Kajiyama N, Nakano E
Research and Development Division, Kikkoman Corporation, Chiba, Japan.
Biosci Biotechnol Biochem. 1994 Jun;58(6):1170-1. doi: 10.1271/bbb.58.1170.
We constructed firefly luciferase mutants from Luciola lateralis in which Ala at position 217 was replaced by each of three hydrophobic amino acid residues (Ile, Leu, and Val). These mutants were superior to the wild-type in thermostability. Especially, the purified Ala217Leu mutant still maintained over 70% of the initial activity after 60 min at 50 degrees C. This mutant is the most thermostable firefly luciferase obtained.
我们构建了来自日本扁萤的萤火虫荧光素酶突变体，其中第217位的丙氨酸被三种疏水氨基酸残基（异亮氨酸、亮氨酸和缬氨酸）中的每一种取代。这些突变体在热稳定性方面优于野生型。特别是，纯化后的Ala217Leu突变体在50摄氏度下60分钟后仍保持超过70%的初始活性。该突变体是已获得的最具热稳定性的萤火虫荧光素酶。
