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Recombinant l-phenylalanine ammonia lyase from Rhodosporidium toruloides as a potential anticancer agent
The recombinant producer strain expressing Rhodosporidium toruloides l‐phenylalanine ammonia lyase (PAL) has been obtained, and a purification procedure of PAL has been developed. The purified enzyme, PAL, has the following biochemical and catalytic characteristics: Km for l‐Phe of 0.49 mM, pH optim...
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Published in: | Biotechnology and applied biochemistry 2013-05, Vol.60 (3), p.316-322 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The recombinant producer strain expressing Rhodosporidium toruloides l‐phenylalanine ammonia lyase (PAL) has been obtained, and a purification procedure of PAL has been developed. The purified enzyme, PAL, has the following biochemical and catalytic characteristics: Km for l‐Phe of 0.49 mM, pH optimum at 8.5, and temperature optimum at 50°C. PAL exhibited a significant cytotoxic effect toward the following cell lines: MCF7 (IC50 = 1.97 U/mL), DU145 (IC50 = 7.3 U/mL), which are comparable with E. coli l‐asparaginase type‐II cytotoxicity in vitro. Administration of PAL (200–400 U/kg) to L5178y‐bearing mice for five times (a total dose of 1000–2000 U/kg) was well tolerated and showed the increase of life span (ILS) = 12–16%, P < 0.05. Data obtained suggest that PAL from R. toruloides has a potential for cancer treatment. |
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ISSN: | 0885-4513 1470-8744 |
DOI: | 10.1002/bab.1089 |