| Cloning, expression and characterization of phenylalanine ammonia-lyase from Rhodotorula glutinis. | |
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MedLine Citation:
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PMID: 23338700 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The industrial-scale production of phenylalanine ammonia-lyase (PAL) mainly uses strains of Rhodotorula. However, the PAL gene from Rhodotorula has not been cloned. Here, the full-length gene of PAL from Rhodotorula glutinis was isolated. It was 2,121 bp, encoding a polypeptide with 706 amino acids and a calculated MW of 75.5 kDa. Though R. glutinis is an anamorph of Rhodosporium toruloides, the amino acid sequences of PALs them are not the same (about 74 % identity). PAL was expressed in E. coli and characterized. Its specific activity was 4.2 U mg(-1) and the k (cat)/K (m) was 1.9 × 10(4) mM(-1) s(-1), exhibiting the highest catalytic ability among the reported PALs. The genetic and biochemical information reported here should facilitate future application in industry. |
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Authors:
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Longbao Zhu; Wenjing Cui; Yueqin Fang; Yi Liu; Xinxing Gao; Zhemin Zhou |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-22 |
Journal Detail:
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Title: Biotechnology letters Volume: - ISSN: 1573-6776 ISO Abbreviation: Biotechnol. Lett. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8008051 Medline TA: Biotechnol Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, Wuxi, Jiangsu, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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