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Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae)
Several species of pentatomid bugs feed on pistachio fruits in Iran. Acrosternum arabicum Wagner (Hemiptera: Pentatomidae) is one of the most important pests of pistachio in Rafsanjan, Iran. This study was carried out to investigate the carbohydrase activities, supercooling points, and cold hardines...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7079678/ https://www.ncbi.nlm.nih.gov/pubmed/28076282 http://dx.doi.org/10.1093/jisesa/iew045 |
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author | Mohammadzadeh, Mozhgan Izadi, Hamzeh |
author_facet | Mohammadzadeh, Mozhgan Izadi, Hamzeh |
author_sort | Mohammadzadeh, Mozhgan |
collection | PubMed |
description | Several species of pentatomid bugs feed on pistachio fruits in Iran. Acrosternum arabicum Wagner (Hemiptera: Pentatomidae) is one of the most important pests of pistachio in Rafsanjan, Iran. This study was carried out to investigate the carbohydrase activities, supercooling points, and cold hardiness profiles of different developmental stages of A. arabicum under laboratory conditions. The midgut amylolytic of A. arabicum showed an optimal pH at 7.0. The highest amylolytic activity was found in the female adults (35.41 ± 0.90 nmol/min/gut). The mean amylolytic activity measured in first instar nymph was 6.75 ± 0.54 nmol/min/gut. Midgut α- and β-glucosidase showed an optimal activity at pH 5 and 7, respectively. These activities increased from first (83 ± 5 and 54 ± 5 nmol/min, respectively) to fifth (881 ± 17 and 237 ± 14 nmol/min, respectively) instar nymphs. The enzyme activities increased in the adults. Midgut α- and β-galactosidase showed an optimal activity at pH 5. α- and β-galactosidase activities were low in the first instar nymphs (73 ± 5 and 21 ± 3 nmol/min, respectively). The level of α- and β-galactosidase activities in the female adults (533 ± 18 and 246 ± 6 nmol/min, respectively) was higher than the nymphs. The lowest super cooling points (−19 and −18.2 °C, respectively) and the highest cold hardiness (22 and 18% following 24 h exposure at − 20 °C, respectively) were recorded for the eggs and adult females. |
format | Online Article Text |
id | pubmed-7079678 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-70796782020-03-24 Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) Mohammadzadeh, Mozhgan Izadi, Hamzeh J Insect Sci Research Article Several species of pentatomid bugs feed on pistachio fruits in Iran. Acrosternum arabicum Wagner (Hemiptera: Pentatomidae) is one of the most important pests of pistachio in Rafsanjan, Iran. This study was carried out to investigate the carbohydrase activities, supercooling points, and cold hardiness profiles of different developmental stages of A. arabicum under laboratory conditions. The midgut amylolytic of A. arabicum showed an optimal pH at 7.0. The highest amylolytic activity was found in the female adults (35.41 ± 0.90 nmol/min/gut). The mean amylolytic activity measured in first instar nymph was 6.75 ± 0.54 nmol/min/gut. Midgut α- and β-glucosidase showed an optimal activity at pH 5 and 7, respectively. These activities increased from first (83 ± 5 and 54 ± 5 nmol/min, respectively) to fifth (881 ± 17 and 237 ± 14 nmol/min, respectively) instar nymphs. The enzyme activities increased in the adults. Midgut α- and β-galactosidase showed an optimal activity at pH 5. α- and β-galactosidase activities were low in the first instar nymphs (73 ± 5 and 21 ± 3 nmol/min, respectively). The level of α- and β-galactosidase activities in the female adults (533 ± 18 and 246 ± 6 nmol/min, respectively) was higher than the nymphs. The lowest super cooling points (−19 and −18.2 °C, respectively) and the highest cold hardiness (22 and 18% following 24 h exposure at − 20 °C, respectively) were recorded for the eggs and adult females. Oxford University Press 2016-07-01 /pmc/articles/PMC7079678/ /pubmed/28076282 http://dx.doi.org/10.1093/jisesa/iew045 Text en © The Author 2016. Published by Oxford University Press on behalf of the Entomological Society of America. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Article Mohammadzadeh, Mozhgan Izadi, Hamzeh Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) |
title | Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) |
title_full | Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) |
title_fullStr | Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) |
title_full_unstemmed | Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) |
title_short | Enzyme Activity, Cold Hardiness, and Supercooling Point in Developmental Stages of Acrosternum arabicum (Hemiptera: Pentatomidae) |
title_sort | enzyme activity, cold hardiness, and supercooling point in developmental stages of acrosternum arabicum (hemiptera: pentatomidae) |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7079678/ https://www.ncbi.nlm.nih.gov/pubmed/28076282 http://dx.doi.org/10.1093/jisesa/iew045 |
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