Use este identificador para citar ou linkar para este item: https://locus.ufv.br//handle/123456789/13606
Tipo: Artigo
Título: Purification and characterization of trypsin produced by gut bacteria from Anticarsia gemmatalis
Autor(es): Pilon, Franciny Martins
Silva, Camila da Rocha
Visôtto, Liliane Evangelista
Barros, Rafael de Almeida
Silva Júnior, Neilier Rodrigues da
Campos, Wellington Garcia
Oliveira, Maria Goreti de Almeida
Abstract: Purification of active trypsin in the digestive process of insects is essential for the development of potent protease inhibitors (PIs) as an emerging pest control technology and research into insect adaptations to dietary PIs. An important aspect is the presence of proteolytic microorganisms, which contribute to host nutrition. Here, we purified trypsins produced by bacteria Bacillus cereus, Enterococcus mundtii, Enterococcus gallinarum, and Staphylococcus xylosus isolated from the midgut of Anticarsia gemmatalis. The trypsins had a molecular mass of approximately 25 kDa. The enzymes showed increased activity at 40°C, and they were active at pH values 7.5–10. Aprotinin, bis-benzamidine, and soybean Kunitz inhibitor (SKTI) significantly inhibited trypsin activity. The l-1-tosyl-amido-2-phenylethylchloromethyl ketone (TPCK), pepstatin A, E-64, ethylenediamine tetraacetic acid, and calcium ions did not affect the enzyme activity at the concentrations tested. We infer the purified trypsins do not require calcium ions, by which they differ from the trypsins of other microorganisms and the soluble and insoluble trypsins characterized from A. gemmatalis. These data suggest the existence of different isoforms of trypsin in the velvetbean caterpillar midguts.
Palavras-chave: Bacteria
Pest control
Protease inhibitor
Trypsin
Editor: Archives of Insect Biochemistry and Physiology
Tipo de Acesso: Open Access
URI: https://doi.org/10.1002/arch.21407
http://www.locus.ufv.br/handle/123456789/13606
Data do documento: 1-Ago-2017
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