Secretion of β-glycosidase by middle midgut cells and its recycling in the midgut of Tenebrio molitor larvae

Ferreira, Aryel H.; Ribeiro, Alberto F.; Terra, Walter R.; Ferreira, Clélia

doi:10.1016/s0022-1910(01)00151-2

Cited by 26 publications

(9 citation statements)

References 22 publications

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“…The b-glycosidases characterized in this study showed a broad pH optimum at 5.4, similar to the b-glycosidases from M. mulleri (Rouland et al, 1992), Neotermes koshunensis (Shiraki) (Isoptera: Kalotermitidae) (Tokuda et al, 2002), Cicer arietinum (Hosel, 1976), T. nonproteolyticus HG 102 (Xiangyuan et al, 2001), but different to the b-glycosidases from T. molitor larvae (Ferreira et al, 2002), Aspergillus oryzae (4.8) (Petrova et al, 2003), D. saccharalis midgut at 6.7, 6.3 and 7.2, respectively (Azevedo et al, 2003) and Sorghum bicolor Moench seedlings (6.2) (Hosel et al, 1987). Like the b-glycosidases characterized from different organisms, the b-glycosidases from M. subhyalinus p HMB, parahydroxymercuribenzoate workers were also stable over a wide range of pH and temperature.…”

Section: Discussionsupporting

confidence: 51%

Biochemical and catalytic properties of two β-glycosidases purified from workers of the termite Macrotermes subhyalinus (Isoptera: Termitidae)

Kouamé

Kouame

Niamké

et al. 2005

JTI

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Two b-glycosidases were purified from the termite Macrotermes subhyalinus (Rambur) workers by chromatography on gel filtration, ion exchange and hydrophobic interaction columns. The preparations were shown to be homogeneous on polyacrylamide gel. Both enzymes have a similar molecular mass (68 KDa) and optimum pH (5.4) but differ in optimal temperature and thermal stability. The b-glycosidases preferred b-fucosides to b-glucosides, b-galactosides and b-xylosides, and hydrolysed glucoseglucose-b-(1 -4) linkages better than b-(1 -3), b-(1 -2) and b-(1 -6) linkages. They did not hydrolyse saccharides such as melibiose, sucrose, lactose, xylobiose, melizitose, stachyose, lactose, raffinose, laminarin, arabinogalactan, carboxymethylcellulose, inulin, lichenan and starch. b-Glycosidase A and b-glycosidase B of M. subhyalinus workers are capable of catalysing transglucosylation reactions. The yields of glucosylation of hydroxyamino acid derivatives and phenylethanol, catalysed by the two enzymes in the presence of cellobiose as glucosyl donor, were lower than those reported previously with conventional sources of b-glycosidases. In addition, the optimum pH is different for the hydrolysis and transglucosylation reactions.On the basis of this work, it is proposed that the physiological role of b-glycosidase A and b-glycosidase B of M. subhyalinus workers is the digestion of di-and oligosaccharides derived from hemicelluloses and celluloses. q ICIPE 2005 les réactions de transglucosylation. Les rendements des réactions de glucosylation des dérivés d'hydroxyaminoacides et du phényléthanol, en présence de cellobiose comme donneur de glucosyle, sont plus faibles que ceux rapportés par les sources conventionnelles de glycosidases. De plus, les pH optimums d'hydrolyse et de transglycosylation sont différents.A partir de ces résultats, nous pouvons dire que le rô le physiologique des bglycosidases A et B de l'ouvrier du termite M. subhyalinus est de digérer les di et oligosaccharides provenant des hémicelluloses et des celluloses.

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Section: Discussionsupporting

confidence: 51%

Biochemical and catalytic properties of two β-glycosidases purified from workers of the termite Macrotermes subhyalinus (Isoptera: Termitidae)

Kouamé

Kouame

Niamké

et al. 2005

JTI

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“…β-glucosidase activity has also been measured in guts of numerous invertebrates (5, 143, 151, 157, 183, 374, 391). β-glucosidase activity is reduced in some insects that have either been selected for tolerance to plant glycosides (114) or habituated to diets with higher levels of glycosides (152, 355).…”

Section: Interactions Between Naturally Occurring Toxins and Digestivmentioning

confidence: 99%

Comparative Digestive Physiology

Karasov

Douglas

2013

Comprehensive Physiology

242

219

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In vertebrates and invertebrates, morphological and functional features of gastrointestinal (GI) tracts generally reflect food chemistry, such as content of carbohydrates, proteins, fats, and material(s) refractory to rapid digestion (e.g., cellulose). The expression of digestive enzymes and nutrient transporters approximately matches the dietary load of their respective substrates, with relatively modest excess capacity. Mechanisms explaining differences in hydrolase activity between populations and species include gene copy number variations and single-nucleotide polymorphisms. Transcriptional and posttranscriptional adjustments mediate phenotypic changes in the expression of hydrolases and transporters in response to dietary signals. Many species respond to higher food intake by flexibly increasing digestive compartment size. Fermentative processes by symbiotic microorganisms are important for cellulose degradation but are relatively slow, so animals that rely on those processes typically possess special enlarged compartment(s) to maintain a microbiota and other GI structures that slow digesta flow. The taxon richness of the gut microbiota, usually identified by 16S rRNA gene sequencing, is typically an order of magnitude greater in vertebrates than invertebrates, and the interspecific variation in microbial composition is strongly influenced by diet. Many of the nutrient transporters are orthologous across different animal phyla, though functional details may vary (e.g., glucose and amino acid transport with K+ rather than Na+ as a counter ion). Paracellular absorption is important in many birds. Natural toxins are ubiquitous in foods and may influence key features such as digesta transit, enzymatic breakdown, microbial fermentation, and absorption

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“…The properties and secretion of their b-glycosidases has already been studied (Ferreira et al, 2001(Ferreira et al, , 2002.…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization and sequencing of the major β-1,3-glucanase from the midgut of Tenebrio molitor larvae

Genta

Bragatto

Terra

et al. 2009

Insect Biochemistry and Molecular Biology

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Secretion of β-glycosidase by middle midgut cells and its recycling in the midgut of Tenebrio molitor larvae

Cited by 26 publications

References 22 publications

Biochemical and catalytic properties of two β-glycosidases purified from workers of the termite Macrotermes subhyalinus (Isoptera: Termitidae)

Biochemical and catalytic properties of two β-glycosidases purified from workers of the termite Macrotermes subhyalinus (Isoptera: Termitidae)

Comparative Digestive Physiology

Purification, characterization and sequencing of the major β-1,3-glucanase from the midgut of Tenebrio molitor larvae

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