Prospecting for cellulolytic activity in insect digestive fluids

Oppert, Cris; Klingeman, William E.; Willis, Jonathan D.; Oppert, Brenda; Jurat-Fuentes, Juan Luís

doi:10.1016/j.cbpb.2009.10.014

Cited by 71 publications

(65 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The majority of PEs need for maximal activity an optimum temperature range from 40°C to 50°C (Assis et al 2004). Insects have evolved efficient strategies to use lignocellulosic substrates as sources of energy, which makes them an optimal resource for novel cellulolytic enzymes (Cleveland 1924;Oppert et al 2010;Watanabe & Tokuda 2010). The insect digestive system exhibits states that are optimised for degradation of plant biomass, as well as reducing conditions and high alkaline pH in a number of insect orders (Lehane & Billingsley 1996).…”

Section: +mentioning

confidence: 99%

See 1 more Smart Citation

Plant cell wall degrading enzymes, pectinase and cellulase, in the digestive system of the red palm weevil, Rhynchophorus ferrugineus (Coleoptera: Curculionidae)

et al. 2014

View full text Add to dashboard Cite

Vatanparast M., Hosseininaveh V., Ghadamyari M., Minoo Sajjadian S. (2014): Plant cell wall degrading enzymes, pectinase and cellulase, in the digestive system of the red palm weevil, Rhynchophorus ferrugineus (Coleoptera: Curculionidae). Plant Protect. Sci., In digestion, the red palm weevil, Rhynchophorus ferrugineus, has been adapted to overcome the plant cell wall barrier, specially lignocellulosic and pectic compounds, by producing cellulase and pectinase enzymes. Partial biochemical characterisations of cellulase and pectinase were determined in the larval digestive system of the pest. Larval midgut extract showed an optimum activity for cellulase and pectinase against carboxyl methyl cellulose and pectin at pH 6.0 and 7.0, respectively. Larval midgut cellulase and pectinase were more stable at pH 4.0-8.0 and pH 6.0-8.0 than in highly acidic and alkaline condition, respectively. However, cellulase and pectinase showed to be more stable at pH 6.0 and 7.0, respectively, when the incubation time increased. Maximum activity for cellulase and pectinase incubated at different temperatures was observed at 50°C. Cellulase and pectinase activity significantly decreased in the presence of EDTA and SDS. On the contrary, Ca 2+ , Mg 2+, and Na + significantly affect pectinase activity and K + did not affect the enzyme activities. Ca 2+ and Mg 2+ increased cellulase activity as well. K M and V max for pectinase activity were 0.92 mg/ml and 290 units/mg. Zymogram analyses revealed the presence of one form of pectin methyl esterase and one form of cellulase in the larval digestive system.

show abstract

Section: +mentioning

confidence: 99%

“…Several insects from 12 orders, such as Dictyoptera, Orthoptera, and Coleoptera may produce their own cellulases (i.e. endo-β-1,4-glucanase) in their midguts and/or salivary glands (Willis 2009;Oppert et al 2010;Watanabe & Tokuda 2010). The term cellulase mainly includes three enzymes leading to glucose production from hydrolysing cellulose (Clarke 1996).…”

mentioning

confidence: 99%

Plant cell wall degrading enzymes, pectinase and cellulase, in the digestive system of the red palm weevil, Rhynchophorus ferrugineus (Coleoptera: Curculionidae)

et al. 2014

View full text Add to dashboard Cite

show abstract

“…Thus, cellulose digestion by locusts has been rarely studied. Oppert et al (2010) compared the cellulase activity of 8 orders of insects, and found that Orthoptera insects exhibited high intestinal cellulase activity that is similar to that of Coleoptera insects. Willis et al (2010) isolated and purified a type of cellulase from Dissosteira carolina.…”

Section: Introductionmentioning

confidence: 99%

Cellulolytic activity and structure of symbiotic bacteria in locust guts

Su¹,

Liu²,

Li³

et al. 2014

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. Locusts are able to digest the cellulose of Gramineae plants, resulting in their being considered as major crop pests. To illustrate the mechanism involved in cellulose digestion, the cellulolytic activity and zymography in the gut contents of 16 locust species were determined using carboxymethyl cellulose (CMC) as substrate. The diversity of gut symbiotic bacteria was studied using denaturing gradient gel electrophoresis (DGGE). The results showed that high CMC activity was present in Acrididae gut fluid (mean 356.4 U/g proteins). Of the 5 locust species, Oxya chinensis had the highest diversity of intestinal symbiotic bacteria, characterized by the DGGE profile containing more than 20 bands of 16S rRNA. Klebsiella pneumoniae, in the gut of Locusta migratoria manilensis, was identified as the most abundant symbiotic bacterium by DNA sequencing, with a relative abundance of 19.74%. In comparison, Methylobacterium sp was the most dominant species in the Atractomorpha sinensis gut, with a relative abundance of 29.04%. The results indicated that the cellulolytic enzymes and gut microbial Cellulolytic activity of symbiotic bacteria in locust guts communities probably reflected their phylogenetic relationship with different locust species and associated feeding strategies.

show abstract

“…A number of studies have addressed the capacity of mining insects in hydrolyzing cellulose and hemicellulose (e.g., Martin et al, 1981;Oppert et al, 2010). However, the different methods employed hinder the comparison of results with the present study.…”

Section: Discussionmentioning

confidence: 93%

“…The enzyme extractions was according to Oppert et al (2010). Cellulolytic and hemicellulolytic activities were assessed by the quantification of reducing sugars in a modified 3,5-dinitrosalicylic acid assay.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Lignocellulolytic enzymes and bacteria associated with the digestive tracts of Stenochironomus (Diptera: Chironomidae) larvae

Koroiva¹,

Souza²,

Toyama³

et al. 2013

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. We analyzed the digestive activity of the enzymes that digest cellulose and hemicellulose and the bacterial community that is capable of hydrolyzing wood compounds in the digestive tracts of Stenochironomus (Diptera: Chironomidae) larvae, which are miners of decomposing submerged tree and bush branches. Based on quantification of reducing sugars, these larvae have a limited capacity for cellulose degradation but a good capacity for xylan hydrolysis. We isolated 31 types of colonies from two larval morphotypes, of which 19 tested positive for the capacity to hydrolyze at least one of the four substrates that were used as the main carbon source in the culture media. Their woody compound degradation capacity was assessed using colorimetric tests. The bacteria were identified by the analysis of the 16S rRNA gene. None of the bacteria were capable of degrading lignin. The genus Pseudomonas had the greatest species richness; Bacillus spp exhibited the greatest capacity for degrading the different substrates, and Sphingobium was found in both morphotypes. Microorganisms participate in the degradation of wood consumed by Stenochironomus larvae. This is the first report of lignocellulolytic bacteria and enzymes in the digestive tracts of mining chironomids.

show abstract

Prospecting for cellulolytic activity in insect digestive fluids

Cited by 71 publications

References 35 publications

Plant cell wall degrading enzymes, pectinase and cellulase, in the digestive system of the red palm weevil, Rhynchophorus ferrugineus (Coleoptera: Curculionidae)

Plant cell wall degrading enzymes, pectinase and cellulase, in the digestive system of the red palm weevil, Rhynchophorus ferrugineus (Coleoptera: Curculionidae)

Cellulolytic activity and structure of symbiotic bacteria in locust guts

Lignocellulolytic enzymes and bacteria associated with the digestive tracts of Stenochironomus (Diptera: Chironomidae) larvae

Contact Info

Product

Resources

About