Cellulose Digestion in the Wood-Eating Higher Termite, Nasutitermes takasagoensis (Shiraki): Distribution of Cellulases and Properties of Endo-β-1,4-gIucanase

  title={Cellulose Digestion in the Wood-Eating Higher Termite, Nasutitermes takasagoensis (Shiraki): Distribution of Cellulases and Properties of Endo-$\beta$-1,4-gIucanase},
  author={Gaku Tokuda and Hirofumi Watanabe and Tadao Matsumoto and Hiroaki Noda},
  booktitle={Zoological science},
Abstract β-Giucosidase ‘EC’ and endo-β-1,4-gIucanase ‘EC’ activities were measured in the wood-eating higher termite Nasutitermes takasagoensis. β-Glucosidase activity was present mainly in the salivary glands (66.7%) and midgut (22.2%), whereas endo-β-1,4-glucanase activity was detected mainly in the midgut (90.1%). Specific activity of endo-β-1,4-glucanase was also the highest in the midgut, indicating that cellulose is digested in the midgut. The major endo-β-1,4-glucanase… 

Distribution and Properties of Endo-β-1,4-glucanase from a Lower Termite, Coptotermes formosanus (Shiraki)

A multi-enzyme distribution of endo-β-1,4-glucanase activity was found in the digestive system of a worker caste of the lower termite Coptotermes formosanus (Shiraki) by zymogram analysis. Its

Cellulolytic environment in the midgut of the wood-feeding higher termite Nasutitermes takasagoensis.

Evaluation of Cellulolytic Endo-1,4-β-D-Glucanase Activity in the Digestive Fluid of Adult Phytophagous Beetle Hoplasoma unicolor

The qualitative and quantitative analysis of cellulolytic activity in the digestive fluid of H. unicolor highlights prospect of the gut fluid of this insect as an important source of cellulase enzymes that merits further investigations into their extensive characterisation for potential industrial applications.

Purification of β-glucosidase from the salivary glands of the green rice leafhopper, Nephotettix cincticeps (Uhler) (Hemiptera: Cicadellidae), and its detection in the salivary sheath

The green rice leafhopper, Nephotettix cincticeps, is an insect pest of rice and discharges β-glucosidase, which may be involved in the hydrolysis of a phenol glucoside present in the saliva, which is a step in the solidification of gelling saliva to form salivary sheaths.

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

Laminarinase and endo-β-1,4-glucanase were purified and characterised from the midgut gland of the herbivorous land crab Gecarcoidea natalis and the crayfish Cherax destructor and produced glucose and other short oligomers from the hydrolysis of laminarin.

Distribution and Properties of EndovB-1 , 4-glucanase Coptotermes formosanus ( Shiraki ) from a Lower Termite ,

Preliminary results indicate an eperation of collaboration of termite and protozoa in degradation of cellulose, and an identification of the termite origin of cellulase was established in R. speratus.

Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes

SUMMARY Digestive juice from the herbivorous gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes exhibited total cellulase activity and activities of two cellulase enzymes;

Heterologous expression and enzymatic characterization of β-glucosidase from the drywood-eating termite, Neotermes koshunensis

A β-glucosidase cDNA from the termite, Neotermes koshunensis, was successfully overexpressed in Escherichia coli, and the product was purified to homogeneity by affinity purification against



Purification and characterization of an endoglucanase (1,4-beta-D-glucan glucanohydrolase) from Clostridium thermocellum.

An endoglucanase was purified from Clostridium thermocellum by procedures that included centrifugation, ultrafiltration, selective precipitation, ion-exchange Sephadex chromatography and preparative gel electrophoresis, and behaved as a homogeneous protein under non-denaturing conditions.

Enzymatic studies on a cellulase system of Trichoderma viride. II. Purification and Properties of two cellulases.

  • G. Okada
  • Biology, Chemistry
    Journal of biochemistry
  • 1975
Two cellulase components derived from Meicelase, a commercial crude cellulase preparation from Trichoderma viride, were purified by consecutive column chromatography, and were designated as cellulases II-A and cellulase II-B, which retained 27 and 41% of the original CM-cellulose-saccharifying activities after heating at 100 degrees for 10 min.

The Distribution and Origins of the Cellulolytic Enzymes of the Higher Termite, Macrotermes natalensis

It is proposed that a strategy of resource utilization based upon the acquisition of digestive enzymes which expand the range of natural substrates suitable for exploitation as nutrient sources may be a general one.