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- Title
Purification and anticancer activity of glutaminase and urease‐free l‐asparaginase from novel endophyte Chaetomium sp.
- Authors
Arumugam, Nagarajan; Shanmugam, Manoj Kumar; Thangavelu, Perarasu
- Abstract
l‐Asparaginase catalyzes the hydrolysis of asparagine into aspartic acid and ammonia. The present work elaborates the isolation and identification of a novel endophytic fungal isolate producing l‐glutaminase and urease‐free l‐asparaginase. Cell growth and enzyme production were investigated for large production. The isolated endophytic fungi were identified at molecular levels and a phylogenetic tree was constructed. The enzyme synthesis was evaluated by cultivating the isolated microorganisms in potato dextrose agar medium. Out of 27 isolated endophytes, nine were producing "l‐glutaminase and urease‐free l‐asparaginase." l‐Asparaginase from Chaetomium sp. exhibited superior enzyme activity than from the other isolates. Observed optimal conditions for l‐asparaginase activity were 25 min of incubation time, 0.5 mg of enzyme source, 40°C of temperature, and pH 7.0. l‐Asparaginase from Chaetomium sp. exhibited anticancer activity on human blood cancer (MOLT‐4) cells. The current study has demonstrated the production of contaminant‐free l‐asparaginase enzyme from endophytic fungal species. The results showed that: (a) maximum enzyme activity was observed for l‐asparaginase from Chaetomium sp., (b) concentration of glucose in the medium as a carbon source suppressed the enzyme production. Chaetomium sp. is a novel source for "l‐glutaminase and urease‐free l‐asparaginase," which may play a major role in pharmacotherapy.
- Subjects
CHAETOMIUM; TRANSGLUTAMINASES; ANTINEOPLASTIC agents; UREASE; FUNGAL enzymes; ENDOPHYTIC fungi; ASPARTIC acid; CELL growth
- Publication
Biotechnology & Applied Biochemistry, 2022, Vol 69, Issue 5, p2161
- ISSN
0885-4513
- Publication type
Article
- DOI
10.1002/bab.2276