Purification and properties of a β-glycosidase purified from midgut cells of Spodoptera frugiperda (Lepidoptera) larvae

Marana, Sandro R.; Terra, Walter R.; Ferreira, Clélia

doi:10.1016/s0965-1748(00)00090-4

Cited by 54 publications

(57 citation statements)

References 22 publications

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“…In coleopterans, which feed on a diet rich in starch, the predominant endoglycosidases are the a-amylases (Ishimoto and Kitamura, 1989;Lemos et al, 1990;Grossi de Sa´and Chrispeels, 1997;Silva et al, 1999;Titarenko and Chrispeels, 2000;Cristofoletti et al, 2001). In Lepdopterans, which feed on leaves, exoglycosidase(s)-like b-glycosidases are predominantly present (Marana et al, 2000), and Hemipterans, which are plant feeders, use b-galactosidases to digest the carbohydrates present in their diet (Ferreira et al, 1998). Dipterans, which feed on blood, use alkaline a-glucosidases during meal digestion (Dillon and Kordy, 1997) and those that feed on plants, use mainly b-galactosidases (Ferreira et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Silva

Alcazar

Macedo

et al. 2006

Insect Biochemistry and Molecular Biology

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The digestive system of Ceratitis capitata was characterized during its larval development and in the insect stage. Disaccharidases against maltose and sucrose were more evident in the 2nd and 3rd day of larval development and in the adult stage, respectively. Glycosil-hydrolyses with higher specific a-galactosidasic and b-galactosidasic activities were detected in the 2nd and 3rd day of the larval stage, respectively. Specific proteolytic activities against azocasein showed an increase in the 4th and 5th day of the larval stage and in the adult stage. Specific hemoglobin activities were constant between 2nd and 6th day of the larval stage. The larvae used mainly serine proteinases, such as trypsin/chymotrypsin, and the adult insects only chymotrypsin-like enzymes in their digestive process. Two serine proteinases were separated from zymogram between the 4th and 5th day of larval development and in the adult stage. Effect of soybean trypsin inhibitor (SBTI, a serine proteinase inhibitor) on development of C. capitata was examined by bioassay. C. capitata was susceptible to SBTI which affected larval mass at ED 50 3.01%. r

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Section: Discussionmentioning

confidence: 99%

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Silva

Alcazar

Macedo

et al. 2006

Insect Biochemistry and Molecular Biology

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“…Cellobiohydrolases appear to play no role in the initial digestion of cellulose by termites and wood-eating cockroaches (Watanabe and Tokuda, 2010); cellulolytic systems from these insects consist of multiple endo--1,4-glucanases and -glucosidases (Genta et al, 2003;Schulz et al, 1986;Scrivener and Slaytor, 1994;Slaytor, 1992;Tokuda et al, 1999). Other invertebrate endo--1,4-glucanases are known to produce cellobiose, cellotriose and cellotetraose (Watanabe and Tokuda, 2010;Xu and Distel, 2004), whereas partially purified -glucosidases from other species are able to hydrolyse cellotriose, cellotetraose and cellopentaose (Ferreira et al, 2001;Ferreira et al, 2003;Marana et al, 2000). It is possible that the cellulase system from these animals employs a similar mechanism to that of G. natalis.…”

Section: Discussionmentioning

confidence: 99%

The last piece in the cellulase puzzle: the characterisation of β-glucosidase from the herbivorous gecarcinid land crab Gecarcoidea natalis

Allardyce

Linton

Saborowski

2010

Journal of Experimental Biology

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SUMMARYA 160 kDa enzyme with -glucosidase activity was purified from the midgut gland of the land crab Gecarcoidea natalis. The enzyme was capable of releasing glucose progressively from cellobiose, cellotriose or cellotetraose. Although -glucosidases (EC 3.2.1.21) have some activity towards substrates longer than cellobiose, the enzyme was classified as a glucohydrolase (EC 3.2.1.74) as it had a preference for larger substrates (cellobiose

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“…In contrast, β-glucosidase activity in the salivary glands of Nasutitermes takasagoensis is more than 66% of total activity in the digestive system (Tokuda et al 1997). Previous works showed the presence of α-and β-glucosidase activities in the salivary glands of other phytophagous lepidopterans insect (Santo & Terra 1985;Franzl et al 1989;Ferreira et al 1997;Marana et al 2000;Ghadamyari et al 2010). …”

Section: Kinetic Parametersmentioning

confidence: 94%

“…Three β-glycosidases, named βGly1, βGly2 and βGly3, were isolated from midgut tissues of the sugar cane borer, D. saccharalis (Azevedo et al 2003). Also, two β-glycosidases were purified from S. frugiperda midgut (Marana et al 2000). The results of Riseh et al (2012) indicated two and three isoforms of α-and β-glucosidases in crude digestive system extract of last larval instar of R. ferrugineus, respectively.…”

Section: Kinetic Parametersmentioning

confidence: 99%

Biochemical characterization of α- and β-glucosidases in alimentary canal, salivary glands and haemolymph of the rice green caterpillar, Naranga aenescens M. (Lepidoptera: Noctuidae)

et al. 2012

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The biochemical properties of α- and β-glucosidase in salivary glands, alimentary canal and haemolymph of Naranga aenescens larvae, one of the most damaging pests of the rice crop in Iran, were investigated. The specific activity of α-glucosidases were 3.88, 2.74 and 1.58 μmol/min per mg protein in the alimentary canal, salivary glands and haemolymph of last instar larvae, respectively. The specific activity of β-glucosidases were 1.27, 0.077 and 0.414 μmol/min per mg protein in the alimentary canal, salivary glands and haemolymph of last instar larvae, respectively. The optimal pH for α-glucosidases were 6.0, 6.0–8.0 and 6.0 and the maximum activity for β-glucosidases were obtained at pH 6.0, 5.0–7.0 and 5.0 in alimentary canal, salivary glands and haemolymph, respectively. The optimum temperatures for β-glucosidases were determined at 55°C in alimentary canal, 35–45°C in salivary glands and 55°C in haemolymph, whereas the α-glucosidases reached their optimum at 45°C in all three tissues. Effect of metal ions on the activity of α- and β-glucosidases showed that K+ (20 mM) and Mg2+ (10 and 20 mM) increased N. aenescens α- and β-glucosidases activities from salivary glands, while Ca2+ increased α- and β-glucosidases activities in haemolymph. In the presence of Fe2+, Mn2+, Hg+ and Zn2+ (10, 20 mM) and Hg2+ (20 mM), these enzymes from all tissues were completely inactivated. K m values were estimated for the α-glucosidases as 3.96, 0.547 and 3.084 mM and for β-glucosidases as 1.93, 1.014 and 1.93 mM in the alimentary canal, salivary gland and haemolymph, respectively. The zymogram analyses of N. aenescens crude extracts indicated the presence of at least two isoforms for α-glucosidase and one isoform for β-glucosidase.

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Purification and properties of a β-glycosidase purified from midgut cells of Spodoptera frugiperda (Lepidoptera) larvae

Cited by 54 publications

References 22 publications

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

The last piece in the cellulase puzzle: the characterisation of β-glucosidase from the herbivorous gecarcinid land crab Gecarcoidea natalis

Biochemical characterization of α- and β-glucosidases in alimentary canal, salivary glands and haemolymph of the rice green caterpillar, Naranga aenescens M. (Lepidoptera: Noctuidae)

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