Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, Wuxi, Jiangsu, China.
Biotechnol Lett. 2013 May;35(5):751-6. doi: 10.1007/s10529-013-1140-7. Epub 2013 Jan 22.
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.
苯丙氨酸解氨酶（PAL）的工业化生产主要使用红酵母属的菌株。然而，红酵母属的 PAL 基因尚未被克隆。在此，我们从酿酒红酵母中分离出了全长的 PAL 基因。它有 2121 个碱基对，编码一个由 706 个氨基酸组成的多肽，计算分子量为 75.5 kDa。尽管酿酒红酵母是红酵母的无性型，但它们的 PAL 氨基酸序列并不相同（约 74%的同源性）。PAL 在大肠杆菌中表达并进行了表征。其比活为 4.2 U mg(-1)，k cat/K m 为 1.9×10(4) mM(-1) s(-1)，表现出了已报道的 PAL 中最高的催化能力。这里报道的遗传和生化信息应该有助于未来在工业中的应用。
