Purification of three cellulases from the xylophageous larvae of Ergates faber (Coleoptera:Cerambycidae)

Chararas, C.; Eberhard, Ralf; Courtois, Jean-Patrice; Petek, F

doi:10.1016/0020-1790(83)90086-0

Cited by 39 publications

(18 citation statements)

References 17 publications

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“…Two components (53.6 and 48.8 kDa) were isolated from the wood-eating cockroach P. cribrata [65], another two (41 and 42 kDa) from the lower termite R. speratus [66], and one more (47 kDa) from the Japanese arboreal higher termite N. takasagoensis [67]. In another insect taxon, Coleoptera, which is less related to termites and cockroaches, two b-glucosidase components (57 and 70 kDa) and a CBH component (25 kDa) were purified from larvae of the xylophagous beetle Ergates faber [68]. Aside from insects, two cellulolytic components (30 and 40 kDa; possibly EG or CBH) were purified from crayfish.…”

Section: Purification and Character Of Animal Cellulasesmentioning

confidence: 99%

Animal cellulases

Watanabe¹,

Tokuda

2001

CMLS, Cell. Mol. Life Sci.

261

149

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Previous dogma has maintained that cellulose, ingested by xylophagous or herbivorous animals, is digested by cellulolytic symbiotes. The first evidence in conflict with this contention involved the demonstration of cellulolytic activities in symbiote-free secreting organs (e.g., the salivary glands of termites) or defaunated guts. Following these demonstrations, possible endogenous cellulase components were purified from several cellulose-digesting invertebrates, but this research did little to change the general view concerning animal cellulose digestion. Thanks to recent developments in molecular biology, the existence of cellulases of animal origin has been firmly established. To date, cellulase genes have been reported from arthropods (insects and a crayfish) and nematodes. This paper describes and discusses the presence and nature of endogenous cellulases in higher animals.

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Section: Purification and Character Of Animal Cellulasesmentioning

confidence: 99%

Animal cellulases

Watanabe¹,

Tokuda

2001

CMLS, Cell. Mol. Life Sci.

261

149

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“…Indeed, cellulose digestion in insects is rare, because the dietary factor that usually limits growth in plant feeders would be protein quality and not the type of carbohydrate present [2]. Only few insects secrete enzymes able to hydrolyse crystalline cellulose [27,28] because, insects were generally dependent on symbionts for cellulose digestion [29,30]. Furthermore, earlier studies have revealed the presence of symbiotic microorganisms in the gut of another pest, namely red palm weevil of the genus Rhynchophorus [31].…”

Section: Discussionmentioning

confidence: 99%

α-Mannosidases from the Digestive Fluid of Rhynchophorus Palmarum Larvae as Novel Biocatalysts for Transmannosylation Reactions

Bédikou

Koné

Ahi

et al. 2009

Appl Biochem Biotechnol

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Two biological fluids, namely hemolymph and digestive fluid from the larval stage of Rhynchophorus palmarum Linneaus, a serious pest in agroecosystem exploiting oil palm, were screened for hydrolytic activities, by the use of synthetic and natural glycoside substrates. Several exo and endoglycosidase activities were observed but, the interesting alpha-mannosidase activity (0.41 +/- 0.04 UI) had attracted our attention. So, we have previously demonstrated that this activity harbours four distinctive alpha-mannosidase isoforms named RpltM, RplM1, RplM2 and RplM3. We have extended this work to determine the ability of these enzymes to catalyze synthesis reactions. Finally, we have revealed that, alpha-mannosidases from the digestive fluid of R. palmarum larvae catalyze transmannosylation reactions. The stability of the enzymes and the optimization of the transfer product yield were studied as functions of pH, enzyme unit, starting concentration of donor or acceptor and time. It was shown that, in experimental optimum conditions, average yields of 12.34 +/- 0.75, 12.15 +/- 0.79, 5.59 +/- 0.35 and 8.43 +/- 0.50% were obtained for the alpha-mannosidases RpltM, RplM1, RplM2 and RplM3, respectively. On the basis of this work, alpha-mannosidases from the digestive fluid of Rhynchophorus palmarum larvae appear to be a valuable tool for the preparation of neoglycoconjugates.

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“…Yeasts can degrade cellulose, the most abundant carbon source on earth, and other complex polysaccharides 95 to easily consumable glucose that serves as a carbon and energy source for microorganisms in soil. Yeasts can degrade cellulose, the most abundant carbon source on earth, and other complex polysaccharides 95 to easily consumable glucose that serves as a carbon and energy source for microorganisms in soil.…”

Section: Discussionmentioning

confidence: 99%

Natural fruits, flowers, honey, and honeybees harborHelicobacter pylori‐positive yeasts

et al. 2018

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Different genera of osmotolerant yeasts from flowers, fruits, honey, and honeybees contained H. pylori in their vacuole. High frequency of H. pylori-positive yeasts in these samples might be related to their high sugar content. Insects such as honeybees that facilitate transfer and easy access of these yeasts to nectars serve as the main reservoirs of these yeasts, playing an important role in their protection and dispersal. Accordingly, H. pylori inside these yeasts can be carried by honeybees to different sugar- and nutrient-rich environments. Sugar-rich environments and honeybees play an important role in distribution of H. pylori-positive yeasts in nature.

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Purification of three cellulases from the xylophageous larvae of Ergates faber (Coleoptera:Cerambycidae)

Cited by 39 publications

References 17 publications

Animal cellulases

Animal cellulases

α-Mannosidases from the Digestive Fluid of Rhynchophorus Palmarum Larvae as Novel Biocatalysts for Transmannosylation Reactions

Natural fruits, flowers, honey, and honeybees harborHelicobacter pylori‐positive yeasts

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