Glyptotermes liangshanensis Gao, Zhu & Gong, 1982 凉山树白蚁

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1. Revalidation of the presence of Glyptotermes brevicaudatus (Haviland) and Glyptotermes caudomunitus Kemner in India (Isoptera: Kalotermitidae)

   Rituparna Sengupta, Keloth Rajmohana, Poovoli Amina, Jayati Basak, Balmohan Baraik · 2019 · Oriental Insects

   摘要

   The identities of Glyptotermes brevicaudatus (Haviland) and G. caudomunitus Kemner, reported from India were stated ‘doubtful’ in the recent World Catalogue of termites. This study by re-examining the voucher specimens of the two species at the National Zoological Collection, at Zoological Survey of India, Kolkata, and by reconfirming their identities, hereby revalidates their presence in India. The species are redescribed along with adequate images. An identification key to all the 12 species of Glyptotermes known from India is also provided.

2. Revision of Australian Glyptotermes Froggatt (Isoptera: Kalotermitidae)

   Robert H. Eldridge · 1996 · Australian Journal of Entomology

   摘要

   The Australian species of Glyptotermes Froggatt are revised and two new species, G. barretti and G. finniganensis, from Cape York Peninsula, Queensland, are described. The following new synonymy is proposed: G. eucalypti Froggatt (=G. neotuberculatus (Hill)). The revision was based on a morphometric analysis of all available full series collections of Glyptotermes spp. held in Australian institutions. In addition to the above, the Australian species include G. brevicornis Froggatt, G. iridipennis Froggatt and G. tuberculatus Froggatt. Keys to the alate and soldier castes of the six Australian species now included in Glyptotermes are provided.

3. Purification and some properties of endoglucanase from Glyptotermes xiamenensis

   Y. Shi, Yi-Ming Tao, Su-Juan Ma, G. An, Minnan Long, Qingxi Chen · 2009 · Journal of Applied Entomology

   摘要

   An endoglucanase (EGase) from Glyptotermes xiamenensis was purified by extraction with phosphate buffer solution and ammonium sulfate fractionation, and then chromatographed on DEAE Sepharose Fast Flow followed by Sephadex G‐100 columns. The purified enzyme was determined to be homogeneous by polyacrylamide gel electrophoresis (PAGE). Enzyme molecular weight was determined to be 44.8 kDa and the enzyme was a monomeric protein. The specific activity was determined to be 458.7 U/mg. The optimum pH and optimum temperature of the enzyme for the hydrolysis of carboxymethycellulose sodium (CMC‐Na) were investigated to be at pH 5.0 and at 40°C, respectively. The enzyme was stable over the pH range from 4.0 to 9.0 and at the temperature below 45°C. Kinetic behaviour of the enzyme in the hydrolysis of CMC‐Na followed Michaelis–Menten kinetics with constant (Km) of 7.2 mg/ml at pH 5.0 and 40°C. The activation energy was determined to be 49.3 KJ/mol. Chemical modification indicated that the residues of histidine, tryptophan and carboxylate were essential to the enzyme activity.

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