Correlation of cellulase gene expression and cellulolytic activity throughout the gut of the termite Reticulitermes flavipes

Zhou, Xuguo; Smith, Joseph A.; Oi, Faith M.; koehler, Philip G.; Bennett, Gary W.; Scharf, Michael E.

doi:10.1016/j.gene.2007.01.004

Cited by 105 publications

(109 citation statements)

References 54 publications

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“…This combined with the large activity within the midgut gland suggests they are likely to be the product of the endogenous GHF9 gene present in crustaceans, and arthropods in general, and hence are synthesised endogenously within this tissue Crawford et al, 2004;Linton et al, 2006). Endo-β-1,4-glucanases from both G. natalis and C. destructor are also most probably glycosylated given that glycosylation is a common feature of GHF9 endo-β-1,4-glucanases from other arthropods (Table 7) (Lee et al, 2005;Nishida et al, 2007;Zhou et al, 2007). Glycosylation may prevent proteolytic degradation and thus may explain why the endo-β-1,4-glucanases are relatively stable (Langsford et al, 1987).…”

Section: Endo-β-14-glucanase Characteristicsmentioning

confidence: 99%

Purification and characterisation of endo-β-1,4-glucanase and laminarinase enzymes from the gecarcinid land crab Gecarcoidea natalis and the aquatic crayfish Cherax destructor

Allardyce

Linton

2008

Journal of Experimental Biology

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SUMMARY 2.1.4) from G. natalis had a molecular mass of 52 kDa and an optimum pH of 4-7. It mainly hydrolysed β-1,4-glycosidic bonds, but was also capable of significant hydrolysis of β-1,3-glycosidic bonds. Two endo-β-1,4-glucanases, termed 1 and 2, with respective molecular masses of 53±3 and 52 kDa, were purified from C. destructor. Endo-β-1,4-glucanase 1 was only capable of hydrolysing β-1,4-glycosidic bonds and had an optimum pH of 5.5. Endo-β-1,4-glucanases from both species produced some glucose, cellobiose and other short oligomers from the hydrolysis of carboxymethyl cellulose.

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Section: Endo-β-14-glucanase Characteristicsmentioning

confidence: 99%

Purification and characterisation of endo-β-1,4-glucanase and laminarinase enzymes from the gecarcinid land crab Gecarcoidea natalis and the aquatic crayfish Cherax destructor

Allardyce

Linton

2008

Journal of Experimental Biology

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“…The Reticulitermes speratus cellulase (RsEG) encodes an endo-β (1,4)-glucanase (Watnabe et al, 1998). The compartmentalization of the cellulose digestion by endogenous and exogenous cellulolytic enzymes in diverse regions of the digestive tract has been extensively studied to optimize cellulose digestion in termites (Nakashima et al, 2002;Tokuda and Watanabe 2007;Zhou et al, 2007). Traditionally, exogenous cellulolytic enzymes are localized to the insect hindgut, while endogenous enzymes localized to the foregut, midgut and salivary glands.…”

Section: Role Of Cellulasesmentioning

confidence: 99%

“…Thus it has two independent cellulose-digesting systems: one in the midgut where cellulose digestion is accomplished by endogenous cellulases and the other in the hindgut which makes use of other cellulases possibly from symbiotic flagellates. However, the presence of a single unified cellulose digestion system, whereby endogenous and symbiotic cellulases work sequentially and collaboratively across the entire digestive tract of lower termite Reticulitermes flavipes (Kollar) was reported by Zhou et al (2007). The higher termites lack protozoan fauna but have abundant prokaryotic flora in the hindgut.…”

Section: Role Of Cellulasesmentioning

confidence: 99%

Insect cellulolytic enzymes: Novel sources for degradation of lignocellulosic biomass

Taggar

2015

JANS

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Alternative and renewable fuels derived from lignocellulosic biomass offer the potential to reduce our d ependence on fossil fuels and mitigate global climate change. Cellulose is one of the major structural components in all lignocellulosic wastes and enzymatic depolymerization of cellulose by cellulases is an essential step in bio-ethanol production. Wood-degrading insects are potential source of biochemical catalysts for converting wood lignocellulose into biofuels. Cellulose digestion has been demonstrated in more than 20 insect families representing ten distinct insect orders. Termite guts been have considered as the "world's smallest bioreactors" since they digest a significant proportion of cellulose (74-99%) and hemicellulose (65-87%) components of lignocelluloses they ingest. The lower termites harbor protistan symbionts in hindgut whereas higher termites lack these in the hind gut. Studies on cellulose digestion in termites and other insects with reference to ligno-cellulose degrading enzymes have been well focused in this review. The studies on insect cellulolytic systems can lead to the discovery of a variety of novel biocatalysts and genes that encode them, as well as associated unique mechanisms for efficient biomass conversion into biofuels.

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“…Termites efficiently degrade woody cellulose through a symbiotic collaboration with gut microorganisms, and they absorb the degradation products as nutrients (Nakashima et al, 2002;Watanabe et al, 1997;Zhou et al, 2007). In the first step of cellulose degradation, termites secrete an endo-β-1,4-glucanase from their salivary glands that enzymatically reduces the size of cellulose.…”

Section: Introduction 1)mentioning

confidence: 99%

A New α-Amylase from Reticulitermes speratus KMT1

Park¹,

Ham²,

Ahn

et al. 2014

Journal of the Korean Wood Science and Technology

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Termites are wood pests that cause vast economic damage every year. They digest both cellulose and starch, but the enzymes for starch digestion have not been well characterized. We obtained complete amino acid sequence information on the KME1 α-amylase from Reticulitermes speratus KMT1 through analysis of total mRNA sequences. The KME1 enzyme has two α-amylase domains and is 68% identical to the α-amylase from Blattellager manica, its closest relative in the GenBank database. Some unique features of its conserved region and its distant evolutionary relationship to other insect α-amylases suggest that KME1 is a new type of α-amylase.

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Correlation of cellulase gene expression and cellulolytic activity throughout the gut of the termite Reticulitermes flavipes

Cited by 105 publications

References 54 publications

Purification and characterisation of endo-β-1,4-glucanase and laminarinase enzymes from the gecarcinid land crab Gecarcoidea natalis and the aquatic crayfish Cherax destructor

Purification and characterisation of endo-β-1,4-glucanase and laminarinase enzymes from the gecarcinid land crab Gecarcoidea natalis and the aquatic crayfish Cherax destructor

Insect cellulolytic enzymes: Novel sources for degradation of lignocellulosic biomass

A New α-Amylase from Reticulitermes speratus KMT1

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