Cloning, expression and characterization of phenylalanine ammonia-lyase from Rhodotorula glutinis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-05

AUTHORS

Longbao Zhu, Wenjing Cui, Yueqin Fang, Yi Liu, Xinxing Gao, Zhemin Zhou

ABSTRACT

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. More... »

PAGES

751-756

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-013-1140-7

DOI

http://dx.doi.org/10.1007/s10529-013-1140-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027524582

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23338700


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