Digestive proteolytic activity in larvae and adults of Bactrocera oleae Gmelin (Diptera: Tephritidae)

Delkash-Roudsari, Sahar; Zibaee, Arash; Abbci-Mozhdehi, Mohammad Reza

doi:10.1016/j.aspen.2014.04.002

Cited by 7 publications

(3 citation statements)

References 36 publications

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“…Temperature is another critical factor of enzymatic activity in media. Elevating media temperature to optimal values enhances the rate of the enzyme-catalysing reaction due to high kinetic energy and collision frequency of the engaged molecules (Delkash-Roudsari et al, 2014). Active-site localisation of the transition is not unexpected, given that conformational flexibility is often inherent in a catalytic enzyme mechanism.…”

Section: Discussionmentioning

confidence: 99%

Ontogenic development of the digestive enzymes and chemical composition of Hermetia illucens larvae of different ages

Intayung

Chundang

Srikachar

et al. 2021

Entomologia Exp Applicata

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The production of the black soldier fly (BSF), Hermetia illucens L. (Diptera: Stratiomyidae), has potential to promote sustainable food production, and is environmentally friendly through organic waste upcycling. The objective of this study was to determine the digestive enzyme activities and chemical composition of BSF larvae of 6, 12, and 18 days old at various substrate pH and temperature conditions during ontogenic development. Cellulase and chymotrypsin‐like protease (C) activities declined slightly with age, whereas a sharp increase in lipase activity was found with age. High levels of amylase, trypsin‐like protease (T), trehalase, and T/C ratio were present in 12‐day‐old BSF, with a gradual decrease in 18‐day‐old BSF. The highest crude protein and lipid levels were observed at 6 and 18 days of age, respectively. In conclusion, the activities of the various types of enzymes illustrate the polyphagous nature of BSF. Most of the digestive enzymes had high activity at an early age and then dropped at the end of the larval stage; however, the opposite trend was observed in lipase activity, with a high level of fat accumulation in the last stage of larval development.

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Section: Discussionmentioning

confidence: 99%

Ontogenic development of the digestive enzymes and chemical composition of Hermetia illucens larvae of different ages

Intayung

Chundang

Srikachar

et al. 2021

Entomologia Exp Applicata

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“…Hence, the majority of digestive proteases of the larvae are soluble rather than membrane-bound. Moreover, suggestion of Terra & Ferreira (2012) may not be common for all insects since our previous studies on the larvae of U. pulchella, P. demoleus and Bacterocera oleae Gmelin (Diptera: Tephritidae) showed the soluble nature of digestive proteases (Ajamhassani et al, 2012;Yazdani et al, 2013;Delkash-Roudsari et al, 2014). In addition, different assayed proteases had various activities in the anterior-and posterior-midgut preparations.…”

Section: Discussionmentioning

confidence: 85%

Determination of digestive proteolytic profile in the larvae of Dyspessa palidata (Staudinger) (Lepidoptera: Cossidae)

Mardani-Talaee

Zibaee

2015

J Entomol Acarol Res

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Digestive proteolytic profile was determined in the larvae of Dyspessa palidata (Staudinger), which is the most important pest of Alliaceae in Europe and Iran. Compartmentalisation of the proteolytic activities by considering soluble and membrane-bound fractions revealed that soluble fractions of the whole midgut preparations had higher general proteolytic activity than membrane-bound fractions. Also, four proteolytic bands were observed in the soluble fraction of the total midgut preparation in electrophoresis. Compartmentalisation of the specific proteases revealed presence of trypsin, elastase, aminoand carboxy peptidases in posterior midgut but the highest activities of other proteases were found in anterior midgut. The highest activity of general protease was found at pHs of 6 and 8. Also, pH dependency of trypsin, chymotrypsin and elastase were found at values of 8, 7-8 and 9 but cathepsins had the optimal pH at 6. Exopeptidases showed the optimal value at pH of 7 although carboxypeptidase showed same activity at values of 6 and 7. The inhibitory concentrations 50% (IC50) of AEBSF.HCL on trypsin, chymotrypsin and elastase proteases were found to be 3.69, 3.31 and 4.09 mM, respectively. IC50 concentrations of TLCK, SBTI and TPCK significantly inhibited trypsin and chymotrypsin activities. IC50 of E-64 were 3.67 and 4.16 mM on cathepsin B and L but cystatin revealed 5.22 and 4.48 mM concentrations on cathepsin B and L, respectively. EDTA and phenathroline as metalloproteinase inhibitors had IC50 of 3.25 and 3.91 mM on general proteolytic activity. Results of the current study revealed larvae of D. palidata utilised different proteases to increase digestive efficiency when they fed on the host plants containing several toxic molecules.

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“…The high molecular mass trypsins found in some lepidopteran (Brito et al., ; Oliveira et al., ; Zibaee et al., ) and coleopteran species (Wagner et al., ; Hosseininaveh et al., ; Silva et al., ; Castro‐Guillén et al., ) have been suggested to result from oligomerisation, which interferes with binding of proteinaceous inhibitors present in their food. Also, the maintenance of high trypsin and proteinase activity within wide pH range in insects that use different isozymes and different mechanistic classes of proteinases, enables efficient digestion of proteins under variable gut conditions or simply reflects divergence in structure important for digestion of heterogeneous food proteins and circumventing proteinase inhibitors (Ortego et al., ; Zeng et al., ; Silva et al., ; Wright et al., ; Castro‐Guillén et al., ; Sorkhabi‐Abdolmaleki et al., ; Delkash‐Roudsari et al., ).…”

Section: Structural Diversity Of Insect Digestive Trypsinsmentioning

confidence: 99%

Dietary and phylogenetic correlates of digestive trypsin activity in insect pests

Lazarević

Janković-Tomanić

2015

Entomologia Exp Applicata

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Because food proteins are crucial for insect survival, growth, and fecundity, enzymes involved in their digestion have attracted the attention of fundamental entomologists studying the mechanisms and patterns of dietary specialization, and applied entomologists searching for more efficient modes of pest control. Most insects digest proteins using trypsin, an endopeptidase that cleaves polypeptide chains on the carboxyl side of arginine and lysine, two basic amino acids. As the most ancestral proteinase, trypsin is wide-spread in the digestive tract of insects from various orders and with various feeding habits. The present review focuses on biochemical and molecular characteristics, mechanisms of regulation, and adaptive/non-adaptive changes of trypsin activity in response to heterogeneous food environments in a phylogenetic context. Within-and among-species variations in trypsin structure and regulation that contribute to better matching with specific food types are emphasized. We also discuss the relevance of these data for choosing an appropriate strategy for control of insect pests. Pest control strategies to reduce trypsin activity by interfering with substrate binding or trypsin synthesis and secretion have been suggested. Successful application of these procedures requires a multidisciplinary approach and knowledge about digestive physiology of the pest, as well as the structural characteristics of trypsins that determine their interaction with proteinaceous inhibitors and other food compounds, about patterns of developmental changes in trypsin gene expression, adaptive responses of insects to food composition, and various environmental effects on trypsin activity.

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Digestive proteolytic activity in larvae and adults of Bactrocera oleae Gmelin (Diptera: Tephritidae)

Cited by 7 publications

References 36 publications

Ontogenic development of the digestive enzymes and chemical composition of Hermetia illucens larvae of different ages

Ontogenic development of the digestive enzymes and chemical composition of Hermetia illucens larvae of different ages

Determination of digestive proteolytic profile in the larvae of Dyspessa palidata (Staudinger) (Lepidoptera: Cossidae)

Dietary and phylogenetic correlates of digestive trypsin activity in insect pests

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