Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae)
Cellulose is the most abundant polymer in the biosphere, and termites are one of the most important metazoan cellulose processors. Termites are a rich source of digestive enzymes such as endo- β-1,4-glucanases, β-glucosidases, xylanases, amylases, pectinases, and laccases, regardless of whether they...
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Entomological Society of America
2014
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| Online Access: | http://psasir.upm.edu.my/id/eprint/34577/ |
| _version_ | 1848847812601577472 |
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| author | Bujang, Nurmastini Sufina Harrison, Nigel A. Su, Nan Yao |
| author_facet | Bujang, Nurmastini Sufina Harrison, Nigel A. Su, Nan Yao |
| author_sort | Bujang, Nurmastini Sufina |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Cellulose is the most abundant polymer in the biosphere, and termites are one of the most important metazoan cellulose processors. Termites are a rich source of digestive enzymes such as endo- β-1,4-glucanases, β-glucosidases, xylanases, amylases, pectinases, and laccases, regardless of whether they are termite derived or of microbiotic origin. Molecular identification of the termite's digestive enzyme is a critical initial step toward using termites as bioresources for industrial applications. Here, we report five β-glucosidase sequences obtained from four species of higher termites (Anoplotermes schwarzi Banks, Macrotermes carbonarius (Hagen), Rhynchotermes bulbinasus Scheffrahn, Sphaerotermes sphaerothorax (Sjoestedt)) with differing nutritional biologies. The deduced amino acid sequences indicated that they were most similar to β-glucosidases in the glycosyl hydrolase family 1 (GHF1). All complete coding sequences are 490 amino acids long and contain conserved motifs involved in substrate binding and catalysis. Each sequence was also predicted to be glycosylated at two sites. |
| first_indexed | 2025-11-15T09:24:33Z |
| format | Article |
| id | upm-34577 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T09:24:33Z |
| publishDate | 2014 |
| publisher | Entomological Society of America |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-345772015-12-16T02:04:42Z http://psasir.upm.edu.my/id/eprint/34577/ Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) Bujang, Nurmastini Sufina Harrison, Nigel A. Su, Nan Yao Cellulose is the most abundant polymer in the biosphere, and termites are one of the most important metazoan cellulose processors. Termites are a rich source of digestive enzymes such as endo- β-1,4-glucanases, β-glucosidases, xylanases, amylases, pectinases, and laccases, regardless of whether they are termite derived or of microbiotic origin. Molecular identification of the termite's digestive enzyme is a critical initial step toward using termites as bioresources for industrial applications. Here, we report five β-glucosidase sequences obtained from four species of higher termites (Anoplotermes schwarzi Banks, Macrotermes carbonarius (Hagen), Rhynchotermes bulbinasus Scheffrahn, Sphaerotermes sphaerothorax (Sjoestedt)) with differing nutritional biologies. The deduced amino acid sequences indicated that they were most similar to β-glucosidases in the glycosyl hydrolase family 1 (GHF1). All complete coding sequences are 490 amino acids long and contain conserved motifs involved in substrate binding and catalysis. Each sequence was also predicted to be glycosylated at two sites. Entomological Society of America 2014 Article PeerReviewed Bujang, Nurmastini Sufina and Harrison, Nigel A. and Su, Nan Yao (2014) Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae). Annals of the Entomological Society of America, 107 (1). pp. 251-256. ISSN 0013-8746; ESSN: 1938-2901 http://www.bioone.org/doi/abs/10.1603/AN13012 10.1603/AN13012 |
| spellingShingle | Bujang, Nurmastini Sufina Harrison, Nigel A. Su, Nan Yao Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) |
| title | Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) |
| title_full | Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) |
| title_fullStr | Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) |
| title_full_unstemmed | Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) |
| title_short | Molecular cloning of five β-glucosidases from four species of higher termites (Blattodea: termitidae) |
| title_sort | molecular cloning of five β-glucosidases from four species of higher termites (blattodea: termitidae) |
| url | http://psasir.upm.edu.my/id/eprint/34577/ http://psasir.upm.edu.my/id/eprint/34577/ http://psasir.upm.edu.my/id/eprint/34577/ |