Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine

Detalhes bibliográficos
Autor(a) principal: Pilon, Anderson M.
Data de Publicação: 2006
Outros Autores: Guedes, Raul Narciso C., Oliveira, Maria Goreti A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://doi.org/10.1016/j.pestbp.2005.11.005
http://www.locus.ufv.br/handle/123456789/22593
Resumo: Protein digestibility, proteolytic activity, and post-embryonic development of Anticarsia gemmatalis (Hübner) (Lepidoptera: Noctuidae) were assessed in larvae reared on artificial diet containing 0.00, 0.25, 0.50, and 0.75% (w/w) of the synthetic trypsin inhibitor benzamidine. Diet consumption was affected by the inhibitor when the insects were exposed to 0.50% benzamidine showing a 4-day delay and a 70%-higher peak of consumption. Larva weight gain was also affected by benzamidine and again the results of 0.50% benzamidine were unexpected due to the worst performance of the insects at this inhibitor concentration and not at 0.75% benzamidine. These patterns of consumption and weight gain were however consistent with the results of protein digestibility, which affects larvae mortality and adult emergence. The insect proteolytic activity was also affected by benzamidine, particularly at 0.50%. These results indicate that the insects are able to circumvent the potentially harmful effects of the inhibitor since at the highest concentration the negative impact is mitigated.
id UFV_ea6ae093435acb68b1a6fbf5983adbf6
oai_identifier_str oai:locus.ufv.br:123456789/22593
network_acronym_str UFV
network_name_str LOCUS Repositório Institucional da UFV
repository_id_str 2145
spelling Pilon, Anderson M.Guedes, Raul Narciso C.Oliveira, Maria Goreti A.2018-11-26T18:37:06Z2018-11-26T18:37:06Z2006-090048-3575https://doi.org/10.1016/j.pestbp.2005.11.005http://www.locus.ufv.br/handle/123456789/22593Protein digestibility, proteolytic activity, and post-embryonic development of Anticarsia gemmatalis (Hübner) (Lepidoptera: Noctuidae) were assessed in larvae reared on artificial diet containing 0.00, 0.25, 0.50, and 0.75% (w/w) of the synthetic trypsin inhibitor benzamidine. Diet consumption was affected by the inhibitor when the insects were exposed to 0.50% benzamidine showing a 4-day delay and a 70%-higher peak of consumption. Larva weight gain was also affected by benzamidine and again the results of 0.50% benzamidine were unexpected due to the worst performance of the insects at this inhibitor concentration and not at 0.75% benzamidine. These patterns of consumption and weight gain were however consistent with the results of protein digestibility, which affects larvae mortality and adult emergence. The insect proteolytic activity was also affected by benzamidine, particularly at 0.50%. These results indicate that the insects are able to circumvent the potentially harmful effects of the inhibitor since at the highest concentration the negative impact is mitigated.engPesticide Biochemistry and PhysiologyVolume 86, Issue 1, Pages 23-29, September 20062006 Elsevier Inc. All rights reserved.info:eu-repo/semantics/openAccessInsect digestionSerine proteasesProtease inhibitionAdaptation to protease inhibitorsNoctuidaeProtein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidineinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf251624https://locus.ufv.br//bitstream/123456789/22593/1/artigo.pdf1998f687b3ffb3927c9a64464db62a95MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/22593/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/225932018-11-26 15:59:52.091oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-11-26T18:59:52LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
title Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
spellingShingle Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
Pilon, Anderson M.
Insect digestion
Serine proteases
Protease inhibition
Adaptation to protease inhibitors
Noctuidae
title_short Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
title_full Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
title_fullStr Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
title_full_unstemmed Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
title_sort Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine
author Pilon, Anderson M.
author_facet Pilon, Anderson M.
Guedes, Raul Narciso C.
Oliveira, Maria Goreti A.
author_role author
author2 Guedes, Raul Narciso C.
Oliveira, Maria Goreti A.
author2_role author
author
dc.contributor.author.fl_str_mv Pilon, Anderson M.
Guedes, Raul Narciso C.
Oliveira, Maria Goreti A.
dc.subject.pt-BR.fl_str_mv Insect digestion
Serine proteases
Protease inhibition
Adaptation to protease inhibitors
Noctuidae
topic Insect digestion
Serine proteases
Protease inhibition
Adaptation to protease inhibitors
Noctuidae
description Protein digestibility, proteolytic activity, and post-embryonic development of Anticarsia gemmatalis (Hübner) (Lepidoptera: Noctuidae) were assessed in larvae reared on artificial diet containing 0.00, 0.25, 0.50, and 0.75% (w/w) of the synthetic trypsin inhibitor benzamidine. Diet consumption was affected by the inhibitor when the insects were exposed to 0.50% benzamidine showing a 4-day delay and a 70%-higher peak of consumption. Larva weight gain was also affected by benzamidine and again the results of 0.50% benzamidine were unexpected due to the worst performance of the insects at this inhibitor concentration and not at 0.75% benzamidine. These patterns of consumption and weight gain were however consistent with the results of protein digestibility, which affects larvae mortality and adult emergence. The insect proteolytic activity was also affected by benzamidine, particularly at 0.50%. These results indicate that the insects are able to circumvent the potentially harmful effects of the inhibitor since at the highest concentration the negative impact is mitigated.
publishDate 2006
dc.date.issued.fl_str_mv 2006-09
dc.date.accessioned.fl_str_mv 2018-11-26T18:37:06Z
dc.date.available.fl_str_mv 2018-11-26T18:37:06Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1016/j.pestbp.2005.11.005
http://www.locus.ufv.br/handle/123456789/22593
dc.identifier.issn.none.fl_str_mv 0048-3575
identifier_str_mv 0048-3575
url https://doi.org/10.1016/j.pestbp.2005.11.005
http://www.locus.ufv.br/handle/123456789/22593
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartofseries.pt-BR.fl_str_mv Volume 86, Issue 1, Pages 23-29, September 2006
dc.rights.driver.fl_str_mv 2006 Elsevier Inc. All rights reserved.
info:eu-repo/semantics/openAccess
rights_invalid_str_mv 2006 Elsevier Inc. All rights reserved.
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Pesticide Biochemistry and Physiology
publisher.none.fl_str_mv Pesticide Biochemistry and Physiology
dc.source.none.fl_str_mv reponame:LOCUS Repositório Institucional da UFV
instname:Universidade Federal de Viçosa (UFV)
instacron:UFV
instname_str Universidade Federal de Viçosa (UFV)
instacron_str UFV
institution UFV
reponame_str LOCUS Repositório Institucional da UFV
collection LOCUS Repositório Institucional da UFV
bitstream.url.fl_str_mv https://locus.ufv.br//bitstream/123456789/22593/1/artigo.pdf
https://locus.ufv.br//bitstream/123456789/22593/2/license.txt
bitstream.checksum.fl_str_mv 1998f687b3ffb3927c9a64464db62a95
8a4605be74aa9ea9d79846c1fba20a33
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)
repository.mail.fl_str_mv fabiojreis@ufv.br
_version_ 1801213071711010816