Satoru Matsubara,Shinji Sugiura 한국응용곤충학회 2017 Journal of Asia-Pacific Entomology Vol.20 No.1
Larvae of the turnip sawfly Athalia rosae (Hymenoptera: Tenthredinidae) are known to defend themselves using chemicals against predators such as ants,wasps and birds. However, only a fewstudies have tested the effectiveness of such chemical defences under field conditions. In a Japanese farm, a tree frog Hyla japonica (Anura: Hylidae) was observed to attack an A. rosae larva, but spit out the larva immediately after taking it into its mouth. To clarify how A. rosae larvae defend themselves against frogs, we quantitatively investigated how H. japonica attacked A. rosae larvae and palatable caterpillars of Pieris rapae (Lepidoptera: Pieridae) under field conditions.We experimentally placed an A. rosae larva or a P. rapae larva in front of tree frogs on the crop leaves. Frogs attacked both A. rosae and P. rapae larvae. However, the rate of predation by frogs was different between A. rosae and P. rapae larvae: 75% of frogs rejected A. rosae larvae, whereas 100% of frogs ate P. rapae larvae. Athalia rosae larvae attacked by frogs released their haemolymph (containing defensive chemicals) from the injured parts of their bodies. These results suggest that A. rosae larvae can chemically defend themselves against frogs in field conditions.
Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11
Matsubara, Takayoshi,Ammar, Youssef Ben,Anindyawati, Trisanti,Yamamoto, Satoru,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.4
Raw-starch-digesting $\alpha$-amylase (Amyl III) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT-11 using wheat bran in the medium. The purified Amyl III digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl III were maltotriose and maltose, although a small amount of glucose was produced. Amyl III acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl III on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl III and GA I was observed for the digestion of raw starch granules.
Matsubara, Takayoshi,Ammar, Youssef Ben,Anindyawati, Trisanti,Yamamoto, Satoru,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.4
Complementary DNAs encoding $\alpha$-amylases (Amyl I, Amyl III) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl III that was a raw starch digesting $\alpha$-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 63.3% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the raw-starch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.
Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11
( Takayoshi Matsubara ),( Youssef Ben Ammar ),( Trisanti Anindyawati ),( Satoru Yamamoto ),( Kazuo Ito ),( Masaru Iizuka ),( Noshi Minamiura ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.4
Raw-starch-digesting α-amylase (Amyl Ⅲ) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT 11 using wheat bran in the medium. The purified Amyl Ⅲ digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl Ⅲ were maltotriose and maltose, although a small amount of glucose was produced. Amyl Ⅲ acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl Ⅲ on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl Ⅲ and GA I was observed for the digestion of raw starch granules.
( Takayoshi Matsubara ),( Youssef Ben Ammar ),( Trisanti Anindyawati ),( Satoru Yamamoto ),( Kazuo Ito ),( Masaru Iizuka ),( Noshi Minamiura ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.4
Complementary DNAs encoding α-amylases (Amyl I, Amyl Ⅲ) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl Ⅲ that was a raw starch digesting α-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 633% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the rawstarch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.