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HERO ID
1510769
Reference Type
Journal Article
Title
Cloning, expression and characterization of phenylalanine ammonia-lyase from Rhodotorula glutinis
Author(s)
Zhu, L; Cui, W; Fang, Y; Liu, Y; Gao, X; Zhou, Z
Year
2013
Is Peer Reviewed?
Yes
Journal
Biotechnology Letters
ISSN:
0141-5492
EISSN:
1573-6776
Volume
35
Issue
5
Page Numbers
751-756
Language
English
PMID
23338700
DOI
10.1007/s10529-013-1140-7
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.
Tags
IRIS
•
Ammonia
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